-
Notifications
You must be signed in to change notification settings - Fork 9
/
4G6K.pdb
7601 lines (7601 loc) · 601 KB
/
4G6K.pdb
1
2
3
4
5
6
7
8
9
10
11
12
13
14
15
16
17
18
19
20
21
22
23
24
25
26
27
28
29
30
31
32
33
34
35
36
37
38
39
40
41
42
43
44
45
46
47
48
49
50
51
52
53
54
55
56
57
58
59
60
61
62
63
64
65
66
67
68
69
70
71
72
73
74
75
76
77
78
79
80
81
82
83
84
85
86
87
88
89
90
91
92
93
94
95
96
97
98
99
100
101
102
103
104
105
106
107
108
109
110
111
112
113
114
115
116
117
118
119
120
121
122
123
124
125
126
127
128
129
130
131
132
133
134
135
136
137
138
139
140
141
142
143
144
145
146
147
148
149
150
151
152
153
154
155
156
157
158
159
160
161
162
163
164
165
166
167
168
169
170
171
172
173
174
175
176
177
178
179
180
181
182
183
184
185
186
187
188
189
190
191
192
193
194
195
196
197
198
199
200
201
202
203
204
205
206
207
208
209
210
211
212
213
214
215
216
217
218
219
220
221
222
223
224
225
226
227
228
229
230
231
232
233
234
235
236
237
238
239
240
241
242
243
244
245
246
247
248
249
250
251
252
253
254
255
256
257
258
259
260
261
262
263
264
265
266
267
268
269
270
271
272
273
274
275
276
277
278
279
280
281
282
283
284
285
286
287
288
289
290
291
292
293
294
295
296
297
298
299
300
301
302
303
304
305
306
307
308
309
310
311
312
313
314
315
316
317
318
319
320
321
322
323
324
325
326
327
328
329
330
331
332
333
334
335
336
337
338
339
340
341
342
343
344
345
346
347
348
349
350
351
352
353
354
355
356
357
358
359
360
361
362
363
364
365
366
367
368
369
370
371
372
373
374
375
376
377
378
379
380
381
382
383
384
385
386
387
388
389
390
391
392
393
394
395
396
397
398
399
400
401
402
403
404
405
406
407
408
409
410
411
412
413
414
415
416
417
418
419
420
421
422
423
424
425
426
427
428
429
430
431
432
433
434
435
436
437
438
439
440
441
442
443
444
445
446
447
448
449
450
451
452
453
454
455
456
457
458
459
460
461
462
463
464
465
466
467
468
469
470
471
472
473
474
475
476
477
478
479
480
481
482
483
484
485
486
487
488
489
490
491
492
493
494
495
496
497
498
499
500
501
502
503
504
505
506
507
508
509
510
511
512
513
514
515
516
517
518
519
520
521
522
523
524
525
526
527
528
529
530
531
532
533
534
535
536
537
538
539
540
541
542
543
544
545
546
547
548
549
550
551
552
553
554
555
556
557
558
559
560
561
562
563
564
565
566
567
568
569
570
571
572
573
574
575
576
577
578
579
580
581
582
583
584
585
586
587
588
589
590
591
592
593
594
595
596
597
598
599
600
601
602
603
604
605
606
607
608
609
610
611
612
613
614
615
616
617
618
619
620
621
622
623
624
625
626
627
628
629
630
631
632
633
634
635
636
637
638
639
640
641
642
643
644
645
646
647
648
649
650
651
652
653
654
655
656
657
658
659
660
661
662
663
664
665
666
667
668
669
670
671
672
673
674
675
676
677
678
679
680
681
682
683
684
685
686
687
688
689
690
691
692
693
694
695
696
697
698
699
700
701
702
703
704
705
706
707
708
709
710
711
712
713
714
715
716
717
718
719
720
721
722
723
724
725
726
727
728
729
730
731
732
733
734
735
736
737
738
739
740
741
742
743
744
745
746
747
748
749
750
751
752
753
754
755
756
757
758
759
760
761
762
763
764
765
766
767
768
769
770
771
772
773
774
775
776
777
778
779
780
781
782
783
784
785
786
787
788
789
790
791
792
793
794
795
796
797
798
799
800
801
802
803
804
805
806
807
808
809
810
811
812
813
814
815
816
817
818
819
820
821
822
823
824
825
826
827
828
829
830
831
832
833
834
835
836
837
838
839
840
841
842
843
844
845
846
847
848
849
850
851
852
853
854
855
856
857
858
859
860
861
862
863
864
865
866
867
868
869
870
871
872
873
874
875
876
877
878
879
880
881
882
883
884
885
886
887
888
889
890
891
892
893
894
895
896
897
898
899
900
901
902
903
904
905
906
907
908
909
910
911
912
913
914
915
916
917
918
919
920
921
922
923
924
925
926
927
928
929
930
931
932
933
934
935
936
937
938
939
940
941
942
943
944
945
946
947
948
949
950
951
952
953
954
955
956
957
958
959
960
961
962
963
964
965
966
967
968
969
970
971
972
973
974
975
976
977
978
979
980
981
982
983
984
985
986
987
988
989
990
991
992
993
994
995
996
997
998
999
1000
HEADER IMMUNE SYSTEM 19-JUL-12 4G6K
TITLE CRYSTAL STRUCTURE OF THE THERAPEUTIC ANTIBODY BINDING FRAGMENT OF
TITLE 2 GEVOKIZUMAB IN ITS UNBOUND STATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEAVY CHAIN OF GEVOKIZUMAB ANTIBODY BINDING FRAGMENT;
COMPND 3 CHAIN: H;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: LIGHT CHAIN OF GEVOKIZUMAB ANTIBODY BINDING FRAGMENT;
COMPND 7 CHAIN: L;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HUMAN, MOUSE;
SOURCE 4 ORGANISM_TAXID: 9606, 10090;
SOURCE 5 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE 7 EXPRESSION_SYSTEM_CELL_LINE: CHO;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS, MUS MUSCULUS;
SOURCE 10 ORGANISM_COMMON: HUMAN, MOUSE;
SOURCE 11 ORGANISM_TAXID: 9606, 10090;
SOURCE 12 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 13 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE 14 EXPRESSION_SYSTEM_CELL_LINE: CHO
KEYWDS IMMUNOGLOBULIN FOLD, IMMUNE SYSTEM, CYTOKINE, INTERLEUKINE-1BETA
EXPDTA X-RAY DIFFRACTION
AUTHOR M.BLECH,S.HOERER
REVDAT 3 05-FEB-14 4G6K 1 SOURCE
REVDAT 2 17-JUL-13 4G6K 1 JRNL
REVDAT 1 19-DEC-12 4G6K 0
JRNL AUTH M.BLECH,D.PETER,P.FISCHER,M.M.BAUER,M.HAFNER,M.ZEEB,H.NAR
JRNL TITL ONE TARGET-TWO DIFFERENT BINDING MODES: STRUCTURAL INSIGHTS
JRNL TITL 2 INTO GEVOKIZUMAB AND CANAKINUMAB INTERACTIONS TO
JRNL TITL 3 INTERLEUKIN-1BETA
JRNL REF J.MOL.BIOL. V. 425 94 2013
JRNL REFN ISSN 0022-2836
JRNL PMID 23041424
JRNL DOI 10.1016/J.JMB.2012.09.021
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.2
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.75
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 39868
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.184
REMARK 3 R VALUE (WORKING SET) : 0.183
REMARK 3 FREE R VALUE : 0.211
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030
REMARK 3 FREE R VALUE TEST SET COUNT : 2007
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 1.95
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.98
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2900
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.1999
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2761
REMARK 3 BIN R VALUE (WORKING SET) : 0.1991
REMARK 3 BIN FREE R VALUE : 0.2164
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.79
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 139
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3291
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 510
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.43
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.32
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.21880
REMARK 3 B22 (A**2) : 1.02030
REMARK 3 B33 (A**2) : -2.23910
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.212
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.136
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.946
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.933
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 3373 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 4593 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1117 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 68 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 488 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 3373 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 451 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 4052 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.03
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.97
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 15.56
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { H|1 - H|220 }
REMARK 3 ORIGIN FOR THE GROUP (A): 45.6293 17.2370 -27.8362
REMARK 3 T TENSOR
REMARK 3 T11: -0.0499 T22: -0.0407
REMARK 3 T33: -0.0059 T12: -0.0095
REMARK 3 T13: -0.0100 T23: -0.0052
REMARK 3 L TENSOR
REMARK 3 L11: 0.8231 L22: 0.4988
REMARK 3 L33: 0.9988 L12: 0.0107
REMARK 3 L13: -0.7358 L23: -0.1606
REMARK 3 S TENSOR
REMARK 3 S11: 0.0140 S12: -0.0866 S13: 0.0146
REMARK 3 S21: 0.0178 S22: 0.0074 S23: 0.0331
REMARK 3 S31: -0.0080 S32: 0.1013 S33: -0.0214
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { L|1 - L|212 }
REMARK 3 ORIGIN FOR THE GROUP (A): 35.8266 32.1798 -26.6382
REMARK 3 T TENSOR
REMARK 3 T11: -0.0538 T22: -0.0839
REMARK 3 T33: -0.0347 T12: -0.0113
REMARK 3 T13: -0.0067 T23: -0.0376
REMARK 3 L TENSOR
REMARK 3 L11: 1.0443 L22: 0.8369
REMARK 3 L33: 0.5782 L12: -0.1417
REMARK 3 L13: -0.4451 L23: 0.1136
REMARK 3 S TENSOR
REMARK 3 S11: 0.0234 S12: -0.1101 S13: 0.2068
REMARK 3 S21: 0.1252 S22: 0.0191 S23: -0.0396
REMARK 3 S31: -0.0607 S32: 0.0632 S33: -0.0425
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4G6K COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-JUL-12.
