HEADER TRANSPORT PROTEIN 23-DEC-11 3V8U
TITLE THE CRYSTAL STRUCTURE OF TRANSFERRIN BINDING PROTEIN B (TBPB) FROM
TITLE 2 NEISSERIA MENINGITIDIS SEROGROUP B
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSFERRIN BINDING-PROTEIN B;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: NEISSERIA MENINGITIDIS SEROGROUP B;
SOURCE 3 ORGANISM_TAXID: 491;
SOURCE 4 GENE: TBPB;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS TRANSFERRIN BINDING PROTEIN, LIPOPROTEIN, TRANSPORT PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR N.NOINAJ,N.EASLEY,S.K.BUCHANAN
REVDAT 3 18-APR-12 3V8U 1 JRNL
REVDAT 2 29-FEB-12 3V8U 1 JRNL
REVDAT 1 15-FEB-12 3V8U 0
JRNL AUTH N.NOINAJ,N.C.EASLEY,M.OKE,N.MIZUNO,J.GUMBART,E.BOURA,
JRNL AUTH 2 A.N.STEERE,O.ZAK,P.AISEN,E.TAJKHORSHID,R.W.EVANS,
JRNL AUTH 3 A.R.GORRINGE,A.B.MASON,A.C.STEVEN,S.K.BUCHANAN
JRNL TITL STRUCTURAL BASIS FOR IRON PIRACY BY PATHOGENIC NEISSERIA.
JRNL REF NATURE V. 483 53 2012
JRNL REFN ISSN 0028-0836
JRNL PMID 22327295
JRNL DOI 10.1038/NATURE10823
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7.3_928)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.50
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.060
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.1
REMARK 3 NUMBER OF REFLECTIONS : 48517
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.255
REMARK 3 R VALUE (WORKING SET) : 0.253
REMARK 3 FREE R VALUE : 0.308
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.040
REMARK 3 FREE R VALUE TEST SET COUNT : 1961
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 29.5077 - 5.7709 0.99 3560 154 0.2048 0.2541
REMARK 3 2 5.7709 - 4.5861 1.00 3514 145 0.1863 0.2628
REMARK 3 3 4.5861 - 4.0080 1.00 3507 148 0.1803 0.2277
REMARK 3 4 4.0080 - 3.6423 0.85 2964 131 0.2334 0.3057
REMARK 3 5 3.6423 - 3.3816 0.85 2987 123 0.2530 0.2869
REMARK 3 6 3.3816 - 3.1825 0.98 3418 146 0.2519 0.3016
REMARK 3 7 3.1825 - 3.0233 0.98 3409 141 0.2535 0.3136
REMARK 3 8 3.0233 - 2.8918 0.97 3375 141 0.2682 0.3263
REMARK 3 9 2.8918 - 2.7806 0.97 3360 140 0.2929 0.3256
REMARK 3 10 2.7806 - 2.6847 0.96 3353 144 0.3263 0.3868
REMARK 3 11 2.6847 - 2.6008 0.95 3304 132 0.3579 0.4161
REMARK 3 12 2.6008 - 2.5265 0.95 3315 140 0.4011 0.4530
REMARK 3 13 2.5265 - 2.4600 0.94 3292 143 0.4194 0.4518
REMARK 3 14 2.4600 - 2.4000 0.93 3198 133 0.4682 0.5342
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 0.90
REMARK 3 SHRINKAGE RADIUS : 0.60
REMARK 3 K_SOL : 0.30
REMARK 3 B_SOL : 29.16
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.520
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 39.410
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -5.28830
REMARK 3 B22 (A**2) : 0.60310
REMARK 3 B33 (A**2) : 4.68530
REMARK 3 B12 (A**2) : -0.00000
REMARK 3 B13 (A**2) : -1.72350
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.010 8394
REMARK 3 ANGLE : 1.459 11322
REMARK 3 CHIRALITY : 0.100 1188
REMARK 3 PLANARITY : 0.006 1492
REMARK 3 DIHEDRAL : 18.056 3044
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 20
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: chain A and resi 98:145
REMARK 3 ORIGIN FOR THE GROUP (A): -24.2291 5.3040 -40.3125
REMARK 3 T TENSOR
REMARK 3 T11: 0.2235 T22: 1.0261
REMARK 3 T33: 0.2427 T12: -0.0370
REMARK 3 T13: -0.0174 T23: 0.1398
REMARK 3 L TENSOR
REMARK 3 L11: 1.5611 L22: 2.5929
REMARK 3 L33: 2.6547 L12: 0.7143
REMARK 3 L13: 0.9475 L23: 1.8650
REMARK 3 S TENSOR
REMARK 3 S11: 0.0119 S12: 0.3827 S13: 0.0447
REMARK 3 S21: -0.2501 S22: -0.0998 S23: 0.1541
REMARK 3 S31: -0.1395 S32: -0.1919 S33: 0.0985
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: chain A and resi 37:97
REMARK 3 ORIGIN FOR THE GROUP (A): -22.7439 -11.3677 -40.7651
REMARK 3 T TENSOR
REMARK 3 T11: 0.2630 T22: 1.1041
REMARK 3 T33: 0.2692 T12: 0.0232
REMARK 3 T13: -0.0198 T23: -0.1372
REMARK 3 L TENSOR
REMARK 3 L11: 2.4966 L22: 2.1743
REMARK 3 L33: 2.3905 L12: 1.4581
REMARK 3 L13: 1.6712 L23: 0.6278
REMARK 3 S TENSOR
REMARK 3 S11: 0.1356 S12: 0.2812 S13: -0.1513
REMARK 3 S21: -0.2211 S22: -0.0564 S23: 0.0741
REMARK 3 S31: 0.2078 S32: -0.0134 S33: -0.0397
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: chain A and resi 146:233
REMARK 3 ORIGIN FOR THE GROUP (A): -30.6984 -4.8104 -37.9238
REMARK 3 T TENSOR
REMARK 3 T11: 0.1392 T22: 0.8749
REMARK 3 T33: 0.1734 T12: 0.0285
REMARK 3 T13: -0.0642 T23: 0.0494
REMARK 3 L TENSOR
REMARK 3 L11: 1.3552 L22: 0.8612
REMARK 3 L33: 1.0698 L12: 0.3004
REMARK 3 L13: 0.6810 L23: 0.4781
REMARK 3 S TENSOR
REMARK 3 S11: 0.0455 S12: 0.2390 S13: -0.0788
REMARK 3 S21: -0.1395 S22: 0.0591 S23: 0.1105
REMARK 3 S31: 0.0151 S32: -0.0236 S33: -0.0195
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: chain A and resi 234:262
REMARK 3 ORIGIN FOR THE GROUP (A): -30.0269 8.0824 -23.3384
REMARK 3 T TENSOR
REMARK 3 T11: 0.3138 T22: 0.7524
REMARK 3 T33: 0.4389 T12: 0.0333
REMARK 3 T13: -0.2037 T23: -0.0280
REMARK 3 L TENSOR
REMARK 3 L11: 3.4175 L22: 0.9256
REMARK 3 L33: 3.4982 L12: -0.8859
REMARK 3 L13: 1.8880 L23: -1.1357
REMARK 3 S TENSOR
REMARK 3 S11: -0.1938 S12: -0.3744 S13: 0.3240
REMARK 3 S21: 0.0656 S22: 0.1038 S23: 0.1444
REMARK 3 S31: -0.1977 S32: -0.3919 S33: 0.1585
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: chain A and resi 263:293
REMARK 3 ORIGIN FOR THE GROUP (A): -32.6683 1.5972 -23.8749
REMARK 3 T TENSOR
REMARK 3 T11: 0.1620 T22: 0.6112
REMARK 3 T33: 0.1634 T12: 0.0809
