HEADER TRANSPORT PROTEIN 06-JAN-12 3VE1
TITLE THE 2.9 ANGSTROM CRYSTAL STRUCTURE OF TRANSFERRIN BINDING PROTEIN B
TITLE 2 (TBPB) FROM SEROGROUP B M982 NEISSERIA MENINGITIDIS IN COMPLEX WITH
TITLE 3 HUMAN TRANSFERRIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSFERRIN-BINDING PROTEIN 2;
COMPND 3 CHAIN: A, C;
COMPND 4 SYNONYM: TBP-2;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: SEROTRANSFERRIN;
COMPND 8 CHAIN: B, D;
COMPND 9 SYNONYM: TRANSFERRIN, BETA-1 METAL-BINDING GLOBULIN, SIDEROPHILIN;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: NEISSERIA MENINGITIDIS SEROGROUP B;
SOURCE 3 ORGANISM_TAXID: 491;
SOURCE 4 STRAIN: M982;
SOURCE 5 GENE: TBPB, TBP2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: TF, PRO1400;
SOURCE 16 EXPRESSION_SYSTEM: PICHIA PASTORIS
KEYWDS TRANSFERRIN RECEPTOR, IRON ACQUISITION, VACCINE CANDIDATE, PROTEIN-
KEYWDS 2 PROTEIN COMPLEX, HOST PATHOGEN INTERACTION, RECEPTOR, TRANSFERRIN,
KEYWDS 3 LIPOPROTEIN, OUTERMEMBRANE PROTEIN, TRANSPORT PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR C.CALMETTES,T.F.MORAES
REVDAT 3 18-SEP-13 3VE1 1 REMARK
REVDAT 2 05-SEP-12 3VE1 1 JRNL
REVDAT 1 22-FEB-12 3VE1 0
JRNL AUTH C.CALMETTES,J.ALCANTARA,R.H.YU,A.B.SCHRYVERS,T.F.MORAES
JRNL TITL THE STRUCTURAL BASIS OF TRANSFERRIN SEQUESTRATION BY
JRNL TITL 2 TRANSFERRIN-BINDING PROTEIN B.
JRNL REF NAT.STRUCT.MOL.BIOL. V. 19 358 2012
JRNL REFN ISSN 1545-9993
JRNL PMID 22343719
JRNL DOI 10.1038/NSMB.2251
REMARK 2
REMARK 2 RESOLUTION. 2.96 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7.1_743)
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) : 2.96
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.93
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 70132
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.209
REMARK 3 R VALUE (WORKING SET) : 0.207
REMARK 3 FREE R VALUE : 0.249
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.560
REMARK 3 FREE R VALUE TEST SET COUNT : 2497
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 37.9314 - 7.7261 0.98 3956 146 0.1916 0.2029
REMARK 3 2 7.7261 - 6.1409 1.00 3853 143 0.2018 0.2338
REMARK 3 3 6.1409 - 5.3671 1.00 3833 141 0.2111 0.2827
REMARK 3 4 5.3671 - 4.8775 1.00 3793 141 0.1827 0.2081
REMARK 3 5 4.8775 - 4.5285 1.00 3785 139 0.1562 0.1774
REMARK 3 6 4.5285 - 4.2619 1.00 3765 139 0.1665 0.2070
REMARK 3 7 4.2619 - 4.0487 1.00 3789 140 0.1770 0.2049
REMARK 3 8 4.0487 - 3.8726 1.00 3748 138 0.1936 0.2542
REMARK 3 9 3.8726 - 3.7237 1.00 3761 140 0.2097 0.2835
REMARK 3 10 3.7237 - 3.5953 1.00 3739 138 0.2174 0.2513
REMARK 3 11 3.5953 - 3.4829 1.00 3751 138 0.2192 0.2679
REMARK 3 12 3.4829 - 3.3834 1.00 3740 138 0.2278 0.2956
REMARK 3 13 3.3834 - 3.2944 1.00 3753 139 0.2368 0.2889
REMARK 3 14 3.2944 - 3.2141 1.00 3710 136 0.2530 0.2948
REMARK 3 15 3.2141 - 3.1411 1.00 3735 138 0.2712 0.3106
REMARK 3 16 3.1411 - 3.0742 1.00 3716 138 0.2813 0.3620
REMARK 3 17 3.0742 - 3.0128 1.00 3726 138 0.2980 0.3590
REMARK 3 18 3.0128 - 2.9559 0.93 3482 127 0.3170 0.4040
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.00
REMARK 3 SHRINKAGE RADIUS : 0.72
REMARK 3 K_SOL : 0.33
REMARK 3 B_SOL : 40.62
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.860
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.830
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 68.94
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.38530
REMARK 3 B22 (A**2) : -2.08570
REMARK 3 B33 (A**2) : -2.29960
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 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 19511
REMARK 3 ANGLE : 1.409 26242
REMARK 3 CHIRALITY : 0.105 2754
REMARK 3 PLANARITY : 0.006 3444
REMARK 3 DIHEDRAL : 16.643 7201
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 26
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (chain C and resid 38:106)
REMARK 3 ORIGIN FOR THE GROUP (A): 53.5754 -66.6188 -23.9779
REMARK 3 T TENSOR
REMARK 3 T11: 0.4233 T22: 0.4052
REMARK 3 T33: 0.4688 T12: 0.1102
REMARK 3 T13: -0.0563 T23: -0.2142
REMARK 3 L TENSOR
REMARK 3 L11: 4.8545 L22: 2.1108
REMARK 3 L33: 1.4758 L12: 2.6804
REMARK 3 L13: -1.4762 L23: -0.9948
REMARK 3 S TENSOR
REMARK 3 S11: 0.0469 S12: -0.3677 S13: -0.1812
REMARK 3 S21: 0.1597 S22: -0.0958 S23: -0.3319
REMARK 3 S31: 0.0084 S32: 0.0803 S33: 0.0116
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (chain C and resid 107:121)
REMARK 3 ORIGIN FOR THE GROUP (A): 41.9697 -50.9752 -31.4567
REMARK 3 T TENSOR
REMARK 3 T11: 0.6452 T22: 1.2833
REMARK 3 T33: 1.3375 T12: -0.1606
REMARK 3 T13: -0.0697 T23: -0.0067
REMARK 3 L TENSOR
REMARK 3 L11: 5.6472 L22: 7.8483
REMARK 3 L33: 3.1583 L12: 2.4644
REMARK 3 L13: -3.9407 L23: -3.3832
REMARK 3 S TENSOR
REMARK 3 S11: -0.9553 S12: 1.1664 S13: 1.6713
REMARK 3 S21: 0.2901 S22: -1.7154 S23: -1.4285