REMARK 100 THE RCSB ID CODE IS RCSB073801.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-NOV-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS, AUTOPROC
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 41364
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 57.400
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 6.500
REMARK 200 R MERGE (I) : 0.07600
REMARK 200 R SYM (I) : 0.08400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 1PZ5 AND 3BKJ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.59
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.65
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 14.3% W/V PEG 3350 AND 0.14M TRI-
REMARK 280 SODIUM CITRATE AT PH 5.0 EQUILIBRATED AGAINST 24% W/V PEG 3350,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 37.17250
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 44.43100
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.54600
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 44.43100
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 37.17250
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 37.54600
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3520 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19590 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 475
REMARK 475 ZERO OCCUPANCY RESIDUES
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)
REMARK 475 M RES C SSEQI
REMARK 475 SER H 135
REMARK 475 LYS H 136
REMARK 475 SER H 139
REMARK 475 GLY H 140
REMARK 475 GLY L 212
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 GLY H 57 C
REMARK 480 LYS H 66 CD CE NZ
REMARK 480 LYS H 77 CD CE NZ
REMARK 480 LYS H 83 CG CD CE NZ
REMARK 480 SER H 137 N CA C O
REMARK 480 THR H 138 N CA C O
REMARK 480 GLN L 3 CD OE1 NE2
REMARK 480 LYS L 53 CD CE NZ
REMARK 480 LYS L 145 CG CD CE NZ
REMARK 480 LYS L 190 CG CD CE NZ
REMARK 480 ASN L 210 N CA C O
REMARK 480 ARG L 211 N CA C O
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 SER H 15 -14.94 82.24
REMARK 500 LEU H 50 -61.17 -108.15
REMARK 500 TYR H 102 166.55 78.05
REMARK 500 PHE H 107 84.51 -68.70
REMARK 500 THR H 138 97.50 -177.73
REMARK 500 ASP H 151 65.47 61.87
REMARK 500 THR H 198 -23.60 -141.71
REMARK 500 THR L 51 -51.98 69.13
REMARK 500 ASN L 138 74.31 49.90
REMARK 500 ASN L 152 -2.44 69.12
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 LEU H 196 21.5 L L OUTSIDE RANGE
REMARK 500 ILE L 29 24.1 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH H 531 DISTANCE = 5.02 ANGSTROMS
REMARK 525 HOH H 540 DISTANCE = 7.69 ANGSTROMS
REMARK 525 HOH H 551 DISTANCE = 7.16 ANGSTROMS
REMARK 525 HOH L 401 DISTANCE = 10.63 ANGSTROMS
REMARK 525 HOH L 492 DISTANCE = 16.17 ANGSTROMS
REMARK 525 HOH L 503 DISTANCE = 5.20 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4G6J RELATED DB: PDB
REMARK 900 RELATED ID: 4G6M RELATED DB: PDB
REMARK 900 RELATED ID: 4G5Z RELATED DB: PDB
DBREF 4G6K H 1 220 PDB 4G6K 4G6K 1 220
DBREF 4G6K L 1 212 PDB 4G6K 4G6K 1 212
SEQRES 1 H 220 GLN VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL LYS
SEQRES 2 H 220 PRO SER GLN THR LEU SER LEU THR CYS SER PHE SER GLY
SEQRES 3 H 220 PHE SER LEU SER THR SER GLY MET GLY VAL GLY TRP ILE
SEQRES 4 H 220 ARG GLN PRO SER GLY LYS GLY LEU GLU TRP LEU ALA HIS
SEQRES 5 H 220 ILE TRP TRP ASP GLY ASP GLU SER TYR ASN PRO SER LEU
SEQRES 6 H 220 LYS SER ARG LEU THR ILE SER LYS ASP THR SER LYS ASN
SEQRES 7 H 220 GLN VAL SER LEU LYS ILE THR SER VAL THR ALA ALA ASP
SEQRES 8 H 220 THR ALA VAL TYR PHE CYS ALA ARG ASN ARG TYR ASP PRO
SEQRES 9 H 220 PRO TRP PHE VAL ASP TRP GLY GLN GLY THR LEU VAL THR
SEQRES 10 H 220 VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO
SEQRES 11 H 220 LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA
SEQRES 12 H 220 ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO
SEQRES 13 H 220 VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY
SEQRES 14 H 220 VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU
SEQRES 15 H 220 TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SER
SEQRES 16 H 220 LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS
SEQRES 17 H 220 PRO SER ASN THR LYS VAL ASP LYS ARG VAL GLU PRO
SEQRES 1 L 212 ASP ILE GLN MET THR GLN SER THR SER SER LEU SER ALA
SEQRES 2 L 212 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER
SEQRES 3 L 212 GLN ASP ILE SER ASN TYR LEU SER TRP TYR GLN GLN LYS
SEQRES 4 L 212 PRO GLY LYS ALA VAL LYS LEU LEU ILE TYR TYR THR SER
SEQRES 5 L 212 LYS LEU HIS SER GLY VAL PRO SER ARG PHE SER GLY SER
SEQRES 6 L 212 GLY SER GLY THR ASP TYR THR LEU THR ILE SER SER LEU
SEQRES 7 L 212 GLN GLN GLU ASP PHE ALA THR TYR PHE CYS LEU GLN GLY
SEQRES 8 L 212 LYS MET LEU PRO TRP THR PHE GLY GLN GLY THR LYS LEU
SEQRES 9 L 212 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE
SEQRES 10 L 212 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA
SEQRES 11 L 212 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU
SEQRES 12 L 212 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER
SEQRES 13 L 212 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS
SEQRES 14 L 212 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER
SEQRES 15 L 212 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU
SEQRES 16 L 212 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER
SEQRES 17 L 212 PHE ASN ARG GLY
FORMUL 3 HOH *510(H2 O)
HELIX 1 1 PRO H 63 LYS H 66 5 4
HELIX 2 2 THR H 75 LYS H 77 5 3
HELIX 3 3 THR H 88 THR H 92 5 5
HELIX 4 4 SER H 163 ALA H 165 5 3
HELIX 5 5 SER H 194 LEU H 196 5 3
HELIX 6 6 GLN L 79 PHE L 83 5 5
HELIX 7 7 SER L 121 LYS L 126 1 6
HELIX 8 8 LYS L 183 HIS L 189 1 7
SHEET 1 A 4 GLN H 3 SER H 7 0
SHEET 2 A 4 LEU H 18 SER H 25 -1 O SER H 23 N GLN H 5
SHEET 3 A 4 GLN H 79 ILE H 84 -1 O ILE H 84 N LEU H 18
SHEET 4 A 4 LEU H 69 ASP H 74 -1 N ASP H 74 O GLN H 79
SHEET 1 B 6 LEU H 11 VAL H 12 0
SHEET 2 B 6 THR H 114 VAL H 118 1 O THR H 117 N VAL H 12
SHEET 3 B 6 ALA H 93 ARG H 101 -1 N TYR H 95 O THR H 114
SHEET 4 B 6 MET H 34 GLN H 41 -1 N ILE H 39 O PHE H 96
SHEET 5 B 6 GLU H 48 TRP H 54 -1 O LEU H 50 N TRP H 38
SHEET 6 B 6 GLU H 59 TYR H 61 -1 O SER H 60 N HIS H 52
SHEET 1 C 4 LEU H 11 VAL H 12 0
SHEET 2 C 4 THR H 114 VAL H 118 1 O THR H 117 N VAL H 12
SHEET 3 C 4 ALA H 93 ARG H 101 -1 N TYR H 95 O THR H 114
SHEET 4 C 4 ASP H 109 TRP H 110 -1 O ASP H 109 N ARG H 99
SHEET 1 D 4 SER H 127 LEU H 131 0
SHEET 2 D 4 THR H 142 TYR H 152 -1 O GLY H 146 N LEU H 131
SHEET 3 D 4 TYR H 183 PRO H 192 -1 O LEU H 185 N VAL H 149
SHEET 4 D 4 VAL H 170 THR H 172 -1 N HIS H 171 O VAL H 188
SHEET 1 E 4 SER H 127 LEU H 131 0
SHEET 2 E 4 THR H 142 TYR H 152 -1 O GLY H 146 N LEU H 131
SHEET 3 E 4 TYR H 183 PRO H 192 -1 O LEU H 185 N VAL H 149
SHEET 4 E 4 VAL H 176 LEU H 177 -1 N VAL H 176 O SER H 184
SHEET 1 F 3 THR H 158 TRP H 161 0
SHEET 2 F 3 ILE H 202 HIS H 207 -1 O ASN H 206 N THR H 158
SHEET 3 F 3 THR H 212 ARG H 217 -1 O VAL H 214 N VAL H 205
SHEET 1 G 4 MET L 4 THR L 5 0
SHEET 2 G 4 VAL L 19 ALA L 25 -1 O ARG L 24 N THR L 5
SHEET 3 G 4 ASP L 70 ILE L 75 -1 O LEU L 73 N ILE L 21
SHEET 4 G 4 PHE L 62 SER L 67 -1 N SER L 63 O THR L 74
SHEET 1 H 6 SER L 10 SER L 14 0
SHEET 2 H 6 THR L 102 LYS L 107 1 O LYS L 107 N ALA L 13
SHEET 3 H 6 ALA L 84 GLN L 90 -1 N ALA L 84 O LEU L 104
SHEET 4 H 6 LEU L 33 GLN L 38 -1 N GLN L 38 O THR L 85
SHEET 5 H 6 LYS L 45 TYR L 49 -1 O ILE L 48 N TRP L 35
SHEET 6 H 6 LYS L 53 LEU L 54 -1 O LYS L 53 N TYR L 49
SHEET 1 I 4 SER L 10 SER L 14 0
SHEET 2 I 4 THR L 102 LYS L 107 1 O LYS L 107 N ALA L 13
SHEET 3 I 4 ALA L 84 GLN L 90 -1 N ALA L 84 O LEU L 104
SHEET 4 I 4 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90
SHEET 1 J 4 SER L 114 PHE L 118 0
SHEET 2 J 4 THR L 129 PHE L 139 -1 O ASN L 137 N SER L 114
SHEET 3 J 4 TYR L 173 SER L 182 -1 O LEU L 175 N LEU L 136
SHEET 4 J 4 SER L 159 VAL L 163 -1 N SER L 162 O SER L 176
SHEET 1 K 4 ALA L 153 LEU L 154 0
SHEET 2 K 4 LYS L 145 VAL L 150 -1 N VAL L 150 O ALA L 153
SHEET 3 K 4 VAL L 191 THR L 197 -1 O GLU L 195 N GLN L 147
SHEET 4 K 4 VAL L 205 ASN L 210 -1 O VAL L 205 N VAL L 196
SSBOND 1 CYS H 22 CYS H 97 1555 1555 2.05
SSBOND 2 CYS H 147 CYS H 203 1555 1555 2.03
SSBOND 3 CYS L 23 CYS L 88 1555 1555 2.05
SSBOND 4 CYS L 134 CYS L 194 1555 1555 2.03
CISPEP 1 ASP H 103 PRO H 104 0 1.45
CISPEP 2 PHE H 153 PRO H 154 0 -4.66
CISPEP 3 GLU H 155 PRO H 156 0 3.74
CISPEP 4 LEU H 196 GLY H 197 0 4.95
CISPEP 5 LEU L 94 PRO L 95 0 -0.40
CISPEP 6 TYR L 140 PRO L 141 0 0.29
CRYST1 74.345 75.092 88.862 90.00 90.00 90.00 P 21 21 21 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.013451 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013317 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011253 0.00000
ATOM 1 N GLN H 1 37.767 11.746 -46.439 1.00 35.99 N
ANISOU 1 N GLN H 1 4405 4781 4488 -408 -390 -200 N
ATOM 2 CA GLN H 1 38.455 10.490 -46.737 1.00 35.32 C
ANISOU 2 CA GLN H 1 4385 4643 4393 -454 -353 -265 C
ATOM 3 C GLN H 1 39.827 10.457 -46.060 1.00 35.35 C
ANISOU 3 C GLN H 1 4439 4550 4442 -405 -302 -252 C
ATOM 4 O GLN H 1 40.143 9.494 -45.357 1.00 35.61 O
ANISOU 4 O GLN H 1 4505 4514 4511 -420 -261 -280 O
ATOM 5 CB GLN H 1 38.602 10.284 -48.258 1.00 37.73 C
ANISOU 5 CB GLN H 1 4712 5005 4618 -489 -369 -296 C
ATOM 6 CG GLN H 1 37.283 10.067 -49.005 1.00 56.55 C
ANISOU 6 CG GLN H 1 7047 7497 6943 -555 -419 -322 C
ATOM 7 CD GLN H 1 36.620 11.342 -49.491 1.00 77.62 C
ANISOU 7 CD GLN H 1 9646 10270 9575 -511 -474 -255 C
ATOM 8 OE1 GLN H 1 36.978 12.468 -49.114 1.00 72.75 O
ANISOU 8 OE1 GLN H 1 9016 9636 8989 -431 -472 -186 O
ATOM 9 NE2 GLN H 1 35.615 11.185 -50.336 1.00 70.83 N
ANISOU 9 NE2 GLN H 1 8739 9524 8647 -563 -522 -273 N
ATOM 10 N VAL H 2 40.624 11.521 -46.256 1.00 28.01 N
ANISOU 10 N VAL H 2 3511 3622 3510 -344 -304 -207 N
ATOM 11 CA VAL H 2 41.973 11.675 -45.706 1.00 25.56 C
ANISOU 11 CA VAL H 2 3234 3241 3235 -297 -263 -190 C
ATOM 12 C VAL H 2 41.935 11.908 -44.189 1.00 25.78 C
ANISOU 12 C VAL H 2 3241 3230 3326 -270 -251 -165 C
ATOM 13 O VAL H 2 41.147 12.722 -43.700 1.00 24.19 O
ANISOU 13 O VAL H 2 2995 3057 3141 -255 -276 -134 O
ATOM 14 CB VAL H 2 42.757 12.788 -46.471 1.00 28.91 C
ANISOU 14 CB VAL H 2 3664 3686 3635 -253 -267 -154 C