REMARK 3 T13: 0.0083 T23: 0.0450
REMARK 3 L TENSOR
REMARK 3 L11: 0.4699 L22: 3.8126
REMARK 3 L33: 2.6142 L12: 0.6878
REMARK 3 L13: -0.1995 L23: -0.2462
REMARK 3 S TENSOR
REMARK 3 S11: -0.1128 S12: -0.3461 S13: -0.2318
REMARK 3 S21: -0.1044 S22: 0.1867 S23: 0.4050
REMARK 3 S31: -0.0253 S32: -0.5517 S33: -0.0808
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: chain A and resi 294:405
REMARK 3 ORIGIN FOR THE GROUP (A): -19.9742 -0.5920 -24.3895
REMARK 3 T TENSOR
REMARK 3 T11: 0.1240 T22: 0.0492
REMARK 3 T33: 0.1086 T12: 0.0110
REMARK 3 T13: -0.0125 T23: 0.0815
REMARK 3 L TENSOR
REMARK 3 L11: 1.3474 L22: 0.9986
REMARK 3 L33: 1.5255 L12: -0.3384
REMARK 3 L13: 0.5606 L23: 0.0009
REMARK 3 S TENSOR
REMARK 3 S11: 0.0479 S12: 0.1350 S13: 0.0035
REMARK 3 S21: -0.0005 S22: 0.0269 S23: -0.0158
REMARK 3 S31: -0.0180 S32: 0.2248 S33: 0.0766
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: chain A and resi 406:565
REMARK 3 ORIGIN FOR THE GROUP (A): 5.7958 -5.5312 -17.5603
REMARK 3 T TENSOR
REMARK 3 T11: 0.2335 T22: 1.0155
REMARK 3 T33: 0.3175 T12: 0.1389
REMARK 3 T13: -0.0987 T23: -0.1131
REMARK 3 L TENSOR
REMARK 3 L11: 2.0390 L22: 0.3997
REMARK 3 L33: 0.2192 L12: -0.0005
REMARK 3 L13: 0.5772 L23: -0.1490
REMARK 3 S TENSOR
REMARK 3 S11: 0.0872 S12: 0.1262 S13: -0.3026
REMARK 3 S21: -0.0534 S22: 0.0380 S23: 0.0954
REMARK 3 S31: 0.0873 S32: -0.0442 S33: -0.1030
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: chain A and resi 566:602
REMARK 3 ORIGIN FOR THE GROUP (A): 14.2683 -0.9173 -4.4211
REMARK 3 T TENSOR
REMARK 3 T11: 0.3051 T22: 0.9310
REMARK 3 T33: 0.2806 T12: 0.1596
REMARK 3 T13: -0.1109 T23: -0.0964
REMARK 3 L TENSOR
REMARK 3 L11: 1.9030 L22: 0.9206
REMARK 3 L33: 1.4386 L12: 0.0747
REMARK 3 L13: 0.6565 L23: 0.4540
REMARK 3 S TENSOR
REMARK 3 S11: -0.0027 S12: -0.2346 S13: 0.0201
REMARK 3 S21: 0.1663 S22: 0.0320 S23: -0.1107
REMARK 3 S31: 0.0815 S32: -0.0098 S33: -0.0726
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: chain A and resi 603:661
REMARK 3 ORIGIN FOR THE GROUP (A): 14.7825 5.3297 -10.4698
REMARK 3 T TENSOR
REMARK 3 T11: 0.1680 T22: 0.8088
REMARK 3 T33: 0.2737 T12: 0.0416
REMARK 3 T13: -0.1080 T23: -0.0817
REMARK 3 L TENSOR
REMARK 3 L11: 3.3937 L22: 1.6859
REMARK 3 L33: 0.9234 L12: -0.7457
REMARK 3 L13: 0.6293 L23: -0.0554
REMARK 3 S TENSOR
REMARK 3 S11: -0.0403 S12: 0.0020 S13: 0.4539
REMARK 3 S21: 0.1365 S22: -0.0297 S23: -0.3911
REMARK 3 S31: -0.0511 S32: 0.1276 S33: 0.0090
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: chain A and resi 662:688
REMARK 3 ORIGIN FOR THE GROUP (A): 12.9334 3.0141 -13.5650
REMARK 3 T TENSOR
REMARK 3 T11: 0.1357 T22: 0.5742
REMARK 3 T33: 0.2416 T12: 0.0671
REMARK 3 T13: -0.0573 T23: -0.0196
REMARK 3 L TENSOR
REMARK 3 L11: 6.2924 L22: 2.7285
REMARK 3 L33: 3.6784 L12: 1.9516
REMARK 3 L13: -0.2002 L23: -1.3577
REMARK 3 S TENSOR
REMARK 3 S11: -0.0566 S12: 0.3103 S13: 0.2051
REMARK 3 S21: -0.0533 S22: 0.1542 S23: 0.1259
REMARK 3 S31: -0.0654 S32: -0.0358 S33: -0.0945
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: chain B and resi 37:97
REMARK 3 ORIGIN FOR THE GROUP (A): 10.0415 28.6912 -40.1205
REMARK 3 T TENSOR
REMARK 3 T11: 0.1757 T22: 0.6669
REMARK 3 T33: 0.2234 T12: -0.0573
REMARK 3 T13: 0.0062 T23: -0.1321
REMARK 3 L TENSOR
REMARK 3 L11: 3.2265 L22: 3.0046
REMARK 3 L33: 2.8526 L12: 1.7016
REMARK 3 L13: 1.7563 L23: 1.1156
REMARK 3 S TENSOR
REMARK 3 S11: 0.1121 S12: 0.1274 S13: -0.1177
REMARK 3 S21: -0.2323 S22: -0.0832 S23: 0.0106
REMARK 3 S31: 0.1132 S32: 0.0851 S33: -0.0646
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: chain B and resi 98:145
REMARK 3 ORIGIN FOR THE GROUP (A): 8.4842 45.3310 -38.7712
REMARK 3 T TENSOR
REMARK 3 T11: 0.1890 T22: 0.6635
REMARK 3 T33: 0.2293 T12: 0.0005
REMARK 3 T13: -0.0669 T23: 0.0706
REMARK 3 L TENSOR
REMARK 3 L11: 2.6901 L22: 3.8392
REMARK 3 L33: 4.1001 L12: 0.3541
REMARK 3 L13: 1.3529 L23: 2.6533
REMARK 3 S TENSOR
REMARK 3 S11: -0.1226 S12: -0.0845 S13: 0.2856
REMARK 3 S21: -0.3939 S22: 0.0471 S23: 0.2587
REMARK 3 S31: -0.4309 S32: 0.1386 S33: 0.2037
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: chain B and resi 146:233
REMARK 3 ORIGIN FOR THE GROUP (A): 2.0698 35.0666 -36.8850
REMARK 3 T TENSOR
REMARK 3 T11: 0.1016 T22: 0.7005
REMARK 3 T33: 0.1850 T12: -0.0225
REMARK 3 T13: -0.0862 T23: 0.0754
REMARK 3 L TENSOR
REMARK 3 L11: 1.2880 L22: 0.9721
REMARK 3 L33: 0.7969 L12: 0.0742
REMARK 3 L13: 0.6328 L23: 0.2572
REMARK 3 S TENSOR
REMARK 3 S11: 0.0788 S12: 0.0825 S13: -0.1269
REMARK 3 S21: -0.1532 S22: 0.1063 S23: 0.2072
REMARK 3 S31: 0.0668 S32: -0.0604 S33: -0.0250
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: chain B and resi 234:262
REMARK 3 ORIGIN FOR THE GROUP (A): 2.5702 47.2621 -21.7177
REMARK 3 T TENSOR
REMARK 3 T11: 0.1814 T22: 0.6563
REMARK 3 T33: 0.2344 T12: 0.0696
REMARK 3 T13: -0.0878 T23: -0.0720
REMARK 3 L TENSOR
REMARK 3 L11: 3.4215 L22: 1.2322
REMARK 3 L33: 4.2857 L12: -0.4973
REMARK 3 L13: 2.7956 L23: -1.3612
REMARK 3 S TENSOR
REMARK 3 S11: -0.2847 S12: -0.5135 S13: 0.3538
REMARK 3 S21: 0.0300 S22: 0.0791 S23: 0.1806
REMARK 3 S31: -0.3348 S32: -0.4197 S33: 0.2177
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: chain B and resi 263:293
REMARK 3 ORIGIN FOR THE GROUP (A): -0.0702 40.8118 -22.5857
REMARK 3 T TENSOR
REMARK 3 T11: 0.1370 T22: 0.6690
REMARK 3 T33: 0.2424 T12: 0.0350
REMARK 3 T13: -0.0310 T23: -0.0050