REMARK 3 S31: -1.0929 S32: 3.1714 S33: 2.4349
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (chain C and resid 122:262)
REMARK 3 ORIGIN FOR THE GROUP (A): 45.9703 -67.6817 -34.8124
REMARK 3 T TENSOR
REMARK 3 T11: 0.3586 T22: 0.3867
REMARK 3 T33: 0.3100 T12: 0.0978
REMARK 3 T13: 0.0253 T23: -0.1687
REMARK 3 L TENSOR
REMARK 3 L11: 1.6369 L22: 1.7509
REMARK 3 L33: 1.5802 L12: 0.8311
REMARK 3 L13: -0.5317 L23: -0.6093
REMARK 3 S TENSOR
REMARK 3 S11: -0.1000 S12: 0.2292 S13: 0.0222
REMARK 3 S21: -0.0600 S22: 0.1128 S23: -0.1501
REMARK 3 S31: 0.0809 S32: -0.1488 S33: -0.0179
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (chain C and resid 263:272)
REMARK 3 ORIGIN FOR THE GROUP (A): 43.7142 -59.2172 -55.8959
REMARK 3 T TENSOR
REMARK 3 T11: 1.3286 T22: 1.1596
REMARK 3 T33: 0.8880 T12: 0.0431
REMARK 3 T13: -0.2758 T23: -0.2193
REMARK 3 L TENSOR
REMARK 3 L11: 0.4392 L22: 5.4567
REMARK 3 L33: 9.5523 L12: 1.4151
REMARK 3 L13: -1.8628 L23: -7.2203
REMARK 3 S TENSOR
REMARK 3 S11: -0.1111 S12: 1.3958 S13: -0.0077
REMARK 3 S21: -1.7599 S22: -1.0761 S23: 1.2391
REMARK 3 S31: 1.1902 S32: 0.6109 S33: 0.8252
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (chain C and resid 273:349)
REMARK 3 ORIGIN FOR THE GROUP (A): 43.6636 -78.0253 -37.0430
REMARK 3 T TENSOR
REMARK 3 T11: 0.4509 T22: 0.4366
REMARK 3 T33: 0.4066 T12: -0.0269
REMARK 3 T13: 0.0009 T23: -0.2090
REMARK 3 L TENSOR
REMARK 3 L11: 2.0328 L22: 2.4302
REMARK 3 L33: 3.4676 L12: 0.1371
REMARK 3 L13: -1.0180 L23: 0.3050
REMARK 3 S TENSOR
REMARK 3 S11: -0.2300 S12: 0.4825 S13: -0.3784
REMARK 3 S21: -0.1219 S22: 0.1838 S23: -0.4751
REMARK 3 S31: 0.4176 S32: 0.0513 S33: 0.0310
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (chain C and resid 350:534)
REMARK 3 ORIGIN FOR THE GROUP (A): 36.1919 -87.4978 -9.3856
REMARK 3 T TENSOR
REMARK 3 T11: 0.5929 T22: 0.5023
REMARK 3 T33: 0.4948 T12: -0.1849
REMARK 3 T13: -0.1335 T23: -0.0089
REMARK 3 L TENSOR
REMARK 3 L11: 5.9565 L22: 5.4355
REMARK 3 L33: 6.6212 L12: 1.7602
REMARK 3 L13: 1.7499 L23: -0.0593
REMARK 3 S TENSOR
REMARK 3 S11: 0.5761 S12: -0.7079 S13: -0.3027
REMARK 3 S21: 1.1840 S22: -0.4537 S23: -0.9970
REMARK 3 S31: -0.0466 S32: 0.1825 S33: -0.1767
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (chain C and resid 535:658)
REMARK 3 ORIGIN FOR THE GROUP (A): 22.6039 -99.6462 -3.9552
REMARK 3 T TENSOR
REMARK 3 T11: 1.0882 T22: 0.6595
REMARK 3 T33: 0.5321 T12: -0.5192
REMARK 3 T13: -0.0447 T23: -0.0201
REMARK 3 L TENSOR
REMARK 3 L11: 3.0286 L22: 2.2925
REMARK 3 L33: 2.3766 L12: 0.3729
REMARK 3 L13: 0.8195 L23: 0.5429
REMARK 3 S TENSOR
REMARK 3 S11: 0.4532 S12: -0.8346 S13: -0.9440
REMARK 3 S21: 1.4866 S22: -0.4062 S23: 0.1976
REMARK 3 S31: 0.6902 S32: -0.3452 S33: -0.0518
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: (chain C and resid 675:691)
REMARK 3 ORIGIN FOR THE GROUP (A): 26.7375-102.8137 -7.3976
REMARK 3 T TENSOR
REMARK 3 T11: 0.7454 T22: 0.4989
REMARK 3 T33: 0.4281 T12: -0.2308
REMARK 3 T13: -0.0877 T23: -0.1077
REMARK 3 L TENSOR
REMARK 3 L11: 6.1556 L22: 2.7287
REMARK 3 L33: 2.2585 L12: 1.2619
REMARK 3 L13: 0.7951 L23: -2.1476
REMARK 3 S TENSOR
REMARK 3 S11: 0.5832 S12: -0.2365 S13: -1.1603
REMARK 3 S21: 0.0792 S22: -0.7140 S23: 0.7232
REMARK 3 S31: -0.3159 S32: 0.4607 S33: 0.0267
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: (chain B and resid 3:92)
REMARK 3 ORIGIN FOR THE GROUP (A): 10.4449 -60.7556 -11.6105
REMARK 3 T TENSOR
REMARK 3 T11: 0.2324 T22: 0.1951
REMARK 3 T33: 0.1774 T12: 0.0909
REMARK 3 T13: -0.0129 T23: -0.0390
REMARK 3 L TENSOR
REMARK 3 L11: 4.8963 L22: 4.9350
REMARK 3 L33: 3.9945 L12: -1.0559
REMARK 3 L13: -0.1067 L23: 0.1085
REMARK 3 S TENSOR
REMARK 3 S11: 0.0572 S12: 0.2217 S13: 0.1119
REMARK 3 S21: -0.0126 S22: 0.0599 S23: -0.1181
REMARK 3 S31: 0.0919 S32: 0.2266 S33: -0.0979
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: (chain B and resid 93:248)
REMARK 3 ORIGIN FOR THE GROUP (A): -21.6934 -62.7024 -16.7513
REMARK 3 T TENSOR
REMARK 3 T11: 0.2489 T22: 0.3947
REMARK 3 T33: 0.3802 T12: 0.0559
REMARK 3 T13: -0.0491 T23: 0.0708
REMARK 3 L TENSOR
REMARK 3 L11: 4.6415 L22: 3.3493
REMARK 3 L33: 4.7427 L12: 0.9323
REMARK 3 L13: -0.1746 L23: -0.7399
REMARK 3 S TENSOR
REMARK 3 S11: 0.2076 S12: 0.4884 S13: 0.0434
REMARK 3 S21: -0.1341 S22: -0.0023 S23: 0.6941
REMARK 3 S31: 0.3301 S32: -0.5867 S33: -0.1834
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: (chain B and resid 249:338)
REMARK 3 ORIGIN FOR THE GROUP (A): 3.4503 -60.2535 -17.7843
REMARK 3 T TENSOR
REMARK 3 T11: 0.3224 T22: 0.3277
REMARK 3 T33: 0.1284 T12: -0.0014
REMARK 3 T13: 0.0199 T23: 0.0131
REMARK 3 L TENSOR
REMARK 3 L11: 5.9772 L22: 3.5077
REMARK 3 L33: 2.7253 L12: -1.6760
REMARK 3 L13: 0.2923 L23: -0.3158