ATOM 15 CG1 VAL H 2 44.065 13.156 -45.773 1.00 27.84 C
ANISOU 15 CG1 VAL H 2 3546 3492 3540 -207 -231 -133 C
ATOM 16 CG2 VAL H 2 43.021 12.377 -47.920 1.00 29.30 C
ANISOU 16 CG2 VAL H 2 3747 3765 3619 -278 -268 -183 C
ATOM 17 N GLN H 3 42.799 11.190 -43.455 1.00 21.09 N
ANISOU 17 N GLN H 3 2679 2573 2763 -259 -210 -177 N
ATOM 18 CA GLN H 3 42.936 11.324 -42.007 1.00 20.06 C
ANISOU 18 CA GLN H 3 2532 2408 2681 -231 -195 -154 C
ATOM 19 C GLN H 3 44.403 11.479 -41.630 1.00 21.49 C
ANISOU 19 C GLN H 3 2732 2556 2876 -189 -164 -138 C
ATOM 20 O GLN H 3 45.245 10.776 -42.176 1.00 20.63 O
ANISOU 20 O GLN H 3 2661 2424 2754 -188 -135 -154 O
ATOM 21 CB GLN H 3 42.325 10.118 -41.267 1.00 21.63 C
ANISOU 21 CB GLN H 3 2739 2574 2905 -262 -174 -180 C
ATOM 22 CG GLN H 3 40.798 10.076 -41.313 1.00 39.37 C
ANISOU 22 CG GLN H 3 4950 4860 5149 -305 -205 -191 C
ATOM 23 CD GLN H 3 40.217 9.003 -40.426 1.00 62.58 C
ANISOU 23 CD GLN H 3 7896 7761 8121 -333 -177 -212 C
ATOM 24 OE1 GLN H 3 40.513 7.811 -40.563 1.00 57.73 O
ANISOU 24 OE1 GLN H 3 7325 7102 7508 -359 -136 -246 O
ATOM 25 NE2 GLN H 3 39.342 9.402 -39.514 1.00 57.54 N
ANISOU 25 NE2 GLN H 3 7217 7136 7512 -329 -192 -190 N
ATOM 26 N LEU H 4 44.703 12.406 -40.707 1.00 16.90 N
ANISOU 26 N LEU H 4 2125 1977 2321 -157 -168 -107 N
ATOM 27 CA LEU H 4 46.048 12.640 -40.176 1.00 16.62 C
ANISOU 27 CA LEU H 4 2093 1924 2297 -123 -144 -91 C
ATOM 28 C LEU H 4 45.946 12.666 -38.662 1.00 19.34 C
ANISOU 28 C LEU H 4 2416 2261 2672 -110 -138 -78 C
ATOM 29 O LEU H 4 44.996 13.238 -38.119 1.00 18.17 O
ANISOU 29 O LEU H 4 2243 2123 2536 -118 -157 -71 O
ATOM 30 CB LEU H 4 46.661 13.968 -40.668 1.00 16.75 C
ANISOU 30 CB LEU H 4 2099 1962 2305 -106 -151 -73 C
ATOM 31 CG LEU H 4 46.976 14.067 -42.150 1.00 22.25 C
ANISOU 31 CG LEU H 4 2818 2670 2966 -110 -152 -79 C
ATOM 32 CD1 LEU H 4 45.887 14.812 -42.863 1.00 23.25 C
ANISOU 32 CD1 LEU H 4 2931 2830 3074 -120 -182 -69 C
ATOM 33 CD2 LEU H 4 48.283 14.795 -42.378 1.00 25.09 C
ANISOU 33 CD2 LEU H 4 3180 3028 3326 -86 -131 -64 C
ATOM 34 N GLN H 5 46.928 12.065 -37.981 1.00 15.56 N
ANISOU 34 N GLN H 5 1943 1767 2200 -87 -110 -71 N
ATOM 35 CA GLN H 5 46.946 12.026 -36.523 1.00 14.64 C
ANISOU 35 CA GLN H 5 1807 1653 2103 -72 -104 -56 C
ATOM 36 C GLN H 5 48.351 12.190 -35.997 1.00 17.00 C
ANISOU 36 C GLN H 5 2092 1969 2397 -42 -88 -39 C
ATOM 37 O GLN H 5 49.248 11.417 -36.343 1.00 16.47 O
ANISOU 37 O GLN H 5 2041 1895 2324 -21 -62 -33 O
ATOM 38 CB GLN H 5 46.284 10.733 -35.985 1.00 16.13 C
ANISOU 38 CB GLN H 5 2012 1812 2306 -77 -83 -60 C
ATOM 39 CG GLN H 5 46.223 10.641 -34.448 1.00 24.09 C
ANISOU 39 CG GLN H 5 3000 2825 3328 -57 -75 -39 C
ATOM 40 CD GLN H 5 45.436 11.771 -33.821 1.00 39.31 C
ANISOU 40 CD GLN H 5 4898 4773 5263 -69 -103 -38 C
ATOM 41 OE1 GLN H 5 44.244 11.955 -34.088 1.00 34.84 O
ANISOU 41 OE1 GLN H 5 4329 4203 4707 -94 -118 -48 O
ATOM 42 NE2 GLN H 5 46.098 12.581 -33.003 1.00 29.04 N
ANISOU 42 NE2 GLN H 5 3576 3501 3957 -54 -106 -27 N
ATOM 43 N GLU H 6 48.532 13.202 -35.155 1.00 13.22 N
ANISOU 43 N GLU H 6 1583 1518 1920 -41 -101 -32 N
ATOM 44 CA GLU H 6 49.804 13.499 -34.510 1.00 12.84 C
ANISOU 44 CA GLU H 6 1510 1506 1863 -23 -93 -20 C
ATOM 45 C GLU H 6 49.887 12.720 -33.205 1.00 17.96 C
ANISOU 45 C GLU H 6 2146 2168 2511 0 -82 -1 C
ATOM 46 O GLU H 6 48.873 12.520 -32.538 1.00 17.94 O
ANISOU 46 O GLU H 6 2147 2150 2518 -7 -86 -2 O
ATOM 47 CB GLU H 6 49.948 15.000 -34.213 1.00 13.55 C
ANISOU 47 CB GLU H 6 1577 1620 1953 -44 -106 -30 C
ATOM 48 CG GLU H 6 49.709 15.925 -35.398 1.00 18.09 C
ANISOU 48 CG GLU H 6 2165 2178 2530 -61 -111 -40 C
ATOM 49 CD GLU H 6 48.264 16.290 -35.692 1.00 22.71 C
ANISOU 49 CD GLU H 6 2761 2740 3127 -74 -125 -42 C
ATOM 50 OE1 GLU H 6 47.341 15.651 -35.135 1.00 17.03 O
ANISOU 50 OE1 GLU H 6 2043 2011 2416 -74 -131 -40 O
ATOM 51 OE2 GLU H 6 48.055 17.240 -36.476 1.00 15.68 O
ANISOU 51 OE2 GLU H 6 1876 1844 2237 -80 -126 -40 O
ATOM 52 N SER H 7 51.094 12.283 -32.850 1.00 15.56 N
ANISOU 52 N SER H 7 1824 1896 2192 30 -66 20 N
ATOM 53 CA SER H 7 51.380 11.589 -31.596 1.00 15.93 C
ANISOU 53 CA SER H 7 1851 1972 2228 63 -54 49 C
ATOM 54 C SER H 7 52.707 12.089 -31.056 1.00 20.91 C
ANISOU 54 C SER H 7 2434 2678 2833 75 -60 62 C
ATOM 55 O SER H 7 53.608 12.430 -31.827 1.00 19.64 O
ANISOU 55 O SER H 7 2263 2532 2668 73 -58 58 O
ATOM 56 CB SER H 7 51.394 10.072 -31.776 1.00 19.00 C
ANISOU 56 CB SER H 7 2271 2323 2627 102 -15 74 C
ATOM 57 OG SER H 7 52.340 9.645 -32.740 1.00 24.78 O
ANISOU 57 OG SER H 7 3013 3047 3356 123 9 83 O
ATOM 58 N GLY H 8 52.789 12.169 -29.738 1.00 19.03 N
ANISOU 58 N GLY H 8 2166 2490 2575 83 -69 75 N
ATOM 59 CA GLY H 8 53.970 12.639 -29.030 1.00 20.03 C
ANISOU 59 CA GLY H 8 2237 2707 2667 86 -80 84 C
ATOM 60 C GLY H 8 54.008 12.169 -27.590 1.00 24.49 C
ANISOU 60 C GLY H 8 2774 3329 3201 114 -81 114 C
ATOM 61 O GLY H 8 53.048 11.554 -27.121 1.00 23.74 O
ANISOU 61 O GLY H 8 2708 3193 3118 129 -70 126 O
ATOM 62 N PRO H 9 55.096 12.472 -26.846 1.00 22.34 N
ANISOU 62 N PRO H 9 2443 3158 2886 118 -95 126 N
ATOM 63 CA PRO H 9 55.181 12.015 -25.447 1.00 22.85 C