REMARK 3 L TENSOR
REMARK 3 L11: 1.6906 L22: 3.5811
REMARK 3 L33: 1.4409 L12: 0.6960
REMARK 3 L13: -0.7030 L23: -0.2603
REMARK 3 S TENSOR
REMARK 3 S11: 0.0149 S12: -0.4163 S13: -0.0931
REMARK 3 S21: -0.1063 S22: 0.0185 S23: 0.5486
REMARK 3 S31: -0.0391 S32: -0.4849 S33: -0.1155
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: chain B and resi 294:405
REMARK 3 ORIGIN FOR THE GROUP (A): 12.6341 38.6532 -23.1370
REMARK 3 T TENSOR
REMARK 3 T11: 0.0642 T22: 0.6402
REMARK 3 T33: 0.0982 T12: -0.0192
REMARK 3 T13: -0.0007 T23: -0.0131
REMARK 3 L TENSOR
REMARK 3 L11: 0.8172 L22: 0.5051
REMARK 3 L33: 1.3957 L12: -0.3396
REMARK 3 L13: 0.3195 L23: 0.1563
REMARK 3 S TENSOR
REMARK 3 S11: 0.0136 S12: -0.0900 S13: -0.0405
REMARK 3 S21: 0.0331 S22: 0.0228 S23: -0.0049
REMARK 3 S31: 0.0194 S32: 0.0937 S33: 0.0078
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: chain B and resi 406:565
REMARK 3 ORIGIN FOR THE GROUP (A): 38.3790 33.3919 -16.4231
REMARK 3 T TENSOR
REMARK 3 T11: 0.2227 T22: 1.0845
REMARK 3 T33: 0.2718 T12: 0.1031
REMARK 3 T13: -0.0523 T23: -0.1046
REMARK 3 L TENSOR
REMARK 3 L11: 1.6824 L22: 0.1647
REMARK 3 L33: 0.3685 L12: 0.2518
REMARK 3 L13: 0.3115 L23: -0.1183
REMARK 3 S TENSOR
REMARK 3 S11: 0.0996 S12: 0.0024 S13: -0.1504
REMARK 3 S21: 0.0259 S22: -0.0033 S23: -0.0153
REMARK 3 S31: 0.0823 S32: -0.0254 S33: 0.0117
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: chain B and resi 566:629
REMARK 3 ORIGIN FOR THE GROUP (A): 47.7728 40.5028 -4.7829
REMARK 3 T TENSOR
REMARK 3 T11: 0.2009 T22: 0.8744
REMARK 3 T33: 0.2799 T12: 0.1045
REMARK 3 T13: -0.1316 T23: -0.0712
REMARK 3 L TENSOR
REMARK 3 L11: 1.9277 L22: 1.0324
REMARK 3 L33: 0.7885 L12: -0.4948
REMARK 3 L13: 0.3868 L23: -0.0135
REMARK 3 S TENSOR
REMARK 3 S11: -0.0332 S12: -0.1018 S13: 0.1905
REMARK 3 S21: 0.1402 S22: -0.0049 S23: -0.3009
REMARK 3 S31: 0.0617 S32: 0.2228 S33: -0.0319
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: chain B and resi 630:664
REMARK 3 ORIGIN FOR THE GROUP (A): 45.6140 43.5836 -10.6802
REMARK 3 T TENSOR
REMARK 3 T11: 0.2409 T22: 0.8961
REMARK 3 T33: 0.2052 T12: -0.0857
REMARK 3 T13: -0.0583 T23: 0.0080
REMARK 3 L TENSOR
REMARK 3 L11: 5.7393 L22: 2.5275
REMARK 3 L33: 1.3823 L12: 0.5259
REMARK 3 L13: 1.7930 L23: -0.1175
REMARK 3 S TENSOR
REMARK 3 S11: 0.0582 S12: 0.2671 S13: 0.2164
REMARK 3 S21: 0.1014 S22: -0.1491 S23: -0.2990
REMARK 3 S31: -0.0888 S32: 0.1652 S33: 0.0179
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: chain B and resi 674:688
REMARK 3 ORIGIN FOR THE GROUP (A): 45.1982 40.1281 -10.7786
REMARK 3 T TENSOR
REMARK 3 T11: 0.2008 T22: 0.5935
REMARK 3 T33: 0.1853 T12: -0.0466
REMARK 3 T13: -0.0658 T23: 0.0738
REMARK 3 L TENSOR
REMARK 3 L11: 5.7669 L22: 2.5650
REMARK 3 L33: 5.3459 L12: 1.2399
REMARK 3 L13: 0.5559 L23: -0.8521
REMARK 3 S TENSOR
REMARK 3 S11: 0.0624 S12: 0.0922 S13: 0.0201
REMARK 3 S21: -0.0365 S22: -0.0729 S23: -0.0536
REMARK 3 S31: -0.0848 S32: 0.1147 S33: 0.0745
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 1
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: chain 'A' and (resseq 37:106 or resseq
REMARK 3 121:350 or resseq 380:420 or resseq 439:
REMARK 3 448 or resseq 479:502 or resseq 523:664 or
REMARK 3 resseq 674:688 )
REMARK 3 SELECTION : chain 'B' and (resseq 37:106 or resseq
REMARK 3 121:350 or resseq 380:420 or resseq 439:
REMARK 3 448 or resseq 479:502 or resseq 523:664 or
REMARK 3 resseq 674:688 )
REMARK 3 ATOM PAIRS NUMBER : 4102
REMARK 3 RMSD : 0.060
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3V8U COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-JAN-12.
REMARK 100 THE RCSB ID CODE IS RCSB069740.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-DEC-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 23-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 49472
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.9
REMARK 200 DATA REDUNDANCY : 4.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.12000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.4
REMARK 200 DATA REDUNDANCY IN SHELL : 3.20
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.54000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.700
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.42
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.0 M NACL AND 2.0 M AMMONIUM SULFATE,
REMARK 280 PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 41.06650
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A -25
REMARK 465 SER A -24
REMARK 465 TYR A -23
REMARK 465 TYR A -22
REMARK 465 HIS A -21
REMARK 465 HIS A -20
REMARK 465 HIS A -19
REMARK 465 HIS A -18
REMARK 465 HIS A -17
REMARK 465 HIS A -16
REMARK 465 ASP A -15
REMARK 465 TYR A -14
REMARK 465 ASP A -13
REMARK 465 ILE A -12
REMARK 465 PRO A -11
REMARK 465 THR A -10
REMARK 465 THR A -9
REMARK 465 GLU A -8
REMARK 465 ASN A -7
REMARK 465 LEU A -6
REMARK 465 TYR A -5
REMARK 465 PHE A -4
REMARK 465 GLN A -3
REMARK 465 GLY A -2
REMARK 465 ALA A -1
REMARK 465 MET A 0
REMARK 465 LEU A 1
REMARK 465 GLY A 2
REMARK 465 GLY A 3
REMARK 465 GLY A 4
REMARK 465 GLY A 5
REMARK 465 SER A 6
REMARK 465 PHE A 7
REMARK 465 ASP A 8
REMARK 465 LEU A 9
REMARK 465 ASP A 10
REMARK 465 SER A 11
REMARK 465 VAL A 12
REMARK 465 ASP A 13
REMARK 465 THR A 14
REMARK 465 GLU A 15
REMARK 465 ALA A 16
REMARK 465 PRO A 17
REMARK 465 ARG A 18
REMARK 465 PRO A 19