REMARK 3 S TENSOR
REMARK 3 S11: 0.4786 S12: 0.6580 S13: 0.1954
REMARK 3 S21: -0.1421 S22: -0.3159 S23: -0.0503
REMARK 3 S31: 0.2118 S32: 0.0985 S33: -0.1306
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: (chain B and resid 339:601)
REMARK 3 ORIGIN FOR THE GROUP (A): 1.6538 -38.8826 -48.3751
REMARK 3 T TENSOR
REMARK 3 T11: 0.3474 T22: 0.3980
REMARK 3 T33: 0.3460 T12: -0.0721
REMARK 3 T13: -0.1645 T23: 0.2048
REMARK 3 L TENSOR
REMARK 3 L11: 2.5517 L22: 3.2723
REMARK 3 L33: 1.9412 L12: 0.1512
REMARK 3 L13: -0.2970 L23: 0.0490
REMARK 3 S TENSOR
REMARK 3 S11: -0.1927 S12: 0.3085 S13: 0.1823
REMARK 3 S21: -0.5890 S22: 0.3247 S23: 0.1528
REMARK 3 S31: -0.0028 S32: 0.1371 S33: -0.0775
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: (chain B and resid 602:678)
REMARK 3 ORIGIN FOR THE GROUP (A): -7.9928 -41.2148 -44.4253
REMARK 3 T TENSOR
REMARK 3 T11: 0.3493 T22: 0.4366
REMARK 3 T33: 0.5341 T12: -0.1222
REMARK 3 T13: -0.2572 T23: 0.1822
REMARK 3 L TENSOR
REMARK 3 L11: 3.2305 L22: 1.6075
REMARK 3 L33: 3.7141 L12: 0.0658
REMARK 3 L13: -0.3183 L23: 0.1482
REMARK 3 S TENSOR
REMARK 3 S11: -0.0430 S12: 0.2924 S13: 0.3200
REMARK 3 S21: -0.8765 S22: 0.0932 S23: 0.6537
REMARK 3 S31: -0.1068 S32: 0.0129 S33: -0.0310
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: (chain A and resid 38:107)
REMARK 3 ORIGIN FOR THE GROUP (A): 9.1030 -12.2241 -26.2962
REMARK 3 T TENSOR
REMARK 3 T11: 0.2127 T22: 0.4035
REMARK 3 T33: 0.8774 T12: 0.0341
REMARK 3 T13: -0.0344 T23: 0.2421
REMARK 3 L TENSOR
REMARK 3 L11: 2.5854 L22: 0.9778
REMARK 3 L33: 1.2999 L12: -0.3573
REMARK 3 L13: 0.9699 L23: -0.1228
REMARK 3 S TENSOR
REMARK 3 S11: 0.0705 S12: -0.3051 S13: 0.7109
REMARK 3 S21: 0.1226 S22: -0.0986 S23: 0.9752
REMARK 3 S31: 0.0467 S32: -0.1121 S33: -0.0326
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: (chain A and resid 108:121)
REMARK 3 ORIGIN FOR THE GROUP (A): 20.9978 -28.5663 -30.8711
REMARK 3 T TENSOR
REMARK 3 T11: 0.6399 T22: 1.4273
REMARK 3 T33: 1.6265 T12: 0.0773
REMARK 3 T13: 0.5941 T23: -0.2156
REMARK 3 L TENSOR
REMARK 3 L11: 2.6650 L22: 4.2360
REMARK 3 L33: 6.7151 L12: 1.2979
REMARK 3 L13: -2.2922 L23: 3.0217
REMARK 3 S TENSOR
REMARK 3 S11: -0.7532 S12: -0.1825 S13: -1.9765
REMARK 3 S21: 0.2656 S22: 0.2762 S23: 0.0756
REMARK 3 S31: 1.0348 S32: 0.5256 S33: 0.5048
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: (chain A and resid 122:263)
REMARK 3 ORIGIN FOR THE GROUP (A): 17.2457 -11.9383 -36.8149
REMARK 3 T TENSOR
REMARK 3 T11: 0.3480 T22: 0.4196
REMARK 3 T33: 0.5906 T12: 0.0453
REMARK 3 T13: -0.0797 T23: 0.2384
REMARK 3 L TENSOR
REMARK 3 L11: 0.9256 L22: 2.5208
REMARK 3 L33: 1.3887 L12: 0.6602
REMARK 3 L13: 0.2194 L23: 0.8457
REMARK 3 S TENSOR
REMARK 3 S11: -0.2946 S12: 0.1899 S13: 0.1795
REMARK 3 S21: -0.2152 S22: 0.2341 S23: 0.5550
REMARK 3 S31: 0.0404 S32: 0.0323 S33: 0.0695
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: (chain A and resid 264:271)
REMARK 3 ORIGIN FOR THE GROUP (A): 20.0794 -22.4654 -58.4446
REMARK 3 T TENSOR
REMARK 3 T11: 0.8747 T22: 1.0551
REMARK 3 T33: 0.7624 T12: -0.2771
REMARK 3 T13: -0.1393 T23: 0.0888
REMARK 3 L TENSOR
REMARK 3 L11: 6.8813 L22: 8.6463
REMARK 3 L33: 9.6064 L12: 0.6189
REMARK 3 L13: -2.1291 L23: -3.6924
REMARK 3 S TENSOR
REMARK 3 S11: 0.2050 S12: 1.2358 S13: -0.2488
REMARK 3 S21: -1.5118 S22: -1.3425 S23: -0.0547
REMARK 3 S31: -0.0278 S32: 0.6054 S33: 0.9894
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: (chain A and resid 272:440)
REMARK 3 ORIGIN FOR THE GROUP (A): 22.7846 1.9639 -29.2666
REMARK 3 T TENSOR
REMARK 3 T11: 0.2964 T22: 0.3044
REMARK 3 T33: 0.6716 T12: -0.0107
REMARK 3 T13: -0.0178 T23: 0.2238
REMARK 3 L TENSOR
REMARK 3 L11: 1.5470 L22: 2.7943
REMARK 3 L33: 2.6457 L12: 0.9758
REMARK 3 L13: 0.6336 L23: 0.7924
REMARK 3 S TENSOR
REMARK 3 S11: -0.0254 S12: 0.2337 S13: 0.4939
REMARK 3 S21: -0.2377 S22: 0.1134 S23: 0.7056
REMARK 3 S31: -0.3266 S32: -0.0374 S33: -0.1320
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: (chain A and resid 441:590)
REMARK 3 ORIGIN FOR THE GROUP (A): 30.8451 17.8012 -8.3977
REMARK 3 T TENSOR
REMARK 3 T11: 0.7307 T22: 0.3943
REMARK 3 T33: 0.7414 T12: -0.1343
REMARK 3 T13: 0.3083 T23: -0.0451
REMARK 3 L TENSOR
REMARK 3 L11: 3.2825 L22: 3.5411
REMARK 3 L33: 4.1233 L12: 1.0704
REMARK 3 L13: 0.4147 L23: -0.9916
REMARK 3 S TENSOR
REMARK 3 S11: 0.0979 S12: -0.4811 S13: 0.3084
REMARK 3 S21: 0.9883 S22: -0.4620 S23: 0.5626
REMARK 3 S31: -0.4779 S32: -0.2318 S33: 0.3086
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: (chain A and resid 591:619)
REMARK 3 ORIGIN FOR THE GROUP (A): 43.8788 21.2616 -4.6725
REMARK 3 T TENSOR
REMARK 3 T11: 0.9022 T22: 0.5710
REMARK 3 T33: 0.5589 T12: -0.2788
REMARK 3 T13: 0.1126 T23: 0.0567
REMARK 3 L TENSOR