ANISOU 63 CA PRO H 9 2477 3293 2911 150 -98 161 C
ATOM 64 C PRO H 9 54.304 12.767 -24.441 1.00 27.19 C
ANISOU 64 C PRO H 9 3033 3853 3445 105 -117 125 C
ATOM 65 O PRO H 9 54.141 12.291 -23.318 1.00 28.04 O
ANISOU 65 O PRO H 9 3129 4005 3522 134 -115 155 O
ATOM 66 CB PRO H 9 56.672 12.140 -25.127 1.00 25.03 C
ANISOU 66 CB PRO H 9 2681 3689 3142 164 -111 184 C
ATOM 67 CG PRO H 9 57.136 13.236 -25.991 1.00 29.34 C
ANISOU 67 CG PRO H 9 3217 4231 3701 104 -124 133 C
ATOM 68 CD PRO H 9 56.318 13.197 -27.250 1.00 24.37 C
ANISOU 68 CD PRO H 9 2653 3478 3127 95 -107 112 C
ATOM 69 N GLY H 10 53.780 13.930 -24.827 1.00 22.80 N
ANISOU 69 N GLY H 10 2497 3256 2909 41 -129 67 N
ATOM 70 CA GLY H 10 52.916 14.740 -23.967 1.00 22.34 C
ANISOU 70 CA GLY H 10 2451 3194 2842 -3 -137 30 C
ATOM 71 C GLY H 10 53.647 15.638 -22.985 1.00 25.86 C
ANISOU 71 C GLY H 10 2851 3741 3234 -47 -155 0 C
ATOM 72 O GLY H 10 53.269 16.798 -22.808 1.00 26.41 O
ANISOU 72 O GLY H 10 2934 3796 3306 -108 -154 -54 O
ATOM 73 N LEU H 11 54.673 15.091 -22.312 1.00 21.35 N
ANISOU 73 N LEU H 11 2225 3276 2610 -16 -166 35 N
ATOM 74 CA LEU H 11 55.511 15.788 -21.340 1.00 21.00 C
ANISOU 74 CA LEU H 11 2125 3356 2500 -59 -189 9 C
ATOM 75 C LEU H 11 56.982 15.455 -21.613 1.00 24.52 C
ANISOU 75 C LEU H 11 2502 3899 2916 -36 -202 40 C
ATOM 76 O LEU H 11 57.346 14.282 -21.721 1.00 23.10 O
ANISOU 76 O LEU H 11 2306 3736 2733 44 -193 110 O
ATOM 77 CB LEU H 11 55.104 15.427 -19.891 1.00 21.24 C
ANISOU 77 CB LEU H 11 2146 3446 2477 -40 -194 28 C
ATOM 78 CG LEU H 11 55.961 15.986 -18.731 1.00 26.14 C
ANISOU 78 CG LEU H 11 2703 4217 3012 -82 -221 4 C
ATOM 79 CD1 LEU H 11 55.865 17.513 -18.631 1.00 26.00 C
ANISOU 79 CD1 LEU H 11 2697 4193 2990 -188 -222 -90 C
ATOM 80 CD2 LEU H 11 55.554 15.356 -17.411 1.00 28.50 C
ANISOU 80 CD2 LEU H 11 2998 4575 3257 -41 -223 42 C
ATOM 81 N VAL H 12 57.803 16.503 -21.786 1.00 22.20 N
ANISOU 81 N VAL H 12 2171 3660 2605 -106 -214 -12 N
ATOM 82 CA VAL H 12 59.246 16.420 -22.064 1.00 22.94 C
ANISOU 82 CA VAL H 12 2189 3856 2671 -101 -227 7 C
ATOM 83 C VAL H 12 59.944 17.360 -21.090 1.00 27.34 C
ANISOU 83 C VAL H 12 2684 4545 3159 -181 -253 -46 C
ATOM 84 O VAL H 12 59.432 18.444 -20.817 1.00 26.77 O
ANISOU 84 O VAL H 12 2643 4439 3088 -262 -247 -120 O
ATOM 85 CB VAL H 12 59.610 16.799 -23.537 1.00 26.96 C
ANISOU 85 CB VAL H 12 2716 4291 3238 -119 -210 -11 C
ATOM 86 CG1 VAL H 12 61.049 16.413 -23.872 1.00 27.04 C
ANISOU 86 CG1 VAL H 12 2649 4398 3226 -91 -216 27 C
ATOM 87 CG2 VAL H 12 58.655 16.174 -24.542 1.00 26.49 C
ANISOU 87 CG2 VAL H 12 2733 4087 3245 -69 -184 14 C
ATOM 88 N LYS H 13 61.111 16.958 -20.578 1.00 24.50 N
ANISOU 88 N LYS H 13 2236 4337 2738 -159 -277 -9 N
ATOM 89 CA LYS H 13 61.878 17.788 -19.657 1.00 25.03 C
ANISOU 89 CA LYS H 13 2230 4552 2728 -241 -306 -61 C
ATOM 90 C LYS H 13 62.705 18.824 -20.434 1.00 29.15 C
ANISOU 90 C LYS H 13 2724 5083 3270 -328 -300 -125 C
ATOM 91 O LYS H 13 63.120 18.528 -21.562 1.00 28.06 O
ANISOU 91 O LYS H 13 2587 4893 3184 -291 -284 -94 O
ATOM 92 CB LYS H 13 62.787 16.914 -18.773 1.00 28.47 C
ANISOU 92 CB LYS H 13 2571 5165 3082 -179 -337 12 C
ATOM 93 CG LYS H 13 62.015 16.101 -17.741 1.00 38.34 C
ANISOU 93 CG LYS H 13 3845 6429 4295 -111 -340 64 C
ATOM 94 CD LYS H 13 62.936 15.401 -16.749 1.00 45.90 C
ANISOU 94 CD LYS H 13 4701 7580 5157 -55 -371 135 C
ATOM 95 CE LYS H 13 62.173 14.549 -15.758 1.00 54.15 C
ANISOU 95 CE LYS H 13 5775 8633 6168 21 -366 195 C
ATOM 96 NZ LYS H 13 61.394 15.364 -14.785 1.00 60.66 N
ANISOU 96 NZ LYS H 13 6634 9464 6950 -61 -377 119 N
ATOM 97 N PRO H 14 62.978 20.031 -19.865 1.00 26.63 N
ANISOU 97 N PRO H 14 2382 4824 2911 -445 -307 -215 N
ATOM 98 CA PRO H 14 63.833 21.004 -20.580 1.00 26.67 C
ANISOU 98 CA PRO H 14 2357 4839 2935 -532 -293 -275 C
ATOM 99 C PRO H 14 65.210 20.418 -20.914 1.00 30.66 C
ANISOU 99 C PRO H 14 2760 5471 3417 -493 -315 -220 C
ATOM 100 O PRO H 14 65.728 19.608 -20.141 1.00 30.51 O
ANISOU 100 O PRO H 14 2667 5595 3332 -438 -349 -159 O
ATOM 101 CB PRO H 14 63.950 22.174 -19.594 1.00 29.30 C
ANISOU 101 CB PRO H 14 2674 5249 3211 -660 -297 -376 C
ATOM 102 CG PRO H 14 62.791 22.020 -18.666 1.00 33.72 C
ANISOU 102 CG PRO H 14 3293 5771 3748 -642 -298 -379 C
ATOM 103 CD PRO H 14 62.576 20.546 -18.539 1.00 28.86 C
ANISOU 103 CD PRO H 14 2665 5173 3125 -507 -320 -269 C
ATOM 104 N SER H 15 65.770 20.804 -22.088 1.00 26.83 N
ANISOU 104 N SER H 15 2274 4933 2988 -515 -290 -233 N
ATOM 105 CA SER H 15 67.052 20.385 -22.686 1.00 26.92 C
ANISOU 105 CA SER H 15 2198 5033 2997 -483 -296 -185 C
ATOM 106 C SER H 15 67.002 19.049 -23.448 1.00 30.36 C
ANISOU 106 C SER H 15 2651 5410 3474 -344 -284 -79 C
ATOM 107 O SER H 15 67.920 18.754 -24.217 1.00 30.40 O
ANISOU 107 O SER H 15 2608 5445 3498 -312 -273 -41 O
ATOM 108 CB SER H 15 68.211 20.427 -21.688 1.00 31.44 C
ANISOU 108 CB SER H 15 2639 5830 3476 -522 -338 -187 C
ATOM 109 OG SER H 15 68.256 19.257 -20.886 1.00 38.28 O
ANISOU 109 OG SER H 15 3460 6798 4286 -419 -370 -97 O
ATOM 110 N GLN H 16 65.934 18.252 -23.250 1.00 26.15 N
ANISOU 110 N GLN H 16 2189 4791 2957 -266 -280 -35 N