REMARK 465 ALA A 20
REMARK 465 PRO A 21
REMARK 465 LYS A 22
REMARK 465 TYR A 23
REMARK 465 GLN A 24
REMARK 465 ASP A 25
REMARK 465 VAL A 26
REMARK 465 PHE A 27
REMARK 465 SER A 28
REMARK 465 GLU A 29
REMARK 465 LYS A 30
REMARK 465 PRO A 31
REMARK 465 GLN A 32
REMARK 465 ALA A 33
REMARK 465 GLN A 34
REMARK 465 LYS A 35
REMARK 465 ASP A 36
REMARK 465 SER A 108
REMARK 465 ASN A 109
REMARK 465 HIS A 110
REMARK 465 GLN A 111
REMARK 465 ASN A 112
REMARK 465 GLY A 113
REMARK 465 ASN A 114
REMARK 465 THR A 115
REMARK 465 GLY A 116
REMARK 465 ASN A 117
REMARK 465 GLY A 118
REMARK 465 ILE A 119
REMARK 465 ASN A 120
REMARK 465 PRO A 351
REMARK 465 ALA A 352
REMARK 465 ASN A 353
REMARK 465 GLY A 354
REMARK 465 ASN A 355
REMARK 465 THR A 356
REMARK 465 ALA A 357
REMARK 465 ALA A 358
REMARK 465 ALA A 359
REMARK 465 SER A 360
REMARK 465 GLY A 361
REMARK 465 GLY A 362
REMARK 465 THR A 363
REMARK 465 ASP A 364
REMARK 465 ALA A 365
REMARK 465 ALA A 366
REMARK 465 ALA A 367
REMARK 465 SER A 368
REMARK 465 ASN A 369
REMARK 465 GLY A 370
REMARK 465 ALA A 371
REMARK 465 ALA A 372
REMARK 465 GLY A 373
REMARK 465 THR A 374
REMARK 465 SER A 375
REMARK 465 SER A 376
REMARK 465 GLU A 377
REMARK 465 ASN A 378
REMARK 465 GLY A 379
REMARK 465 GLU A 421
REMARK 465 ALA A 422
REMARK 465 SER A 423
REMARK 465 GLU A 424
REMARK 465 SER A 425
REMARK 465 GLY A 426
REMARK 465 ASN A 427
REMARK 465 ASN A 428
REMARK 465 GLN A 429
REMARK 465 ALA A 430
REMARK 465 ASN A 431
REMARK 465 GLN A 432
REMARK 465 GLY A 433
REMARK 465 THR A 434
REMARK 465 ASN A 435
REMARK 465 GLY A 436
REMARK 465 GLY A 437
REMARK 465 THR A 438
REMARK 465 GLU A 449
REMARK 465 SER A 450
REMARK 465 ASP A 451
REMARK 465 LYS A 452
REMARK 465 LYS A 453
REMARK 465 ASP A 454
REMARK 465 ALA A 455
REMARK 465 GLN A 456
REMARK 465 ALA A 457
REMARK 465 GLY A 458
REMARK 465 THR A 459
REMARK 465 GLN A 460
REMARK 465 THR A 461
REMARK 465 ASN A 462
REMARK 465 GLY A 463
REMARK 465 ALA A 464
REMARK 465 GLN A 465
REMARK 465 THR A 466
REMARK 465 ALA A 467
REMARK 465 SER A 468
REMARK 465 ASN A 469
REMARK 465 THR A 470
REMARK 465 ALA A 471
REMARK 465 GLY A 472
REMARK 465 ASP A 473
REMARK 465 THR A 474
REMARK 465 ASN A 475
REMARK 465 GLY A 476
REMARK 465 LYS A 477
REMARK 465 THR A 478
REMARK 465 SER A 503
REMARK 465 LYS A 504
REMARK 465 SER A 505
REMARK 465 ALA A 506
REMARK 465 MET A 507
REMARK 465 GLN A 508
REMARK 465 ALA A 509
REMARK 465 GLY A 510
REMARK 465 GLU A 511
REMARK 465 SER A 512
REMARK 465 SER A 513
REMARK 465 SER A 514
REMARK 465 GLN A 515
REMARK 465 ALA A 516
REMARK 465 ASP A 517
REMARK 465 ALA A 518
REMARK 465 LYS A 519
REMARK 465 THR A 520
REMARK 465 GLU A 521
REMARK 465 GLN A 522
REMARK 465 LYS A 665
REMARK 465 GLN A 666
REMARK 465 THR A 667
REMARK 465 LYS A 668
REMARK 465 ASN A 669
REMARK 465 ALA A 670
REMARK 465 THR A 671
REMARK 465 ASN A 672
REMARK 465 ALA A 673
REMARK 465 GLN A 689
REMARK 465 PRO A 690
REMARK 465 VAL A 691
REMARK 465 GLN A 692
REMARK 465 MET B -25
REMARK 465 SER B -24
REMARK 465 TYR B -23
REMARK 465 TYR B -22
REMARK 465 HIS B -21
REMARK 465 HIS B -20
REMARK 465 HIS B -19
REMARK 465 HIS B -18
REMARK 465 HIS B -17
REMARK 465 HIS B -16
REMARK 465 ASP B -15
REMARK 465 TYR B -14
REMARK 465 ASP B -13
REMARK 465 ILE B -12
REMARK 465 PRO B -11
REMARK 465 THR B -10
REMARK 465 THR B -9
REMARK 465 GLU B -8
REMARK 465 ASN B -7
REMARK 465 LEU B -6
REMARK 465 TYR B -5
REMARK 465 PHE B -4
REMARK 465 GLN B -3
REMARK 465 GLY B -2
REMARK 465 ALA B -1
REMARK 465 MET B 0
REMARK 465 LEU B 1
REMARK 465 GLY B 2
REMARK 465 GLY B 3
REMARK 465 GLY B 4
REMARK 465 GLY B 5
REMARK 465 SER B 6
REMARK 465 PHE B 7
REMARK 465 ASP B 8
REMARK 465 LEU B 9
REMARK 465 ASP B 10
REMARK 465 SER B 11
REMARK 465 VAL B 12
REMARK 465 ASP B 13
REMARK 465 THR B 14
REMARK 465 GLU B 15
REMARK 465 ALA B 16
REMARK 465 PRO B 17
REMARK 465 ARG B 18
REMARK 465 PRO B 19
REMARK 465 ALA B 20
REMARK 465 PRO B 21
REMARK 465 LYS B 22
REMARK 465 TYR B 23
REMARK 465 GLN B 24
REMARK 465 ASP B 25
REMARK 465 VAL B 26
REMARK 465 PHE B 27
REMARK 465 SER B 28
REMARK 465 GLU B 29
REMARK 465 LYS B 30
REMARK 465 PRO B 31
REMARK 465 GLN B 32
REMARK 465 ALA B 33
REMARK 465 GLN B 34
REMARK 465 LYS B 35
REMARK 465 ASP B 36
REMARK 465 SER B 108
REMARK 465 ASN B 109
REMARK 465 HIS B 110
REMARK 465 GLN B 111
REMARK 465 ASN B 112
REMARK 465 GLY B 113
REMARK 465 ASN B 114
REMARK 465 THR B 115
REMARK 465 GLY B 116
REMARK 465 ASN B 117
REMARK 465 GLY B 118
REMARK 465 ILE B 119
REMARK 465 ASN B 120
REMARK 465 PRO B 351
REMARK 465 ALA B 352
REMARK 465 ASN B 353
REMARK 465 GLY B 354
REMARK 465 ASN B 355
REMARK 465 THR B 356
REMARK 465 ALA B 357
REMARK 465 ALA B 358
REMARK 465 ALA B 359
REMARK 465 SER B 360
REMARK 465 GLY B 361
REMARK 465 GLY B 362
REMARK 465 THR B 363
REMARK 465 ASP B 364
REMARK 465 ALA B 365
REMARK 465 ALA B 366
REMARK 465 ALA B 367
REMARK 465 SER B 368
REMARK 465 ASN B 369
REMARK 465 GLY B 370
REMARK 465 ALA B 371
REMARK 465 ALA B 372
REMARK 465 GLY B 373
REMARK 465 THR B 374
REMARK 465 SER B 375
REMARK 465 SER B 376
REMARK 465 GLU B 377
REMARK 465 ASN B 378
REMARK 465 GLY B 379
REMARK 465 GLU B 421
REMARK 465 ALA B 422
REMARK 465 SER B 423
REMARK 465 GLU B 424
REMARK 465 SER B 425
REMARK 465 GLY B 426
REMARK 465 ASN B 427
REMARK 465 ASN B 428
REMARK 465 GLN B 429
REMARK 465 ALA B 430
REMARK 465 ASN B 431
REMARK 465 GLN B 432
REMARK 465 GLY B 433
REMARK 465 THR B 434
REMARK 465 ASN B 435