REMARK 3 L11: 8.5167 L22: 7.8067
REMARK 3 L33: 3.4420 L12: 1.5674
REMARK 3 L13: 5.2081 L23: 2.3032
REMARK 3 S TENSOR
REMARK 3 S11: -0.1261 S12: -1.2063 S13: 0.8238
REMARK 3 S21: 2.1246 S22: -0.6070 S23: 0.4249
REMARK 3 S31: 0.5666 S32: 0.6612 S33: 0.7735
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: (chain A and resid 620:689)
REMARK 3 ORIGIN FOR THE GROUP (A): 39.0241 18.1013 -5.9417
REMARK 3 T TENSOR
REMARK 3 T11: 0.7397 T22: 0.5009
REMARK 3 T33: 0.6172 T12: -0.1731
REMARK 3 T13: 0.1819 T23: 0.0761
REMARK 3 L TENSOR
REMARK 3 L11: 5.3926 L22: 4.3401
REMARK 3 L33: 3.8146 L12: 0.3910
REMARK 3 L13: 1.2889 L23: 2.2410
REMARK 3 S TENSOR
REMARK 3 S11: 0.2014 S12: -0.9251 S13: 0.1674
REMARK 3 S21: 1.2425 S22: 0.1430 S23: 0.2698
REMARK 3 S31: 0.1862 S32: -0.0771 S33: -0.2798
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: (chain D and resid 3:91)
REMARK 3 ORIGIN FOR THE GROUP (A): 51.4388 -17.3645 -11.2750
REMARK 3 T TENSOR
REMARK 3 T11: 0.3328 T22: 0.1548
REMARK 3 T33: 0.2349 T12: 0.0891
REMARK 3 T13: -0.0615 T23: -0.0210
REMARK 3 L TENSOR
REMARK 3 L11: 6.2172 L22: 4.8903
REMARK 3 L33: 3.8778 L12: -1.4867
REMARK 3 L13: -0.8579 L23: -0.6454
REMARK 3 S TENSOR
REMARK 3 S11: 0.1447 S12: 0.1212 S13: -0.3327
REMARK 3 S21: -0.0371 S22: 0.0370 S23: 0.4485
REMARK 3 S31: 0.0855 S32: -0.0944 S33: -0.1975
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: (chain D and resid 92:245)
REMARK 3 ORIGIN FOR THE GROUP (A): 83.9428 -15.0978 -16.2510
REMARK 3 T TENSOR
REMARK 3 T11: 0.3265 T22: 0.3856
REMARK 3 T33: 0.2229 T12: 0.2091
REMARK 3 T13: 0.0873 T23: 0.0621
REMARK 3 L TENSOR
REMARK 3 L11: 4.7752 L22: 2.8916
REMARK 3 L33: 3.4353 L12: -0.2300
REMARK 3 L13: 0.2073 L23: 0.9574
REMARK 3 S TENSOR
REMARK 3 S11: 0.6200 S12: 0.7913 S13: 0.2121
REMARK 3 S21: -0.2901 S22: -0.5740 S23: -0.6016
REMARK 3 S31: -0.2293 S32: 0.5568 S33: -0.0551
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: (chain D and resid 246:340)
REMARK 3 ORIGIN FOR THE GROUP (A): 59.9695 -18.9534 -17.6259
REMARK 3 T TENSOR
REMARK 3 T11: 0.3215 T22: 0.3392
REMARK 3 T33: 0.1177 T12: 0.0582
REMARK 3 T13: -0.0300 T23: -0.0278
REMARK 3 L TENSOR
REMARK 3 L11: 4.7262 L22: 2.6608
REMARK 3 L33: 2.4956 L12: -0.5700
REMARK 3 L13: -0.3671 L23: 0.4098
REMARK 3 S TENSOR
REMARK 3 S11: 0.5392 S12: 0.5056 S13: -0.1737
REMARK 3 S21: -0.2183 S22: -0.4021 S23: 0.1027
REMARK 3 S31: 0.0839 S32: -0.1983 S33: -0.1042
REMARK 3 TLS GROUP : 25
REMARK 3 SELECTION: (chain D and resid 341:609)
REMARK 3 ORIGIN FOR THE GROUP (A): 62.1381 -41.4558 -46.5785
REMARK 3 T TENSOR
REMARK 3 T11: 0.4241 T22: 0.4018
REMARK 3 T33: 0.2857 T12: 0.0548
REMARK 3 T13: 0.0592 T23: -0.1329
REMARK 3 L TENSOR
REMARK 3 L11: 3.5008 L22: 3.4555
REMARK 3 L33: 2.8450 L12: 0.0572
REMARK 3 L13: 0.4238 L23: -0.2768
REMARK 3 S TENSOR
REMARK 3 S11: -0.2165 S12: 0.4340 S13: 0.0200
REMARK 3 S21: -0.3972 S22: 0.3007 S23: 0.0188
REMARK 3 S31: -0.0926 S32: -0.1708 S33: -0.0867
REMARK 3 TLS GROUP : 26
REMARK 3 SELECTION: (chain D and resid 610:679)
REMARK 3 ORIGIN FOR THE GROUP (A): 69.5284 -36.8825 -42.8683
REMARK 3 T TENSOR
REMARK 3 T11: 0.4346 T22: 0.3654
REMARK 3 T33: 0.2528 T12: -0.0130
REMARK 3 T13: 0.0252 T23: -0.1484
REMARK 3 L TENSOR
REMARK 3 L11: 2.6655 L22: 4.2341
REMARK 3 L33: 4.1135 L12: 0.3056
REMARK 3 L13: 0.3342 L23: 1.0309
REMARK 3 S TENSOR
REMARK 3 S11: -0.1188 S12: 0.5823 S13: -0.0484
REMARK 3 S21: -0.6349 S22: 0.0039 S23: -0.4899
REMARK 3 S31: -0.2526 S32: -0.2521 S33: 0.0692
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 2
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: chain B and (resseq 3:212 or resseq 219:
REMARK 3 333 or resseq 337:348 or resseq 350:679 )
REMARK 3 and (not element H) and (not element D)
REMARK 3 SELECTION : chain D and (resseq 3:212 or resseq 219:
REMARK 3 333 or resseq 337:348 or resseq 350:679 )
REMARK 3 and (not element H) and (not element D)
REMARK 3 ATOM PAIRS NUMBER : 5166
REMARK 3 RMSD : 0.091
REMARK 3 NCS GROUP : 2
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: chain A and (resseq 39:109 or resseq 121:
REMARK 3 267 or resseq 271:297 or resseq 303:350 or
REMARK 3 resseq 376:417 or resseq 436:446 or resseq
REMARK 3 476:499 or resseq 520:620 or resseq 629:
REMARK 3 658 or resseq 675:689 ) and (not element
REMARK 3 H) and (not element D)
REMARK 3 SELECTION : chain C and (resseq 39:109 or resseq 121:
REMARK 3 267 or resseq 271:297 or resseq 303:350 or
REMARK 3 resseq 376:417 or resseq 436:446 or resseq
REMARK 3 476:499 or resseq 520:620 or resseq 629:
REMARK 3 658 or resseq 675:689 ) and (not element
REMARK 3 H) and (not element D)
REMARK 3 ATOM PAIRS NUMBER : 4041
REMARK 3 RMSD : 0.062
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3VE1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-JAN-12.