ATOM 111 CA GLN H 16 65.758 16.957 -23.916 1.00 25.58 C
ANISOU 111 CA GLN H 16 2147 4648 2923 -142 -259 56 C
ATOM 112 C GLN H 16 65.281 17.108 -25.371 1.00 28.29 C
ANISOU 112 C GLN H 16 2576 4821 3352 -138 -220 41 C
ATOM 113 O GLN H 16 64.975 18.217 -25.813 1.00 26.86 O
ANISOU 113 O GLN H 16 2434 4570 3200 -223 -209 -33 O
ATOM 114 CB GLN H 16 64.785 16.063 -23.127 1.00 26.72 C
ANISOU 114 CB GLN H 16 2336 4766 3053 -70 -263 104 C
ATOM 115 CG GLN H 16 65.333 15.550 -21.796 1.00 38.44 C
ANISOU 115 CG GLN H 16 3733 6424 4449 -35 -296 152 C
ATOM 116 CD GLN H 16 64.435 14.509 -21.161 1.00 56.16 C
ANISOU 116 CD GLN H 16 6024 8628 6686 54 -287 215 C
ATOM 117 OE1 GLN H 16 63.200 14.552 -21.257 1.00 51.27 O
ANISOU 117 OE1 GLN H 16 5498 7874 6108 46 -271 188 O
ATOM 118 NE2 GLN H 16 65.039 13.560 -20.466 1.00 47.36 N
ANISOU 118 NE2 GLN H 16 4842 7635 5518 141 -294 304 N
ATOM 119 N THR H 17 65.229 15.984 -26.108 1.00 25.03 N
ANISOU 119 N THR H 17 2192 4343 2974 -39 -195 113 N
ATOM 120 CA THR H 17 64.775 15.942 -27.496 1.00 24.35 C
ANISOU 120 CA THR H 17 2186 4108 2958 -26 -160 106 C
ATOM 121 C THR H 17 63.307 15.513 -27.552 1.00 27.75 C
ANISOU 121 C THR H 17 2715 4408 3420 2 -150 106 C
ATOM 122 O THR H 17 62.932 14.504 -26.950 1.00 27.72 O
ANISOU 122 O THR H 17 2719 4412 3402 70 -150 158 O
ATOM 123 CB THR H 17 65.706 15.059 -28.355 1.00 31.57 C
ANISOU 123 CB THR H 17 3073 5033 3891 52 -131 173 C
ATOM 124 OG1 THR H 17 67.030 15.574 -28.273 1.00 29.95 O
ANISOU 124 OG1 THR H 17 2769 4955 3657 16 -142 168 O
ATOM 125 CG2 THR H 17 65.283 14.998 -29.828 1.00 29.52 C
ANISOU 125 CG2 THR H 17 2896 4626 3693 63 -94 163 C
ATOM 126 N LEU H 18 62.486 16.295 -28.266 1.00 23.40 N
ANISOU 126 N LEU H 18 2234 3744 2912 -50 -140 51 N
ATOM 127 CA LEU H 18 61.070 16.016 -28.487 1.00 22.66 C
ANISOU 127 CA LEU H 18 2228 3529 2852 -34 -132 46 C
ATOM 128 C LEU H 18 60.917 15.268 -29.816 1.00 25.76 C
ANISOU 128 C LEU H 18 2673 3827 3289 18 -102 76 C
ATOM 129 O LEU H 18 61.420 15.730 -30.842 1.00 25.63 O
ANISOU 129 O LEU H 18 2659 3785 3293 -2 -87 61 O
ATOM 130 CB LEU H 18 60.242 17.328 -28.489 1.00 22.39 C
ANISOU 130 CB LEU H 18 2236 3437 2836 -115 -135 -24 C
ATOM 131 CG LEU H 18 58.821 17.282 -29.106 1.00 26.69 C
ANISOU 131 CG LEU H 18 2867 3851 3424 -106 -123 -33 C
ATOM 132 CD1 LEU H 18 57.881 16.398 -28.300 1.00 26.66 C
ANISOU 132 CD1 LEU H 18 2885 3831 3412 -63 -131 -5 C
ATOM 133 CD2 LEU H 18 58.236 18.669 -29.231 1.00 29.75 C
ANISOU 133 CD2 LEU H 18 3286 4188 3830 -178 -116 -92 C
ATOM 134 N SER H 19 60.231 14.119 -29.789 1.00 21.26 N
ANISOU 134 N SER H 19 2144 3204 2731 81 -89 116 N
ATOM 135 CA SER H 19 59.971 13.320 -30.985 1.00 20.78 C
ANISOU 135 CA SER H 19 2140 3049 2706 123 -56 137 C
ATOM 136 C SER H 19 58.464 13.287 -31.243 1.00 22.58 C
ANISOU 136 C SER H 19 2444 3175 2962 106 -58 110 C
ATOM 137 O SER H 19 57.690 12.970 -30.339 1.00 21.35 O
ANISOU 137 O SER H 19 2297 3015 2798 114 -66 117 O
ATOM 138 CB SER H 19 60.540 11.912 -30.834 1.00 26.23 C
ANISOU 138 CB SER H 19 2816 3761 3389 210 -26 206 C
ATOM 139 OG SER H 19 60.434 11.192 -32.052 1.00 37.77 O
ANISOU 139 OG SER H 19 4335 5134 4883 242 13 217 O
ATOM 140 N LEU H 20 58.053 13.672 -32.460 1.00 18.05 N
ANISOU 140 N LEU H 20 1917 2526 2416 82 -50 82 N
ATOM 141 CA LEU H 20 56.646 13.723 -32.875 1.00 17.04 C
ANISOU 141 CA LEU H 20 1850 2312 2311 62 -54 58 C
ATOM 142 C LEU H 20 56.444 12.891 -34.126 1.00 19.47 C
ANISOU 142 C LEU H 20 2209 2551 2637 88 -28 67 C
ATOM 143 O LEU H 20 57.332 12.849 -34.978 1.00 18.46 O
ANISOU 143 O LEU H 20 2077 2428 2510 100 -9 74 O
ATOM 144 CB LEU H 20 56.226 15.180 -33.166 1.00 17.00 C
ANISOU 144 CB LEU H 20 1853 2291 2315 2 -71 13 C
ATOM 145 CG LEU H 20 56.314 16.177 -32.007 1.00 22.37 C
ANISOU 145 CG LEU H 20 2495 3026 2978 -40 -88 -11 C
ATOM 146 CD1 LEU H 20 56.481 17.587 -32.521 1.00 22.60 C
ANISOU 146 CD1 LEU H 20 2526 3042 3018 -94 -83 -49 C
ATOM 147 CD2 LEU H 20 55.106 16.081 -31.098 1.00 25.42 C
ANISOU 147 CD2 LEU H 20 2901 3391 3366 -44 -100 -16 C
ATOM 148 N THR H 21 55.273 12.245 -34.251 1.00 15.81 N
ANISOU 148 N THR H 21 1793 2025 2187 91 -24 62 N
ATOM 149 CA THR H 21 54.938 11.442 -35.428 1.00 15.62 C
ANISOU 149 CA THR H 21 1823 1937 2176 102 1 58 C
ATOM 150 C THR H 21 53.578 11.854 -35.982 1.00 19.09 C
ANISOU 150 C THR H 21 2299 2329 2625 60 -20 25 C
ATOM 151 O THR H 21 52.656 12.115 -35.215 1.00 18.85 O
ANISOU 151 O THR H 21 2264 2297 2600 43 -40 17 O
ATOM 152 CB THR H 21 55.044 9.929 -35.122 1.00 22.55 C
ANISOU 152 CB THR H 21 2720 2790 3057 152 42 91 C
ATOM 153 OG1 THR H 21 56.380 9.635 -34.720 1.00 22.46 O
ANISOU 153 OG1 THR H 21 2666 2833 3033 199 63 132 O
ATOM 154 CG2 THR H 21 54.702 9.047 -36.326 1.00 22.05 C
ANISOU 154 CG2 THR H 21 2719 2655 3005 153 78 77 C
ATOM 155 N CYS H 22 53.473 11.907 -37.314 1.00 15.04 N
ANISOU 155 N CYS H 22 1820 1784 2111 47 -14 8 N
ATOM 156 CA CYS H 22 52.253 12.190 -38.054 1.00 15.15 C
ANISOU 156 CA CYS H 22 1864 1765 2126 13 -33 -18 C
ATOM 157 C CYS H 22 51.908 10.919 -38.829 1.00 18.75 C
ANISOU 157 C CYS H 22 2368 2176 2579 16 -7 -29 C
ATOM 158 O CYS H 22 52.656 10.527 -39.725 1.00 18.24 O