REMARK 465 GLY B 436
REMARK 465 GLY B 437
REMARK 465 THR B 438
REMARK 465 GLU B 449
REMARK 465 SER B 450
REMARK 465 ASP B 451
REMARK 465 LYS B 452
REMARK 465 LYS B 453
REMARK 465 ASP B 454
REMARK 465 ALA B 455
REMARK 465 GLN B 456
REMARK 465 ALA B 457
REMARK 465 GLY B 458
REMARK 465 THR B 459
REMARK 465 GLN B 460
REMARK 465 THR B 461
REMARK 465 ASN B 462
REMARK 465 GLY B 463
REMARK 465 ALA B 464
REMARK 465 GLN B 465
REMARK 465 THR B 466
REMARK 465 ALA B 467
REMARK 465 SER B 468
REMARK 465 ASN B 469
REMARK 465 THR B 470
REMARK 465 ALA B 471
REMARK 465 GLY B 472
REMARK 465 ASP B 473
REMARK 465 THR B 474
REMARK 465 ASN B 475
REMARK 465 GLY B 476
REMARK 465 LYS B 477
REMARK 465 THR B 478
REMARK 465 SER B 503
REMARK 465 LYS B 504
REMARK 465 SER B 505
REMARK 465 ALA B 506
REMARK 465 MET B 507
REMARK 465 GLN B 508
REMARK 465 ALA B 509
REMARK 465 GLY B 510
REMARK 465 GLU B 511
REMARK 465 SER B 512
REMARK 465 SER B 513
REMARK 465 SER B 514
REMARK 465 GLN B 515
REMARK 465 ALA B 516
REMARK 465 ASP B 517
REMARK 465 ALA B 518
REMARK 465 LYS B 519
REMARK 465 THR B 520
REMARK 465 GLU B 521
REMARK 465 GLN B 522
REMARK 465 LYS B 665
REMARK 465 GLN B 666
REMARK 465 THR B 667
REMARK 465 LYS B 668
REMARK 465 ASN B 669
REMARK 465 ALA B 670
REMARK 465 THR B 671
REMARK 465 ASN B 672
REMARK 465 ALA B 673
REMARK 465 GLN B 689
REMARK 465 PRO B 690
REMARK 465 VAL B 691
REMARK 465 GLN B 692
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLN A 37 CG CD OE1 NE2
REMARK 470 LYS A 89 CG CD CE NZ
REMARK 470 GLU A 91 CG CD OE1 OE2
REMARK 470 THR A 92 OG1 CG2
REMARK 470 ASP A 93 CG OD1 OD2
REMARK 470 GLU A 153 CG CD OE1 OE2
REMARK 470 LYS A 155 CG CD CE NZ
REMARK 470 GLN A 205 CG CD OE1 NE2
REMARK 470 LYS A 230 CG CD CE NZ
REMARK 470 ASN A 268 CG OD1 ND2
REMARK 470 ASN A 269 CG OD1 ND2
REMARK 470 GLN A 270 CG CD OE1 NE2
REMARK 470 GLN A 300 CG CD OE1 NE2
REMARK 470 ASN A 301 CG OD1 ND2
REMARK 470 SER A 302 OG
REMARK 470 ASP A 349 CG OD1 OD2
REMARK 470 LYS A 350 CG CD CE NZ
REMARK 470 LYS A 380 CG CD CE NZ
REMARK 470 LYS A 391 CG CD CE NZ
REMARK 470 ASP A 445 CG OD1 OD2
REMARK 470 LYS A 501 CG CD CE NZ
REMARK 470 ASN A 502 CG OD1 ND2
REMARK 470 GLN A 543 CG CD OE1 NE2
REMARK 470 ASP A 558 CG OD1 OD2
REMARK 470 ASP A 584 CG OD1 OD2
REMARK 470 ASP A 664 CG OD1 OD2
REMARK 470 SER A 674 OG
REMARK 470 GLN B 37 CG CD OE1 NE2
REMARK 470 GLU B 91 CG CD OE1 OE2
REMARK 470 THR B 92 OG1 CG2
REMARK 470 ASP B 93 CG OD1 OD2
REMARK 470 GLU B 153 CG CD OE1 OE2
REMARK 470 LYS B 155 CG CD CE NZ
REMARK 470 GLN B 205 CG CD OE1 NE2
REMARK 470 GLU B 224 CG CD OE1 OE2
REMARK 470 LYS B 230 CG CD CE NZ
REMARK 470 ASN B 268 CG OD1 ND2
REMARK 470 ASN B 269 CG OD1 ND2
REMARK 470 GLN B 270 CG CD OE1 NE2
REMARK 470 GLN B 300 CG CD OE1 NE2
REMARK 470 ASN B 301 CG OD1 ND2
REMARK 470 SER B 302 OG
REMARK 470 ASP B 349 CG OD1 OD2
REMARK 470 LYS B 350 CG CD CE NZ
REMARK 470 LYS B 380 CG CD CE NZ
REMARK 470 LYS B 391 CG CD CE NZ
REMARK 470 ASP B 445 CG OD1 OD2
REMARK 470 LYS B 501 CG CD CE NZ
REMARK 470 ASN B 502 CG OD1 ND2
REMARK 470 GLN B 543 CG CD OE1 NE2
REMARK 470 ASP B 558 CG OD1 OD2
REMARK 470 ASP B 584 CG OD1 OD2
REMARK 470 TYR B 637 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ASP B 664 CG OD1 OD2
REMARK 470 SER B 674 OG
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 NH1 ARG A 261 OD1 ASN A 263 2.11
REMARK 500 OG SER A 173 O GLY A 322 2.12
REMARK 500 O GLN B 205 N SER B 207 2.13
REMARK 500 O GLN A 205 N SER A 207 2.14
REMARK 500 OG SER B 173 O GLY B 322 2.16
REMARK 500 NH1 ARG B 261 OD1 ASN B 263 2.19
REMARK 500 O PRO A 53 N ALA A 55 2.19
REMARK 500 OD2 ASP B 412 NH2 ARG B 500 2.19
REMARK 500 OD2 ASP A 412 NH2 ARG A 500 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (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,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LEU B 625 N - CA - C ANGL. DEV. = -20.4 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
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 PRO A 53 -145.29 -71.49
REMARK 500 GLN A 54 -65.53 47.76
REMARK 500 ASP A 58 -30.01 62.53
REMARK 500 GLU A 91 59.92 -143.29
REMARK 500 THR A 92 -9.24 -167.02
REMARK 500 ASP A 93 -163.67 -58.81
REMARK 500 SER A 94 -79.80 40.38
REMARK 500 LYS A 127 94.69 63.37
REMARK 500 TYR A 129 51.74 -158.98
REMARK 500 GLU A 130 -99.35 164.31
REMARK 500 LYS A 155 107.25 16.41
REMARK 500 GLU A 171 68.43 66.30
REMARK 500 LYS A 195 -93.78 -145.88
REMARK 500 LYS A 196 19.03 -140.00
REMARK 500 ILE A 204 160.58 -48.23
REMARK 500 GLN A 205 97.00 -7.64
REMARK 500 PRO A 206 46.63 -33.23
REMARK 500 SER A 209 44.70 72.62
REMARK 500 ASP A 212 -64.67 -107.43
REMARK 500 SER A 218 -32.39 -25.81
REMARK 500 GLU A 223 98.15 -163.67
REMARK 500 THR A 234 -27.40 -31.21
REMARK 500 ASP A 235 -3.47 79.89
REMARK 500 GLN A 237 -146.63 65.85
REMARK 500 GLU A 238 -69.14 76.66
REMARK 500 THR A 266 40.52 -99.13
REMARK 500 ASP A 267 -140.01 -76.87
REMARK 500 ASN A 268 -137.59 35.71
REMARK 500 ALA A 271 -57.01 -172.17
REMARK 500 THR A 272 -37.53 105.45
REMARK 500 ASP A 296 63.63 -105.88
REMARK 500 PRO A 298 96.11 -63.38
REMARK 500 ASN A 301 -7.11 59.97
REMARK 500 LYS A 346 -137.73 -129.14
REMARK 500 LYS A 348 -144.27 -58.87
REMARK 500 ASP A 349 -45.32 -163.34
REMARK 500 PHE A 403 45.20 -101.98
REMARK 500 THR A 480 100.47 76.15
REMARK 500 LYS A 501 -151.73 -102.25
REMARK 500 PRO A 540 170.11 -59.93
REMARK 500 ASN A 544 82.65 50.02