REMARK 100 THE RCSB ID CODE IS RCSB069927.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-JUN-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-E
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 70285
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.950
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 10.500
REMARK 200 R MERGE (I) : 0.11500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.06
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 10.70
REMARK 200 R MERGE FOR SHELL (I) : 0.64000
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.67
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.84
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M SODIUM CACODYLATE PH 6.5, 14% PEG
REMARK 280 3350, 0.1M SODIUM MALONATE, AND 20% GLYCEROL, VAPOR DIFFUSION,
REMARK 280 HANGING 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 64.01150
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 84.75550
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 76.75450
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 84.75550
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 64.01150
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 76.75450
REMARK 290 SMTRY3 4 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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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 GLY A 34
REMARK 465 SER A 35
REMARK 465 LYS A 36
REMARK 465 ASP A 37
REMARK 465 GLN A 111
REMARK 465 ASN A 112
REMARK 465 GLY A 113
REMARK 465 SER A 114
REMARK 465 ALA A 115
REMARK 465 GLY A 116
REMARK 465 ASN A 117
REMARK 465 GLY A 118
REMARK 465 GLU A 351
REMARK 465 ASN A 352
REMARK 465 GLY A 353
REMARK 465 ALA A 354
REMARK 465 ALA A 355
REMARK 465 ALA A 356
REMARK 465 SER A 357
REMARK 465 GLY A 358
REMARK 465 SER A 359
REMARK 465 THR A 360
REMARK 465 GLY A 361
REMARK 465 ALA A 362
REMARK 465 ALA A 363
REMARK 465 ALA A 364
REMARK 465 SER A 365
REMARK 465 GLY A 366
REMARK 465 GLY A 367
REMARK 465 ALA A 368
REMARK 465 ALA A 369
REMARK 465 GLY A 370
REMARK 465 THR A 371
REMARK 465 SER A 372
REMARK 465 SER A 373
REMARK 465 GLU A 374
REMARK 465 ASN A 375
REMARK 465 SER A 420
REMARK 465 GLU A 421
REMARK 465 SER A 422
REMARK 465 GLY A 423
REMARK 465 ASN A 424
REMARK 465 THR A 425
REMARK 465 GLN A 426
REMARK 465 ALA A 427
REMARK 465 ASP A 428
REMARK 465 LYS A 429
REMARK 465 GLY A 430
REMARK 465 LYS A 431
REMARK 465 ASN A 432
REMARK 465 GLY A 433
REMARK 465 GLY A 434
REMARK 465 THR A 435
REMARK 465 SER A 447
REMARK 465 ASP A 448
REMARK 465 LYS A 449
REMARK 465 LYS A 450
REMARK 465 ASP A 451
REMARK 465 ALA A 452
REMARK 465 GLN A 453
REMARK 465 ALA A 454
REMARK 465 GLY A 455
REMARK 465 THR A 456
REMARK 465 GLN A 457
REMARK 465 THR A 458
REMARK 465 ASN A 459
REMARK 465 GLY A 460
REMARK 465 ALA A 461
REMARK 465 GLN A 462
REMARK 465 THR A 463
REMARK 465 ALA A 464
REMARK 465 SER A 465
REMARK 465 ASN A 466
REMARK 465 THR A 467
REMARK 465 ALA A 468
REMARK 465 GLY A 469
REMARK 465 ASP A 470
REMARK 465 THR A 471
REMARK 465 ASN A 472
REMARK 465 GLY A 473
REMARK 465 LYS A 474
REMARK 465 SER A 500
REMARK 465 LYS A 501
REMARK 465 SER A 502
REMARK 465 ALA A 503
REMARK 465 MET A 504
REMARK 465 GLN A 505
REMARK 465 ALA A 506
REMARK 465 GLY A 507
REMARK 465 GLY A 508
REMARK 465 ASN A 509
REMARK 465 SER A 510
REMARK 465 SER A 511
REMARK 465 GLN A 512
REMARK 465 ALA A 513
REMARK 465 ASP A 514
REMARK 465 ALA A 515
REMARK 465 LYS A 516
REMARK 465 THR A 517
REMARK 465 GLU A 518
REMARK 465 GLN A 622
REMARK 465 LYS A 623
REMARK 465 ASN A 624
REMARK 465 THR A 625
REMARK 465 THR A 626
REMARK 465 GLN A 661
REMARK 465 THR A 662
REMARK 465 GLU A 663
REMARK 465 LYS A 664
REMARK 465 ALA A 665
REMARK 465 THR A 666
REMARK 465 ALA A 667
REMARK 465 THR A 668
REMARK 465 SER A 669
REMARK 465 SER A 670
REMARK 465 ASP A 671
REMARK 465 GLY A 672
REMARK 465 ASN A 673
REMARK 465 SER A 674
REMARK 465 VAL A 690
REMARK 465 GLN A 691
REMARK 465 VAL B 1
REMARK 465 PRO B 2
REMARK 465 ALA B 334
REMARK 465 PRO B 335
REMARK 465 GLY C 34
REMARK 465 SER C 35
REMARK 465 LYS C 36
REMARK 465 ASP C 37
REMARK 465 HIS C 110
REMARK 465 GLN C 111
REMARK 465 ASN C 112
REMARK 465 GLY C 113
REMARK 465 SER C 114
REMARK 465 ALA C 115
REMARK 465 GLY C 116
REMARK 465 ASN C 117
REMARK 465 THR C 268
REMARK 465 ASN C 269
REMARK 465 GLU C 351
REMARK 465 ASN C 352
REMARK 465 GLY C 353
REMARK 465 ALA C 354
REMARK 465 ALA C 355
REMARK 465 ALA C 356
REMARK 465 SER C 357
REMARK 465 GLY C 358
REMARK 465 SER C 359
REMARK 465 THR C 360
REMARK 465 GLY C 361
REMARK 465 ALA C 362
REMARK 465 ALA C 363
REMARK 465 ALA C 364
REMARK 465 SER C 365
REMARK 465 GLY C 366
REMARK 465 GLY C 367
REMARK 465 ALA C 368
REMARK 465 ALA C 369
REMARK 465 GLY C 370