ANISOU 158 O CYS H 22 2326 2100 2505 29 21 -29 O
ATOM 159 CB CYS H 22 52.450 13.380 -38.991 1.00 16.08 C
ANISOU 159 CB CYS H 22 1981 1893 2236 -6 -47 -29 C
ATOM 160 SG CYS H 22 51.020 13.746 -40.039 1.00 20.39 S
ANISOU 160 SG CYS H 22 2556 2417 2772 -37 -71 -48 S
ATOM 161 N SER H 23 50.801 10.259 -38.460 1.00 14.97 N
ANISOU 161 N SER H 23 1907 1672 2110 1 -8 -40 N
ATOM 162 CA SER H 23 50.336 9.043 -39.117 1.00 15.01 C
ANISOU 162 CA SER H 23 1960 1630 2113 -11 22 -60 C
ATOM 163 C SER H 23 49.124 9.378 -39.959 1.00 17.98 C
ANISOU 163 C SER H 23 2349 2006 2476 -61 -11 -93 C
ATOM 164 O SER H 23 48.190 10.018 -39.472 1.00 17.54 O
ANISOU 164 O SER H 23 2267 1969 2428 -79 -46 -93 O
ATOM 165 CB SER H 23 50.013 7.964 -38.090 1.00 18.72 C
ANISOU 165 CB SER H 23 2438 2072 2603 4 53 -47 C
ATOM 166 OG SER H 23 51.152 7.774 -37.271 1.00 27.15 O
ANISOU 166 OG SER H 23 3483 3158 3675 57 77 -7 O
ATOM 167 N PHE H 24 49.147 8.975 -41.232 1.00 14.75 N
ANISOU 167 N PHE H 24 1978 1583 2044 -80 3 -119 N
ATOM 168 CA PHE H 24 48.069 9.313 -42.160 1.00 14.29 C
ANISOU 168 CA PHE H 24 1925 1544 1962 -127 -33 -148 C
ATOM 169 C PHE H 24 47.533 8.165 -43.008 1.00 17.73 C
ANISOU 169 C PHE H 24 2407 1951 2377 -169 -9 -192 C
ATOM 170 O PHE H 24 48.177 7.125 -43.135 1.00 17.18 O
ANISOU 170 O PHE H 24 2379 1836 2311 -159 47 -202 O
ATOM 171 CB PHE H 24 48.491 10.507 -43.049 1.00 15.93 C
ANISOU 171 CB PHE H 24 2121 1788 2144 -119 -58 -137 C
ATOM 172 CG PHE H 24 49.772 10.296 -43.821 1.00 17.40 C
ANISOU 172 CG PHE H 24 2335 1962 2316 -96 -22 -135 C
ATOM 173 CD1 PHE H 24 50.979 10.792 -43.344 1.00 20.17 C
ANISOU 173 CD1 PHE H 24 2663 2318 2683 -57 -7 -104 C
ATOM 174 CD2 PHE H 24 49.772 9.600 -45.026 1.00 19.22 C
ANISOU 174 CD2 PHE H 24 2612 2178 2512 -118 -1 -166 C
ATOM 175 CE1 PHE H 24 52.163 10.596 -44.060 1.00 21.29 C
ANISOU 175 CE1 PHE H 24 2824 2451 2813 -34 29 -99 C
ATOM 176 CE2 PHE H 24 50.956 9.408 -45.742 1.00 22.21 C
ANISOU 176 CE2 PHE H 24 3019 2543 2879 -94 38 -162 C
ATOM 177 CZ PHE H 24 52.143 9.905 -45.252 1.00 20.20 C
ANISOU 177 CZ PHE H 24 2737 2293 2646 -49 54 -126 C
ATOM 178 N SER H 25 46.341 8.375 -43.596 1.00 15.09 N
ANISOU 178 N SER H 25 2065 1650 2020 -217 -48 -218 N
ATOM 179 CA SER H 25 45.653 7.449 -44.502 1.00 15.69 C
ANISOU 179 CA SER H 25 2177 1718 2065 -276 -37 -270 C
ATOM 180 C SER H 25 44.868 8.270 -45.533 1.00 19.69 C
ANISOU 180 C SER H 25 2660 2297 2524 -308 -94 -280 C
ATOM 181 O SER H 25 44.619 9.458 -45.309 1.00 18.51 O
ANISOU 181 O SER H 25 2465 2190 2378 -282 -137 -242 O
ATOM 182 CB SER H 25 44.708 6.536 -43.723 1.00 19.37 C
ANISOU 182 CB SER H 25 2645 2156 2560 -312 -20 -293 C
ATOM 183 OG SER H 25 43.734 7.290 -43.019 1.00 26.37 O
ANISOU 183 OG SER H 25 3475 3082 3461 -316 -70 -272 O
ATOM 184 N GLY H 26 44.501 7.639 -46.646 1.00 17.75 N
ANISOU 184 N GLY H 26 2447 2066 2232 -361 -90 -329 N
ATOM 185 CA GLY H 26 43.721 8.279 -47.702 1.00 18.28 C
ANISOU 185 CA GLY H 26 2489 2214 2241 -393 -145 -338 C
ATOM 186 C GLY H 26 44.534 8.884 -48.827 1.00 22.77 C
ANISOU 186 C GLY H 26 3078 2809 2765 -368 -147 -326 C
ATOM 187 O GLY H 26 43.972 9.295 -49.847 1.00 23.29 O
ANISOU 187 O GLY H 26 3131 2946 2771 -392 -186 -333 O
ATOM 188 N PHE H 27 45.858 8.970 -48.637 1.00 18.83 N
ANISOU 188 N PHE H 27 2605 2259 2290 -316 -106 -303 N
ATOM 189 CA PHE H 27 46.806 9.478 -49.631 1.00 18.30 C
ANISOU 189 CA PHE H 27 2561 2203 2188 -288 -94 -289 C
ATOM 190 C PHE H 27 48.172 8.832 -49.402 1.00 21.48 C
ANISOU 190 C PHE H 27 3006 2534 2620 -254 -27 -288 C
ATOM 191 O PHE H 27 48.420 8.277 -48.330 1.00 20.97 O
ANISOU 191 O PHE H 27 2939 2421 2606 -238 2 -281 O
ATOM 192 CB PHE H 27 46.895 11.025 -49.612 1.00 19.33 C
ANISOU 192 CB PHE H 27 2646 2377 2322 -243 -132 -231 C
ATOM 193 CG PHE H 27 47.704 11.623 -48.485 1.00 19.88 C
ANISOU 193 CG PHE H 27 2691 2410 2452 -192 -116 -189 C
ATOM 194 CD1 PHE H 27 47.137 11.826 -47.231 1.00 21.68 C
ANISOU 194 CD1 PHE H 27 2881 2632 2726 -187 -133 -173 C
ATOM 195 CD2 PHE H 27 49.036 11.984 -48.675 1.00 21.18 C
ANISOU 195 CD2 PHE H 27 2870 2552 2625 -153 -82 -168 C
ATOM 196 CE1 PHE H 27 47.888 12.380 -46.187 1.00 21.78 C
ANISOU 196 CE1 PHE H 27 2871 2619 2785 -148 -119 -141 C
ATOM 197 CE2 PHE H 27 49.787 12.529 -47.628 1.00 22.93 C
ANISOU 197 CE2 PHE H 27 3063 2752 2897 -116 -69 -136 C
ATOM 198 CZ PHE H 27 49.207 12.727 -46.393 1.00 20.37 C
ANISOU 198 CZ PHE H 27 2703 2426 2611 -116 -90 -124 C
ATOM 199 N SER H 28 49.050 8.908 -50.410 1.00 17.17 N
ANISOU 199 N SER H 28 2496 1988 2042 -240 0 -290 N
ATOM 200 CA SER H 28 50.403 8.378 -50.319 1.00 16.43 C
ANISOU 200 CA SER H 28 2436 1835 1972 -200 66 -282 C
ATOM 201 C SER H 28 51.399 9.527 -50.433 1.00 18.99 C
ANISOU 201 C SER H 28 2733 2178 2304 -148 62 -232 C
ATOM 202 O SER H 28 51.239 10.409 -51.279 1.00 18.01 O
ANISOU 202 O SER H 28 2601 2099 2141 -150 32 -222 O
ATOM 203 CB SER H 28 50.653 7.347 -51.418 1.00 19.58 C
ANISOU 203 CB SER H 28 2906 2207 2328 -231 118 -333 C
ATOM 204 OG SER H 28 51.999 6.898 -51.415 1.00 24.26 O
ANISOU 204 OG SER H 28 3530 2746 2944 -184 187 -317 O