REMARK 500 SER A 560 -110.26 -106.77
REMARK 500 ALA A 583 -50.32 77.71
REMARK 500 ASP A 609 -111.90 58.09
REMARK 500 THR A 633 -75.21 -128.33
REMARK 500 PRO A 634 -121.18 -57.15
REMARK 500 LYS A 635 97.39 161.83
REMARK 500 THR A 639 -133.40 -71.94
REMARK 500 PRO A 650 -73.06 -15.23
REMARK 500 PRO B 53 -146.75 -71.69
REMARK 500
REMARK 500 THIS ENTRY HAS 99 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 VAL A 90 GLU A 91 -112.69
REMARK 500 THR A 92 ASP A 93 -106.36
REMARK 500 ASP A 624 LEU A 625 -128.90
REMARK 500 THR A 633 PRO A 634 -148.09
REMARK 500 PRO A 634 LYS A 635 66.23
REMARK 500 GLY A 649 PRO A 650 -131.30
REMARK 500 VAL B 90 GLU B 91 -79.08
REMARK 500 THR B 92 ASP B 93 -58.68
REMARK 500 ASP B 624 LEU B 625 -89.99
REMARK 500 THR B 633 PRO B 634 -148.11
REMARK 500 PRO B 634 LYS B 635 119.40
REMARK 500 GLY B 649 PRO B 650 -80.78
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 THR A 633 24.6 L L OUTSIDE RANGE
REMARK 500 THR B 633 24.8 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3V83 RELATED DB: PDB
REMARK 900 RELATED ID: 3V89 RELATED DB: PDB
REMARK 900 RELATED ID: 3V8X RELATED DB: PDB
DBREF 3V8U A 1 692 UNP Q9JPI9 Q9JPI9_NEIME 22 712
DBREF 3V8U B 1 692 UNP Q9JPI9 Q9JPI9_NEIME 22 712
SEQADV 3V8U MET A -25 UNP Q9JPI9 EXPRESSION TAG
SEQADV 3V8U SER A -24 UNP Q9JPI9 EXPRESSION TAG
SEQADV 3V8U TYR A -23 UNP Q9JPI9 EXPRESSION TAG
SEQADV 3V8U TYR A -22 UNP Q9JPI9 EXPRESSION TAG
SEQADV 3V8U HIS A -21 UNP Q9JPI9 EXPRESSION TAG
SEQADV 3V8U HIS A -20 UNP Q9JPI9 EXPRESSION TAG
SEQADV 3V8U HIS A -19 UNP Q9JPI9 EXPRESSION TAG
SEQADV 3V8U HIS A -18 UNP Q9JPI9 EXPRESSION TAG
SEQADV 3V8U HIS A -17 UNP Q9JPI9 EXPRESSION TAG
SEQADV 3V8U HIS A -16 UNP Q9JPI9 EXPRESSION TAG
SEQADV 3V8U ASP A -15 UNP Q9JPI9 EXPRESSION TAG
SEQADV 3V8U TYR A -14 UNP Q9JPI9 EXPRESSION TAG
SEQADV 3V8U ASP A -13 UNP Q9JPI9 EXPRESSION TAG
SEQADV 3V8U ILE A -12 UNP Q9JPI9 EXPRESSION TAG
SEQADV 3V8U PRO A -11 UNP Q9JPI9 EXPRESSION TAG
SEQADV 3V8U THR A -10 UNP Q9JPI9 EXPRESSION TAG
SEQADV 3V8U THR A -9 UNP Q9JPI9 EXPRESSION TAG
SEQADV 3V8U GLU A -8 UNP Q9JPI9 EXPRESSION TAG
SEQADV 3V8U ASN A -7 UNP Q9JPI9 EXPRESSION TAG
SEQADV 3V8U LEU A -6 UNP Q9JPI9 EXPRESSION TAG
SEQADV 3V8U TYR A -5 UNP Q9JPI9 EXPRESSION TAG
SEQADV 3V8U PHE A -4 UNP Q9JPI9 EXPRESSION TAG
SEQADV 3V8U GLN A -3 UNP Q9JPI9 EXPRESSION TAG
SEQADV 3V8U GLY A -2 UNP Q9JPI9 EXPRESSION TAG
SEQADV 3V8U ALA A -1 UNP Q9JPI9 EXPRESSION TAG
SEQADV 3V8U MET A 0 UNP Q9JPI9 EXPRESSION TAG
SEQADV 3V8U MET B -25 UNP Q9JPI9 EXPRESSION TAG
SEQADV 3V8U SER B -24 UNP Q9JPI9 EXPRESSION TAG
SEQADV 3V8U TYR B -23 UNP Q9JPI9 EXPRESSION TAG
SEQADV 3V8U TYR B -22 UNP Q9JPI9 EXPRESSION TAG
SEQADV 3V8U HIS B -21 UNP Q9JPI9 EXPRESSION TAG
SEQADV 3V8U HIS B -20 UNP Q9JPI9 EXPRESSION TAG
SEQADV 3V8U HIS B -19 UNP Q9JPI9 EXPRESSION TAG
SEQADV 3V8U HIS B -18 UNP Q9JPI9 EXPRESSION TAG
SEQADV 3V8U HIS B -17 UNP Q9JPI9 EXPRESSION TAG
SEQADV 3V8U HIS B -16 UNP Q9JPI9 EXPRESSION TAG
SEQADV 3V8U ASP B -15 UNP Q9JPI9 EXPRESSION TAG
SEQADV 3V8U TYR B -14 UNP Q9JPI9 EXPRESSION TAG
SEQADV 3V8U ASP B -13 UNP Q9JPI9 EXPRESSION TAG
SEQADV 3V8U ILE B -12 UNP Q9JPI9 EXPRESSION TAG
SEQADV 3V8U PRO B -11 UNP Q9JPI9 EXPRESSION TAG
SEQADV 3V8U THR B -10 UNP Q9JPI9 EXPRESSION TAG
SEQADV 3V8U THR B -9 UNP Q9JPI9 EXPRESSION TAG
SEQADV 3V8U GLU B -8 UNP Q9JPI9 EXPRESSION TAG
SEQADV 3V8U ASN B -7 UNP Q9JPI9 EXPRESSION TAG
SEQADV 3V8U LEU B -6 UNP Q9JPI9 EXPRESSION TAG
SEQADV 3V8U TYR B -5 UNP Q9JPI9 EXPRESSION TAG
SEQADV 3V8U PHE B -4 UNP Q9JPI9 EXPRESSION TAG
SEQADV 3V8U GLN B -3 UNP Q9JPI9 EXPRESSION TAG
SEQADV 3V8U GLY B -2 UNP Q9JPI9 EXPRESSION TAG
SEQADV 3V8U ALA B -1 UNP Q9JPI9 EXPRESSION TAG
SEQADV 3V8U MET B 0 UNP Q9JPI9 EXPRESSION TAG
SEQRES 1 A 717 MET SER TYR TYR HIS HIS HIS HIS HIS HIS ASP TYR ASP
SEQRES 2 A 717 ILE PRO THR THR GLU ASN LEU TYR PHE GLN GLY ALA MET
SEQRES 3 A 717 LEU GLY GLY GLY GLY SER PHE ASP LEU ASP SER VAL ASP
SEQRES 4 A 717 THR GLU ALA PRO ARG PRO ALA PRO LYS TYR GLN ASP VAL
SEQRES 5 A 717 PHE SER GLU LYS PRO GLN ALA GLN LYS ASP GLN GLY GLY
SEQRES 6 A 717 TYR GLY PHE ALA MET ARG LEU LYS ARG ARG ASN TRP TYR
SEQRES 7 A 717 PRO GLN ALA LYS GLU ASP GLU VAL LYS LEU ASP GLU SER
SEQRES 8 A 717 ASP TRP GLU ALA THR GLY LEU PRO ASP GLU PRO LYS GLU
SEQRES 9 A 717 LEU PRO LYS ARG GLN LYS SER VAL ILE GLU LYS VAL GLU
SEQRES 10 A 717 THR ASP SER ASP ASN ASN ILE TYR SER SER PRO TYR LEU
SEQRES 11 A 717 LYS PRO SER ASN HIS GLN ASN GLY ASN THR GLY ASN GLY
SEQRES 12 A 717 ILE ASN GLN PRO LYS ASN GLN ALA LYS ASP TYR GLU ASN
SEQRES 13 A 717 PHE LYS TYR VAL TYR SER GLY TRP PHE TYR LYS HIS ALA
SEQRES 14 A 717 LYS ARG GLU PHE ASN LEU LYS VAL GLU PRO LYS SER ALA
SEQRES 15 A 717 LYS ASN GLY ASP ASP GLY TYR ILE PHE TYR HIS GLY LYS
SEQRES 16 A 717 GLU PRO SER ARG GLN LEU PRO ALA SER GLY LYS ILE THR
SEQRES 17 A 717 TYR LYS GLY VAL TRP HIS PHE ALA THR ASP THR LYS LYS
SEQRES 18 A 717 GLY GLN LYS PHE ARG GLU ILE ILE GLN PRO SER LYS SER
SEQRES 19 A 717 GLN GLY ASP ARG TYR SER GLY PHE SER GLY ASP ASP GLY
SEQRES 20 A 717 GLU GLU TYR SER ASN LYS ASN LYS SER THR LEU THR ASP
SEQRES 21 A 717 GLY GLN GLU GLY TYR GLY PHE THR SER ASN LEU GLU VAL
SEQRES 22 A 717 ASP PHE HIS ASN LYS LYS LEU THR GLY LYS LEU ILE ARG
SEQRES 23 A 717 ASN ASN ALA ASN THR ASP ASN ASN GLN ALA THR THR THR
SEQRES 24 A 717 GLN TYR TYR SER LEU GLU ALA GLN VAL THR GLY ASN ARG
SEQRES 25 A 717 PHE ASN GLY LYS ALA THR ALA THR ASP LYS PRO GLN GLN