REMARK 465 THR C 371
REMARK 465 SER C 372
REMARK 465 SER C 373
REMARK 465 GLU C 421
REMARK 465 SER C 422
REMARK 465 GLY C 423
REMARK 465 ASN C 424
REMARK 465 THR C 425
REMARK 465 GLN C 426
REMARK 465 ALA C 427
REMARK 465 ASP C 428
REMARK 465 LYS C 429
REMARK 465 GLY C 430
REMARK 465 LYS C 431
REMARK 465 ASN C 432
REMARK 465 GLY C 433
REMARK 465 GLY C 434
REMARK 465 ASP C 448
REMARK 465 LYS C 449
REMARK 465 LYS C 450
REMARK 465 ASP C 451
REMARK 465 ALA C 452
REMARK 465 GLN C 453
REMARK 465 ALA C 454
REMARK 465 GLY C 455
REMARK 465 THR C 456
REMARK 465 GLN C 457
REMARK 465 THR C 458
REMARK 465 ASN C 459
REMARK 465 GLY C 460
REMARK 465 ALA C 461
REMARK 465 GLN C 462
REMARK 465 THR C 463
REMARK 465 ALA C 464
REMARK 465 SER C 465
REMARK 465 ASN C 466
REMARK 465 THR C 467
REMARK 465 ALA C 468
REMARK 465 GLY C 469
REMARK 465 ASP C 470
REMARK 465 THR C 471
REMARK 465 ASN C 472
REMARK 465 GLY C 473
REMARK 465 LYS C 474
REMARK 465 THR C 475
REMARK 465 SER C 500
REMARK 465 LYS C 501
REMARK 465 SER C 502
REMARK 465 ALA C 503
REMARK 465 MET C 504
REMARK 465 GLN C 505
REMARK 465 ALA C 506
REMARK 465 GLY C 507
REMARK 465 GLY C 508
REMARK 465 ASN C 509
REMARK 465 SER C 510
REMARK 465 SER C 511
REMARK 465 GLN C 512
REMARK 465 ALA C 513
REMARK 465 ASP C 514
REMARK 465 ALA C 515
REMARK 465 LYS C 516
REMARK 465 THR C 517
REMARK 465 GLU C 518
REMARK 465 GLN C 519
REMARK 465 LEU C 620
REMARK 465 ASP C 621
REMARK 465 GLN C 622
REMARK 465 LYS C 623
REMARK 465 ASN C 624
REMARK 465 THR C 625
REMARK 465 THR C 626
REMARK 465 ASP C 659
REMARK 465 LYS C 660
REMARK 465 GLN C 661
REMARK 465 THR C 662
REMARK 465 GLU C 663
REMARK 465 LYS C 664
REMARK 465 ALA C 665
REMARK 465 THR C 666
REMARK 465 ALA C 667
REMARK 465 THR C 668
REMARK 465 SER C 669
REMARK 465 SER C 670
REMARK 465 ASP C 671
REMARK 465 GLY C 672
REMARK 465 ASN C 673
REMARK 465 SER C 674
REMARK 465 VAL D 1
REMARK 465 PRO D 2
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 ARG A 288 NE - CZ - NH1 ANGL. DEV. = -6.3 DEGREES
REMARK 500 ARG A 288 NE - CZ - NH2 ANGL. DEV. = 5.4 DEGREES
REMARK 500 PRO A 629 C - N - CA ANGL. DEV. = -11.6 DEGREES
REMARK 500 ALA B 218 N - CA - C ANGL. DEV. = -20.0 DEGREES
REMARK 500 CYS B 241 CA - CB - SG ANGL. DEV. = 6.8 DEGREES
REMARK 500 ARG C 288 CD - NE - CZ ANGL. DEV. = 8.7 DEGREES
REMARK 500 ARG C 288 NE - CZ - NH1 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ARG C 288 NE - CZ - NH2 ANGL. DEV. = -7.0 DEGREES
REMARK 500 PRO C 629 C - N - CA ANGL. DEV. = 23.1 DEGREES
REMARK 500 PRO C 629 C - N - CD ANGL. DEV. = -20.9 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 GLN A 121 153.21 81.79
REMARK 500 HIS A 129 79.89 -117.20
REMARK 500 ASN A 265 -127.25 44.21
REMARK 500 ASN A 267 -5.39 90.05
REMARK 500 ASP A 271 -20.36 75.18
REMARK 500 VAL A 309 -62.88 -134.61
REMARK 500 SER A 401 38.00 70.45
REMARK 500 LYS A 418 -62.33 -95.51
REMARK 500 LYS A 565 -178.54 167.07
REMARK 500 ALA A 593 -103.45 64.60
REMARK 500 ALA A 614 -142.12 58.36
REMARK 500 ASP A 619 -10.38 89.88
REMARK 500 TYR A 656 138.54 -175.55
REMARK 500 VAL B 29 -62.99 -120.89
REMARK 500 ASP B 58 -57.90 -121.43
REMARK 500 PRO B 74 31.68 -91.63
REMARK 500 VAL B 80 -58.98 -126.87
REMARK 500 SER B 87 157.41 178.22
REMARK 500 SER B 125 -71.60 -60.80
REMARK 500 TRP B 128 -66.98 -132.84
REMARK 500 CYS B 161 -7.47 82.63
REMARK 500 LYS B 217 -22.20 72.81
REMARK 500 ASP B 219 -9.57 87.14
REMARK 500 ASP B 277 -3.89 66.32
REMARK 500 LEU B 294 -18.74 69.12
REMARK 500 ASP B 337 -0.52 69.66
REMARK 500 SER B 348 -148.93 49.06
REMARK 500 VAL B 407 -60.74 -124.30
REMARK 500 ASP B 438 -5.92 76.39
REMARK 500 ALA B 453 159.79 179.52
REMARK 500 THR B 457 -70.60 -48.01
REMARK 500 TRP B 460 -68.29 -130.80
REMARK 500 CYS B 506 -2.24 75.02
REMARK 500 LYS B 527 -63.89 -132.75
REMARK 500 SER B 616 -65.11 -91.59
REMARK 500 THR B 626 -9.33 60.93
REMARK 500 LEU B 630 -21.19 68.35
REMARK 500 HIS B 642 -123.71 59.82
REMARK 500 ASN B 645 -9.23 -58.91
REMARK 500 ASP C 94 39.73 -90.32
REMARK 500 PRO C 204 48.01 -83.11
REMARK 500 ASN C 265 -126.17 42.09
REMARK 500 LYS C 298 157.37 174.96
REMARK 500 LYS C 299 -75.72 -81.38
REMARK 500 GLU C 300 -84.10 -124.85
REMARK 500 VAL C 309 -60.42 -133.53
REMARK 500 SER C 401 37.05 70.17
REMARK 500 ASP C 419 -73.18 -94.46
REMARK 500 LYS C 565 -171.31 75.49
REMARK 500 GLU C 566 -61.44 -93.57
REMARK 500
REMARK 500 THIS ENTRY HAS 70 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 SER A 108 ASN A 109 -32.52
REMARK 500 SER C 108 ASN C 109 -30.77
REMARK 500 ALA D 218 ASP D 219 134.62
REMARK 500 THR D 336 ASP D 337 138.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 ASP A 564 11.60
REMARK 500 ASP C 564 -13.49
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 GLU A 222 21.7 L L OUTSIDE RANGE