ATOM 205 N LEU H 29 52.444 9.503 -49.598 1.00 15.65 N
ANISOU 205 N LEU H 29 2294 1724 1930 -102 96 -200 N
ATOM 206 CA LEU H 29 53.495 10.509 -49.669 1.00 15.11 C
ANISOU 206 CA LEU H 29 2198 1670 1872 -61 101 -160 C
ATOM 207 C LEU H 29 54.498 10.157 -50.797 1.00 19.76 C
ANISOU 207 C LEU H 29 2833 2242 2433 -46 153 -166 C
ATOM 208 O LEU H 29 55.457 10.885 -51.006 1.00 19.71 O
ANISOU 208 O LEU H 29 2809 2246 2434 -15 168 -136 O
ATOM 209 CB LEU H 29 54.161 10.721 -48.292 1.00 14.40 C
ANISOU 209 CB LEU H 29 2060 1573 1839 -26 106 -124 C
ATOM 210 CG LEU H 29 55.223 11.839 -48.136 1.00 18.34 C
ANISOU 210 CG LEU H 29 2517 2095 2355 5 109 -87 C
ATOM 211 CD1 LEU H 29 54.717 13.230 -48.611 1.00 18.30 C
ANISOU 211 CD1 LEU H 29 2496 2123 2333 -10 70 -77 C
ATOM 212 CD2 LEU H 29 55.677 11.930 -46.719 1.00 19.49 C
ANISOU 212 CD2 LEU H 29 2613 2247 2544 26 107 -63 C
ATOM 213 N SER H 30 54.251 9.074 -51.546 1.00 16.77 N
ANISOU 213 N SER H 30 2513 1837 2021 -73 186 -210 N
ATOM 214 CA SER H 30 55.086 8.707 -52.694 1.00 17.63 C
ANISOU 214 CA SER H 30 2674 1928 2096 -63 240 -222 C
ATOM 215 C SER H 30 54.486 9.309 -53.986 1.00 21.14 C
ANISOU 215 C SER H 30 3140 2422 2471 -97 206 -242 C
ATOM 216 O SER H 30 55.138 9.299 -55.032 1.00 21.45 O
ANISOU 216 O SER H 30 3218 2459 2473 -88 242 -247 O
ATOM 217 CB SER H 30 55.221 7.189 -52.802 1.00 21.82 C
ANISOU 217 CB SER H 30 3267 2396 2627 -74 309 -261 C
ATOM 218 OG SER H 30 54.008 6.575 -53.198 1.00 31.83 O
ANISOU 218 OG SER H 30 4570 3666 3857 -140 291 -319 O
ATOM 219 N THR H 31 53.241 9.834 -53.906 1.00 16.83 N
ANISOU 219 N THR H 31 2565 1924 1903 -130 138 -248 N
ATOM 220 CA THR H 31 52.547 10.457 -55.039 1.00 16.06 C
ANISOU 220 CA THR H 31 2475 1891 1735 -156 97 -255 C
ATOM 221 C THR H 31 53.273 11.747 -55.424 1.00 17.85 C
ANISOU 221 C THR H 31 2680 2140 1962 -110 96 -201 C
ATOM 222 O THR H 31 53.536 12.571 -54.553 1.00 15.73 O
ANISOU 222 O THR H 31 2363 1866 1746 -79 84 -160 O
ATOM 223 CB THR H 31 51.066 10.709 -54.677 1.00 22.38 C
ANISOU 223 CB THR H 31 3238 2742 2525 -193 28 -263 C
ATOM 224 OG1 THR H 31 50.443 9.462 -54.383 1.00 19.25 O
ANISOU 224 OG1 THR H 31 2865 2320 2129 -242 38 -318 O
ATOM 225 CG2 THR H 31 50.293 11.425 -55.788 1.00 21.90 C
ANISOU 225 CG2 THR H 31 3170 2764 2387 -209 -20 -257 C
ATOM 226 N SER H 32 53.612 11.908 -56.719 1.00 15.18 N
ANISOU 226 N SER H 32 2382 1825 1563 -108 115 -205 N
ATOM 227 CA SER H 32 54.301 13.099 -57.240 1.00 14.70 C
ANISOU 227 CA SER H 32 2308 1781 1496 -67 124 -155 C
ATOM 228 C SER H 32 53.561 14.394 -56.840 1.00 18.53 C
ANISOU 228 C SER H 32 2738 2308 1994 -53 71 -108 C
ATOM 229 O SER H 32 52.345 14.487 -57.020 1.00 17.61 O
ANISOU 229 O SER H 32 2608 2243 1838 -77 19 -114 O
ATOM 230 CB SER H 32 54.431 13.009 -58.758 1.00 17.84 C
ANISOU 230 CB SER H 32 2759 2210 1810 -74 144 -169 C
ATOM 231 OG SER H 32 55.274 14.030 -59.266 1.00 24.16 O
ANISOU 231 OG SER H 32 3556 3013 2610 -31 170 -120 O
ATOM 232 N GLY H 33 54.296 15.337 -56.245 1.00 15.19 N
ANISOU 232 N GLY H 33 2282 1862 1628 -17 89 -64 N
ATOM 233 CA GLY H 33 53.762 16.618 -55.789 1.00 14.53 C
ANISOU 233 CA GLY H 33 2153 1800 1568 -1 58 -20 C
ATOM 234 C GLY H 33 53.381 16.665 -54.319 1.00 17.78 C
ANISOU 234 C GLY H 33 2520 2192 2045 -8 34 -20 C
ATOM 235 O GLY H 33 53.220 17.755 -53.762 1.00 17.11 O
ANISOU 235 O GLY H 33 2401 2106 1994 8 27 14 O
ATOM 236 N MET H 34 53.226 15.491 -53.676 1.00 13.55 N
ANISOU 236 N MET H 34 1988 1635 1525 -31 29 -60 N
ATOM 237 CA MET H 34 52.806 15.400 -52.273 1.00 11.97 C
ANISOU 237 CA MET H 34 1749 1419 1380 -38 7 -62 C
ATOM 238 C MET H 34 53.838 15.906 -51.273 1.00 15.02 C
ANISOU 238 C MET H 34 2103 1776 1828 -16 33 -41 C
ATOM 239 O MET H 34 55.041 15.725 -51.457 1.00 14.33 O
ANISOU 239 O MET H 34 2025 1669 1752 0 76 -38 O
ATOM 240 CB MET H 34 52.364 13.971 -51.912 1.00 13.70 C
ANISOU 240 CB MET H 34 1986 1622 1597 -67 3 -106 C
ATOM 241 CG MET H 34 51.258 13.920 -50.862 1.00 16.41 C
ANISOU 241 CG MET H 34 2294 1973 1968 -86 -38 -110 C
ATOM 242 SD MET H 34 49.667 14.602 -51.423 1.00 19.60 S
ANISOU 242 SD MET H 34 2677 2443 2326 -105 -98 -100 S
ATOM 243 CE MET H 34 49.174 13.349 -52.617 1.00 16.78 C
ANISOU 243 CE MET H 34 2368 2112 1897 -153 -101 -156 C
ATOM 244 N GLY H 35 53.338 16.518 -50.209 1.00 12.01 N
ANISOU 244 N GLY H 35 1683 1397 1485 -18 9 -28 N
ATOM 245 CA GLY H 35 54.150 17.038 -49.120 1.00 11.52 C
ANISOU 245 CA GLY H 35 1584 1318 1476 -9 26 -15 C
ATOM 246 C GLY H 35 53.414 16.999 -47.802 1.00 15.27 C
ANISOU 246 C GLY H 35 2027 1792 1982 -20 -4 -20 C
ATOM 247 O GLY H 35 52.181 16.928 -47.774 1.00 14.35 O
ANISOU 247 O GLY H 35 1911 1688 1854 -32 -38 -24 O
ATOM 248 N VAL H 36 54.169 17.017 -46.699 1.00 12.82 N
ANISOU 248 N VAL H 36 1687 1475 1711 -17 9 -20 N
ATOM 249 CA VAL H 36 53.622 17.030 -45.338 1.00 12.50 C
ANISOU 249 CA VAL H 36 1615 1436 1699 -27 -14 -23 C
ATOM 250 C VAL H 36 54.400 18.071 -44.549 1.00 15.67 C
ANISOU 250 C VAL H 36 1981 1844 2131 -31 1 -15 C
ATOM 251 O VAL H 36 55.630 18.092 -44.601 1.00 14.25 O
ANISOU 251 O VAL H 36 1787 1670 1956 -26 29 -13 O
ATOM 252 CB VAL H 36 53.619 15.635 -44.639 1.00 16.30 C