SEQRES 26 A 717 ASN SER GLU THR LYS GLU HIS PRO PHE VAL SER ASP SER
SEQRES 27 A 717 SER SER LEU SER GLY GLY PHE PHE GLY PRO GLN GLY GLU
SEQRES 28 A 717 GLU LEU GLY PHE ARG PHE LEU SER ASP ASP GLN LYS VAL
SEQRES 29 A 717 ALA VAL VAL GLY SER ALA LYS THR LYS ASP LYS PRO ALA
SEQRES 30 A 717 ASN GLY ASN THR ALA ALA ALA SER GLY GLY THR ASP ALA
SEQRES 31 A 717 ALA ALA SER ASN GLY ALA ALA GLY THR SER SER GLU ASN
SEQRES 32 A 717 GLY LYS LEU THR THR VAL LEU ASP ALA VAL GLU LEU LYS
SEQRES 33 A 717 LEU GLY ASP LYS LYS VAL GLN LYS LEU ASP ASN PHE SER
SEQRES 34 A 717 ASN ALA ALA GLN LEU VAL VAL ASP GLY ILE MET ILE PRO
SEQRES 35 A 717 LEU LEU PRO GLU ALA SER GLU SER GLY ASN ASN GLN ALA
SEQRES 36 A 717 ASN GLN GLY THR ASN GLY GLY THR ALA PHE THR ARG LYS
SEQRES 37 A 717 PHE ASP HIS THR PRO GLU SER ASP LYS LYS ASP ALA GLN
SEQRES 38 A 717 ALA GLY THR GLN THR ASN GLY ALA GLN THR ALA SER ASN
SEQRES 39 A 717 THR ALA GLY ASP THR ASN GLY LYS THR LYS THR TYR GLU
SEQRES 40 A 717 VAL GLU VAL CYS CYS SER ASN LEU ASN TYR LEU LYS TYR
SEQRES 41 A 717 GLY MET LEU THR ARG LYS ASN SER LYS SER ALA MET GLN
SEQRES 42 A 717 ALA GLY GLU SER SER SER GLN ALA ASP ALA LYS THR GLU
SEQRES 43 A 717 GLN VAL GLU GLN SER MET PHE LEU GLN GLY GLU ARG THR
SEQRES 44 A 717 ASP GLU LYS GLU ILE PRO SER GLU GLN ASN ILE VAL TYR
SEQRES 45 A 717 ARG GLY SER TRP TYR GLY TYR ILE ALA ASN ASP LYS SER
SEQRES 46 A 717 THR SER TRP SER GLY ASN ALA SER ASN ALA THR SER GLY
SEQRES 47 A 717 ASN ARG ALA GLU PHE THR VAL ASN PHE ALA ASP LYS LYS
SEQRES 48 A 717 ILE THR GLY THR LEU THR ALA ASP ASN ARG GLN GLU ALA
SEQRES 49 A 717 THR PHE THR ILE ASP GLY ASN ILE LYS ASP ASN GLY PHE
SEQRES 50 A 717 GLU GLY THR ALA LYS THR ALA GLU SER GLY PHE ASP LEU
SEQRES 51 A 717 ASP GLN SER ASN THR THR ARG THR PRO LYS ALA TYR ILE
SEQRES 52 A 717 THR ASP ALA LYS VAL GLN GLY GLY PHE TYR GLY PRO LYS
SEQRES 53 A 717 ALA GLU GLU LEU GLY GLY TRP PHE ALA TYR PRO GLY ASP
SEQRES 54 A 717 LYS GLN THR LYS ASN ALA THR ASN ALA SER GLY ASN SER
SEQRES 55 A 717 SER ALA THR VAL VAL PHE GLY ALA LYS ARG GLN GLN PRO
SEQRES 56 A 717 VAL GLN
SEQRES 1 B 717 MET SER TYR TYR HIS HIS HIS HIS HIS HIS ASP TYR ASP
SEQRES 2 B 717 ILE PRO THR THR GLU ASN LEU TYR PHE GLN GLY ALA MET
SEQRES 3 B 717 LEU GLY GLY GLY GLY SER PHE ASP LEU ASP SER VAL ASP
SEQRES 4 B 717 THR GLU ALA PRO ARG PRO ALA PRO LYS TYR GLN ASP VAL
SEQRES 5 B 717 PHE SER GLU LYS PRO GLN ALA GLN LYS ASP GLN GLY GLY
SEQRES 6 B 717 TYR GLY PHE ALA MET ARG LEU LYS ARG ARG ASN TRP TYR
SEQRES 7 B 717 PRO GLN ALA LYS GLU ASP GLU VAL LYS LEU ASP GLU SER
SEQRES 8 B 717 ASP TRP GLU ALA THR GLY LEU PRO ASP GLU PRO LYS GLU
SEQRES 9 B 717 LEU PRO LYS ARG GLN LYS SER VAL ILE GLU LYS VAL GLU
SEQRES 10 B 717 THR ASP SER ASP ASN ASN ILE TYR SER SER PRO TYR LEU
SEQRES 11 B 717 LYS PRO SER ASN HIS GLN ASN GLY ASN THR GLY ASN GLY
SEQRES 12 B 717 ILE ASN GLN PRO LYS ASN GLN ALA LYS ASP TYR GLU ASN
SEQRES 13 B 717 PHE LYS TYR VAL TYR SER GLY TRP PHE TYR LYS HIS ALA
SEQRES 14 B 717 LYS ARG GLU PHE ASN LEU LYS VAL GLU PRO LYS SER ALA
SEQRES 15 B 717 LYS ASN GLY ASP ASP GLY TYR ILE PHE TYR HIS GLY LYS
SEQRES 16 B 717 GLU PRO SER ARG GLN LEU PRO ALA SER GLY LYS ILE THR
SEQRES 17 B 717 TYR LYS GLY VAL TRP HIS PHE ALA THR ASP THR LYS LYS
SEQRES 18 B 717 GLY GLN LYS PHE ARG GLU ILE ILE GLN PRO SER LYS SER
SEQRES 19 B 717 GLN GLY ASP ARG TYR SER GLY PHE SER GLY ASP ASP GLY
SEQRES 20 B 717 GLU GLU TYR SER ASN LYS ASN LYS SER THR LEU THR ASP
SEQRES 21 B 717 GLY GLN GLU GLY TYR GLY PHE THR SER ASN LEU GLU VAL
SEQRES 22 B 717 ASP PHE HIS ASN LYS LYS LEU THR GLY LYS LEU ILE ARG
SEQRES 23 B 717 ASN ASN ALA ASN THR ASP ASN ASN GLN ALA THR THR THR
SEQRES 24 B 717 GLN TYR TYR SER LEU GLU ALA GLN VAL THR GLY ASN ARG
SEQRES 25 B 717 PHE ASN GLY LYS ALA THR ALA THR ASP LYS PRO GLN GLN
SEQRES 26 B 717 ASN SER GLU THR LYS GLU HIS PRO PHE VAL SER ASP SER
SEQRES 27 B 717 SER SER LEU SER GLY GLY PHE PHE GLY PRO GLN GLY GLU
SEQRES 28 B 717 GLU LEU GLY PHE ARG PHE LEU SER ASP ASP GLN LYS VAL
SEQRES 29 B 717 ALA VAL VAL GLY SER ALA LYS THR LYS ASP LYS PRO ALA
SEQRES 30 B 717 ASN GLY ASN THR ALA ALA ALA SER GLY GLY THR ASP ALA
SEQRES 31 B 717 ALA ALA SER ASN GLY ALA ALA GLY THR SER SER GLU ASN
SEQRES 32 B 717 GLY LYS LEU THR THR VAL LEU ASP ALA VAL GLU LEU LYS
SEQRES 33 B 717 LEU GLY ASP LYS LYS VAL GLN LYS LEU ASP ASN PHE SER
SEQRES 34 B 717 ASN ALA ALA GLN LEU VAL VAL ASP GLY ILE MET ILE PRO
SEQRES 35 B 717 LEU LEU PRO GLU ALA SER GLU SER GLY ASN ASN GLN ALA
SEQRES 36 B 717 ASN GLN GLY THR ASN GLY GLY THR ALA PHE THR ARG LYS
SEQRES 37 B 717 PHE ASP HIS THR PRO GLU SER ASP LYS LYS ASP ALA GLN
SEQRES 38 B 717 ALA GLY THR GLN THR ASN GLY ALA GLN THR ALA SER ASN
SEQRES 39 B 717 THR ALA GLY ASP THR ASN GLY LYS THR LYS THR TYR GLU
SEQRES 40 B 717 VAL GLU VAL CYS CYS SER ASN LEU ASN TYR LEU LYS TYR
SEQRES 41 B 717 GLY MET LEU THR ARG LYS ASN SER LYS SER ALA MET GLN
SEQRES 42 B 717 ALA GLY GLU SER SER SER GLN ALA ASP ALA LYS THR GLU
SEQRES 43 B 717 GLN VAL GLU GLN SER MET PHE LEU GLN GLY GLU ARG THR
SEQRES 44 B 717 ASP GLU LYS GLU ILE PRO SER GLU GLN ASN ILE VAL TYR
SEQRES 45 B 717 ARG GLY SER TRP TYR GLY TYR ILE ALA ASN ASP LYS SER
SEQRES 46 B 717 THR SER TRP SER GLY ASN ALA SER ASN ALA THR SER GLY
SEQRES 47 B 717 ASN ARG ALA GLU PHE THR VAL ASN PHE ALA ASP LYS LYS
SEQRES 48 B 717 ILE THR GLY THR LEU THR ALA ASP ASN ARG GLN GLU ALA