REMARK 500 SER A 314 24.5 L L OUTSIDE RANGE
REMARK 500 PHE A 400 24.1 L L OUTSIDE RANGE
REMARK 500 ALA A 593 25.0 L L OUTSIDE RANGE
REMARK 500 ALA B 218 45.5 L L OUTSIDE RANGE
REMARK 500 ASP B 337 22.9 L L OUTSIDE RANGE
REMARK 500 ASP C 94 24.8 L L OUTSIDE RANGE
REMARK 500 HIS C 129 24.6 L L OUTSIDE RANGE
REMARK 500 GLU C 222 23.2 L L OUTSIDE RANGE
REMARK 500 ALA D 218 22.6 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE D 702 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 392 OD1
REMARK 620 2 HIS D 585 NE2 78.9
REMARK 620 3 TYR D 426 OH 108.7 94.2
REMARK 620 4 CO3 D 701 O1 82.3 156.8 104.7
REMARK 620 5 TYR D 517 OH 143.2 82.3 104.0 105.5
REMARK 620 6 CO3 D 701 O3 72.2 99.2 166.4 61.8 80.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE B 702 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR B 517 OH
REMARK 620 2 ASP B 392 OD1 146.4
REMARK 620 3 CO3 B 701 O3 110.6 88.4
REMARK 620 4 HIS B 585 NE2 80.8 76.5 164.2
REMARK 620 5 CO3 B 701 O1 87.2 77.8 61.3 109.9
REMARK 620 6 TYR B 426 OH 104.4 100.6 96.0 91.5 157.2
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO3 B 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE B 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 705
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 706
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 707
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 708
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO3 D 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE D 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 705
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 706
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3VE2 RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 AUTHOR STATES THAT THE THE DIFFERENCES WITH UNP REFERENCE ARE
REMARK 999 NATURAL VARIANTS
DBREF 3VE1 A 36 691 UNP Q09057 TBB1_NEIMB 56 711
DBREF 3VE1 B 1 679 UNP P02787 TRFE_HUMAN 20 698
DBREF 3VE1 C 36 691 UNP Q09057 TBB1_NEIMB 56 711
DBREF 3VE1 D 1 679 UNP P02787 TRFE_HUMAN 20 698
SEQADV 3VE1 GLY A 34 UNP Q09057 EXPRESSION TAG
SEQADV 3VE1 SER A 35 UNP Q09057 EXPRESSION TAG
SEQADV 3VE1 ASP B 413 UNP P02787 ASN 432 SEE REMARK 999
SEQADV 3VE1 VAL B 429 UNP P02787 ILE 448 SEE REMARK 999
SEQADV 3VE1 ASP B 611 UNP P02787 ASN 630 SEE REMARK 999
SEQADV 3VE1 GLY C 34 UNP Q09057 EXPRESSION TAG
SEQADV 3VE1 SER C 35 UNP Q09057 EXPRESSION TAG
SEQADV 3VE1 ASP D 413 UNP P02787 ASN 432 SEE REMARK 999
SEQADV 3VE1 VAL D 429 UNP P02787 ILE 448 SEE REMARK 999
SEQADV 3VE1 ASP D 611 UNP P02787 ASN 630 SEE REMARK 999
SEQRES 1 A 658 GLY SER LYS ASP GLN GLY GLY TYR GLY PHE ALA MET ARG
SEQRES 2 A 658 LEU LYS ARG ARG ASN TRP TYR PRO GLY ALA GLU GLU SER
SEQRES 3 A 658 GLU VAL LYS LEU ASN GLU SER ASP TRP GLU ALA THR GLY
SEQRES 4 A 658 LEU PRO THR LYS PRO LYS GLU LEU PRO LYS ARG GLN LYS
SEQRES 5 A 658 SER VAL ILE GLU LYS VAL GLU THR ASP GLY ASP SER ASP
SEQRES 6 A 658 ILE TYR SER SER PRO TYR LEU THR PRO SER ASN HIS GLN
SEQRES 7 A 658 ASN GLY SER ALA GLY ASN GLY VAL ASN GLN PRO LYS ASN
SEQRES 8 A 658 GLN ALA THR GLY HIS GLU ASN PHE GLN TYR VAL TYR SER
SEQRES 9 A 658 GLY TRP PHE TYR LYS HIS ALA ALA SER GLU LYS ASP PHE
SEQRES 10 A 658 SER ASN LYS LYS ILE LYS SER GLY ASP ASP GLY TYR ILE
SEQRES 11 A 658 PHE TYR HIS GLY GLU LYS PRO SER ARG GLN LEU PRO ALA
SEQRES 12 A 658 SER GLY LYS VAL ILE TYR LYS GLY VAL TRP HIS PHE VAL
SEQRES 13 A 658 THR ASP THR LYS LYS GLY GLN ASP PHE ARG GLU ILE ILE
SEQRES 14 A 658 GLN PRO SER LYS LYS GLN GLY ASP ARG TYR SER GLY PHE
SEQRES 15 A 658 SER GLY ASP GLY SER GLU GLU TYR SER ASN LYS ASN GLU
SEQRES 16 A 658 SER THR LEU LYS ASP ASP HIS GLU GLY TYR GLY PHE THR
SEQRES 17 A 658 SER ASN LEU GLU VAL ASP PHE GLY ASN LYS LYS LEU THR
SEQRES 18 A 658 GLY LYS LEU ILE ARG ASN ASN ALA SER LEU ASN ASN ASN
SEQRES 19 A 658 THR ASN ASN ASP LYS HIS THR THR GLN TYR TYR SER LEU
SEQRES 20 A 658 ASP ALA GLN ILE THR GLY ASN ARG PHE ASN GLY THR ALA
SEQRES 21 A 658 THR ALA THR ASP LYS LYS GLU ASN GLU THR LYS LEU HIS
SEQRES 22 A 658 PRO PHE VAL SER ASP SER SER SER LEU SER GLY GLY PHE
SEQRES 23 A 658 PHE GLY PRO GLN GLY GLU GLU LEU GLY PHE ARG PHE LEU
SEQRES 24 A 658 SER ASP ASP GLN LYS VAL ALA VAL VAL GLY SER ALA LYS
SEQRES 25 A 658 THR LYS ASP LYS LEU GLU ASN GLY ALA ALA ALA SER GLY
SEQRES 26 A 658 SER THR GLY ALA ALA ALA SER GLY GLY ALA ALA GLY THR
SEQRES 27 A 658 SER SER GLU ASN SER LYS LEU THR THR VAL LEU ASP ALA
SEQRES 28 A 658 VAL GLU LEU THR LEU ASN ASP LYS LYS ILE LYS ASN LEU
SEQRES 29 A 658 ASP ASN PHE SER ASN ALA ALA GLN LEU VAL VAL ASP GLY
SEQRES 30 A 658 ILE MET ILE PRO LEU LEU PRO LYS ASP SER GLU SER GLY
SEQRES 31 A 658 ASN THR GLN ALA ASP LYS GLY LYS ASN GLY GLY THR GLU