SEQRES 49 B 717 THR PHE THR ILE ASP GLY ASN ILE LYS ASP ASN GLY PHE
SEQRES 50 B 717 GLU GLY THR ALA LYS THR ALA GLU SER GLY PHE ASP LEU
SEQRES 51 B 717 ASP GLN SER ASN THR THR ARG THR PRO LYS ALA TYR ILE
SEQRES 52 B 717 THR ASP ALA LYS VAL GLN GLY GLY PHE TYR GLY PRO LYS
SEQRES 53 B 717 ALA GLU GLU LEU GLY GLY TRP PHE ALA TYR PRO GLY ASP
SEQRES 54 B 717 LYS GLN THR LYS ASN ALA THR ASN ALA SER GLY ASN SER
SEQRES 55 B 717 SER ALA THR VAL VAL PHE GLY ALA LYS ARG GLN GLN PRO
SEQRES 56 B 717 VAL GLN
FORMUL 3 HOH *147(H2 O)
HELIX 1 1 ASP A 63 TRP A 67 5 5
HELIX 2 2 PRO A 80 LYS A 89 1 10
HELIX 3 3 ASP B 63 TRP B 67 5 5
HELIX 4 4 PRO B 80 LYS B 89 1 10
SHEET 1 A 5 GLU A 68 ALA A 69 0
SHEET 2 A 5 GLY A 41 ARG A 45 -1 N ALA A 43 O GLU A 68
SHEET 3 A 5 SER A 156 GLY A 169 -1 O ILE A 165 N MET A 44
SHEET 4 A 5 VAL A 135 ASN A 149 -1 N GLU A 147 O LYS A 158
SHEET 5 A 5 TYR A 99 SER A 100 -1 N TYR A 99 O TYR A 141
SHEET 1 B 2 GLN A 175 PRO A 177 0
SHEET 2 B 2 LEU A 381 THR A 383 -1 O THR A 382 N LEU A 176
SHEET 1 C 9 LYS A 181 THR A 192 0
SHEET 2 C 9 PHE A 242 ASP A 249 -1 O LEU A 246 N TYR A 184
SHEET 3 C 9 LYS A 254 ARG A 261 -1 O LYS A 254 N ASP A 249
SHEET 4 C 9 TYR A 277 THR A 284 -1 O ALA A 281 N LEU A 255
SHEET 5 C 9 ARG A 287 ALA A 294 -1 O THR A 293 N SER A 278
SHEET 6 C 9 SER A 313 PHE A 321 -1 O SER A 313 N ALA A 292
SHEET 7 C 9 GLU A 327 LEU A 333 -1 O ARG A 331 N SER A 317
SHEET 8 C 9 VAL A 339 ALA A 345 -1 O VAL A 341 N PHE A 332
SHEET 9 C 9 LYS A 181 THR A 192 -1 N HIS A 189 O VAL A 342
SHEET 1 D 6 VAL A 397 LYS A 399 0
SHEET 2 D 6 LEU A 385 LYS A 391 -1 N GLU A 389 O GLN A 398
SHEET 3 D 6 GLU A 524 GLU A 532 -1 O MET A 527 N LEU A 390
SHEET 4 D 6 LEU A 493 ARG A 500 -1 N LYS A 494 O GLN A 530
SHEET 5 D 6 TYR A 481 CYS A 486 -1 N GLU A 482 O THR A 499
SHEET 6 D 6 THR A 441 HIS A 446 -1 N ARG A 442 O VAL A 485
SHEET 1 E 2 GLN A 408 VAL A 411 0
SHEET 2 E 2 ILE A 414 PRO A 417 -1 O ILE A 416 N LEU A 409
SHEET 1 F10 SER A 562 GLY A 565 0
SHEET 2 F10 ILE A 545 ASN A 557 -1 N ILE A 555 O TRP A 563
SHEET 3 F10 SER A 677 ARG A 687 -1 O VAL A 682 N TYR A 552
SHEET 4 F10 GLU A 654 TYR A 661 -1 N TYR A 661 O ALA A 679
SHEET 5 F10 ALA A 641 TYR A 648 -1 N TYR A 648 O GLU A 654
SHEET 6 F10 GLY A 611 LYS A 617 -1 N GLY A 614 O VAL A 643
SHEET 7 F10 PHE A 601 LYS A 608 -1 N ASN A 606 O GLU A 613
SHEET 8 F10 LYS A 586 THR A 592 -1 N LEU A 591 O PHE A 601
SHEET 9 F10 ARG A 575 ASN A 581 -1 N THR A 579 O THR A 588
SHEET 10 F10 ILE A 545 ASN A 557 -1 N ILE A 545 O VAL A 580
SHEET 1 G 5 GLU B 68 ALA B 69 0
SHEET 2 G 5 GLY B 41 ARG B 45 -1 N ALA B 43 O GLU B 68
SHEET 3 G 5 SER B 156 GLY B 169 -1 O ILE B 165 N MET B 44
SHEET 4 G 5 VAL B 135 ASN B 149 -1 N GLU B 147 O LYS B 158
SHEET 5 G 5 TYR B 99 SER B 100 -1 N TYR B 99 O TYR B 141
SHEET 1 H 2 GLN B 175 PRO B 177 0
SHEET 2 H 2 LEU B 381 THR B 383 -1 O THR B 382 N LEU B 176
SHEET 1 I 9 LYS B 181 THR B 192 0
SHEET 2 I 9 PHE B 242 ASP B 249 -1 O LEU B 246 N TYR B 184
SHEET 3 I 9 LYS B 254 ARG B 261 -1 O LYS B 254 N ASP B 249
SHEET 4 I 9 TYR B 277 THR B 284 -1 O ALA B 281 N LEU B 255
SHEET 5 I 9 ARG B 287 ALA B 294 -1 O THR B 293 N SER B 278
SHEET 6 I 9 SER B 313 PHE B 321 -1 O SER B 313 N ALA B 292
SHEET 7 I 9 GLU B 327 LEU B 333 -1 O ARG B 331 N SER B 317
SHEET 8 I 9 VAL B 339 ALA B 345 -1 O VAL B 341 N PHE B 332
SHEET 9 I 9 LYS B 181 THR B 192 -1 N HIS B 189 O VAL B 342
SHEET 1 J 6 VAL B 397 LYS B 399 0
SHEET 2 J 6 LEU B 385 LYS B 391 -1 N GLU B 389 O GLN B 398
SHEET 3 J 6 GLU B 524 GLU B 532 -1 O MET B 527 N LEU B 390
SHEET 4 J 6 LEU B 493 ARG B 500 -1 N LYS B 494 O GLN B 530
SHEET 5 J 6 TYR B 481 CYS B 486 -1 N GLU B 482 O THR B 499
SHEET 6 J 6 THR B 441 HIS B 446 -1 N ARG B 442 O VAL B 485
SHEET 1 K 2 GLN B 408 VAL B 411 0
SHEET 2 K 2 ILE B 414 PRO B 417 -1 O ILE B 416 N LEU B 409
SHEET 1 L10 SER B 562 GLY B 565 0
SHEET 2 L10 ILE B 545 ASN B 557 -1 N ILE B 555 O TRP B 563
SHEET 3 L10 SER B 677 ARG B 687 -1 O VAL B 682 N TYR B 552
SHEET 4 L10 GLU B 654 TYR B 661 -1 N TYR B 661 O ALA B 679
SHEET 5 L10 ALA B 641 TYR B 648 -1 N TYR B 648 O GLU B 654
SHEET 6 L10 GLY B 611 LYS B 617 -1 N GLY B 614 O VAL B 643
SHEET 7 L10 PHE B 601 LYS B 608 -1 N ASN B 606 O GLU B 613
SHEET 8 L10 LYS B 586 THR B 592 -1 N GLY B 589 O ILE B 603
SHEET 9 L10 ARG B 575 ASN B 581 -1 N THR B 579 O THR B 588
SHEET 10 L10 ILE B 545 ASN B 557 -1 N ILE B 545 O VAL B 580
SSBOND 1 CYS A 486 CYS A 487 1555 1555 2.04
SSBOND 2 CYS B 486 CYS B 487 1555 1555 2.04
CISPEP 1 GLU A 91 THR A 92 0 -5.14
CISPEP 2 TYR A 129 GLU A 130 0 -11.53
CISPEP 3 GLU A 153 PRO A 154 0 2.53
CISPEP 4 GLY A 197 GLN A 198 0 -0.94
CISPEP 5 ASP A 221 GLY A 222 0 10.21
CISPEP 6 GLN A 270 ALA A 271 0 13.97
CISPEP 7 LEU A 392 GLY A 393 0 -4.41
CISPEP 8 CYS A 486 CYS A 487 0 -1.37
CISPEP 9 TYR A 661 PRO A 662 0 -3.51
CISPEP 10 GLU B 91 THR B 92 0 -6.12
CISPEP 11 TYR B 129 GLU B 130 0 -9.63
CISPEP 12 GLU B 153 PRO B 154 0 2.86
CISPEP 13 GLY B 197 GLN B 198 0 -1.77
CISPEP 14 ASP B 221 GLY B 222 0 8.82
CISPEP 15 GLN B 270 ALA B 271 0 13.68
CISPEP 16 LEU B 392 GLY B 393 0 -4.28
CISPEP 17 CYS B 486 CYS B 487 0 -0.79
CISPEP 18 TYR B 661 PRO B 662 0 -6.95
CRYST1 75.030 82.133 111.314 90.00 106.07 90.00 P 1 21 1 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 0.013328 0.000000 0.003839 0.00000
SCALE2 0.000000 0.012175 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009349 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