SEQRES 32 A 658 PHE THR ARG LYS PHE GLU HIS THR PRO GLU SER ASP LYS
SEQRES 33 A 658 LYS ASP ALA GLN ALA GLY THR GLN THR ASN GLY ALA GLN
SEQRES 34 A 658 THR ALA SER ASN THR ALA GLY ASP THR ASN GLY LYS THR
SEQRES 35 A 658 LYS THR TYR GLU VAL GLU VAL CYS CYS SER ASN LEU ASN
SEQRES 36 A 658 TYR LEU LYS TYR GLY MET LEU THR ARG LYS ASN SER LYS
SEQRES 37 A 658 SER ALA MET GLN ALA GLY GLY ASN SER SER GLN ALA ASP
SEQRES 38 A 658 ALA LYS THR GLU GLN VAL GLU GLN SER MET PHE LEU GLN
SEQRES 39 A 658 GLY GLU ARG THR ASP GLU LYS GLU ILE PRO THR ASP GLN
SEQRES 40 A 658 ASN VAL VAL TYR ARG GLY SER TRP TYR GLY HIS ILE ALA
SEQRES 41 A 658 ASN GLY THR SER TRP SER GLY ASN ALA SER ASP LYS GLU
SEQRES 42 A 658 GLY GLY ASN ARG ALA GLU PHE THR VAL ASN PHE ALA ASP
SEQRES 43 A 658 LYS LYS ILE THR GLY LYS LEU THR ALA GLU ASN ARG GLN
SEQRES 44 A 658 ALA GLN THR PHE THR ILE GLU GLY MET ILE GLN GLY ASN
SEQRES 45 A 658 GLY PHE GLU GLY THR ALA LYS THR ALA GLU SER GLY PHE
SEQRES 46 A 658 ASP LEU ASP GLN LYS ASN THR THR ARG THR PRO LYS ALA
SEQRES 47 A 658 TYR ILE THR ASP ALA LYS VAL LYS GLY GLY PHE TYR GLY
SEQRES 48 A 658 PRO LYS ALA GLU GLU LEU GLY GLY TRP PHE ALA TYR PRO
SEQRES 49 A 658 GLY ASP LYS GLN THR GLU LYS ALA THR ALA THR SER SER
SEQRES 50 A 658 ASP GLY ASN SER ALA SER SER ALA THR VAL VAL PHE GLY
SEQRES 51 A 658 ALA LYS ARG GLN GLN PRO VAL GLN
SEQRES 1 B 679 VAL PRO ASP LYS THR VAL ARG TRP CYS ALA VAL SER GLU
SEQRES 2 B 679 HIS GLU ALA THR LYS CYS GLN SER PHE ARG ASP HIS MET
SEQRES 3 B 679 LYS SER VAL ILE PRO SER ASP GLY PRO SER VAL ALA CYS
SEQRES 4 B 679 VAL LYS LYS ALA SER TYR LEU ASP CYS ILE ARG ALA ILE
SEQRES 5 B 679 ALA ALA ASN GLU ALA ASP ALA VAL THR LEU ASP ALA GLY
SEQRES 6 B 679 LEU VAL TYR ASP ALA TYR LEU ALA PRO ASN ASN LEU LYS
SEQRES 7 B 679 PRO VAL VAL ALA GLU PHE TYR GLY SER LYS GLU ASP PRO
SEQRES 8 B 679 GLN THR PHE TYR TYR ALA VAL ALA VAL VAL LYS LYS ASP
SEQRES 9 B 679 SER GLY PHE GLN MET ASN GLN LEU ARG GLY LYS LYS SER
SEQRES 10 B 679 CYS HIS THR GLY LEU GLY ARG SER ALA GLY TRP ASN ILE
SEQRES 11 B 679 PRO ILE GLY LEU LEU TYR CYS ASP LEU PRO GLU PRO ARG
SEQRES 12 B 679 LYS PRO LEU GLU LYS ALA VAL ALA ASN PHE PHE SER GLY
SEQRES 13 B 679 SER CYS ALA PRO CYS ALA ASP GLY THR ASP PHE PRO GLN
SEQRES 14 B 679 LEU CYS GLN LEU CYS PRO GLY CYS GLY CYS SER THR LEU
SEQRES 15 B 679 ASN GLN TYR PHE GLY TYR SER GLY ALA PHE LYS CYS LEU
SEQRES 16 B 679 LYS ASP GLY ALA GLY ASP VAL ALA PHE VAL LYS HIS SER
SEQRES 17 B 679 THR ILE PHE GLU ASN LEU ALA ASN LYS ALA ASP ARG ASP
SEQRES 18 B 679 GLN TYR GLU LEU LEU CYS LEU ASP ASN THR ARG LYS PRO
SEQRES 19 B 679 VAL ASP GLU TYR LYS ASP CYS HIS LEU ALA GLN VAL PRO
SEQRES 20 B 679 SER HIS THR VAL VAL ALA ARG SER MET GLY GLY LYS GLU
SEQRES 21 B 679 ASP LEU ILE TRP GLU LEU LEU ASN GLN ALA GLN GLU HIS
SEQRES 22 B 679 PHE GLY LYS ASP LYS SER LYS GLU PHE GLN LEU PHE SER
SEQRES 23 B 679 SER PRO HIS GLY LYS ASP LEU LEU PHE LYS ASP SER ALA
SEQRES 24 B 679 HIS GLY PHE LEU LYS VAL PRO PRO ARG MET ASP ALA LYS
SEQRES 25 B 679 MET TYR LEU GLY TYR GLU TYR VAL THR ALA ILE ARG ASN
SEQRES 26 B 679 LEU ARG GLU GLY THR CYS PRO GLU ALA PRO THR ASP GLU
SEQRES 27 B 679 CYS LYS PRO VAL LYS TRP CYS ALA LEU SER HIS HIS GLU
SEQRES 28 B 679 ARG LEU LYS CYS ASP GLU TRP SER VAL ASN SER VAL GLY
SEQRES 29 B 679 LYS ILE GLU CYS VAL SER ALA GLU THR THR GLU ASP CYS
SEQRES 30 B 679 ILE ALA LYS ILE MET ASN GLY GLU ALA ASP ALA MET SER
SEQRES 31 B 679 LEU ASP GLY GLY PHE VAL TYR ILE ALA GLY LYS CYS GLY
SEQRES 32 B 679 LEU VAL PRO VAL LEU ALA GLU ASN TYR ASP LYS SER ASP
SEQRES 33 B 679 ASN CYS GLU ASP THR PRO GLU ALA GLY TYR PHE ALA VAL
SEQRES 34 B 679 ALA VAL VAL LYS LYS SER ALA SER ASP LEU THR TRP ASP
SEQRES 35 B 679 ASN LEU LYS GLY LYS LYS SER CYS HIS THR ALA VAL GLY
SEQRES 36 B 679 ARG THR ALA GLY TRP ASN ILE PRO MET GLY LEU LEU TYR
SEQRES 37 B 679 ASN LYS ILE ASN HIS CYS ARG PHE ASP GLU PHE PHE SER
SEQRES 38 B 679 GLU GLY CYS ALA PRO GLY SER LYS LYS ASP SER SER LEU
SEQRES 39 B 679 CYS LYS LEU CYS MET GLY SER GLY LEU ASN LEU CYS GLU
SEQRES 40 B 679 PRO ASN ASN LYS GLU GLY TYR TYR GLY TYR THR GLY ALA
SEQRES 41 B 679 PHE ARG CYS LEU VAL GLU LYS GLY ASP VAL ALA PHE VAL
SEQRES 42 B 679 LYS HIS GLN THR VAL PRO GLN ASN THR GLY GLY LYS ASN
SEQRES 43 B 679 PRO ASP PRO TRP ALA LYS ASN LEU ASN GLU LYS ASP TYR
SEQRES 44 B 679 GLU LEU LEU CYS LEU ASP GLY THR ARG LYS PRO VAL GLU
SEQRES 45 B 679 GLU TYR ALA ASN CYS HIS LEU ALA ARG ALA PRO ASN HIS
SEQRES 46 B 679 ALA VAL VAL THR ARG LYS ASP LYS GLU ALA CYS VAL HIS
SEQRES 47 B 679 LYS ILE LEU ARG GLN GLN GLN HIS LEU PHE GLY SER ASP
SEQRES 48 B 679 VAL THR ASP CYS SER GLY ASN PHE CYS LEU PHE ARG SER
SEQRES 49 B 679 GLU THR LYS ASP LEU LEU PHE ARG ASP ASP THR VAL CYS
SEQRES 50 B 679 LEU ALA LYS LEU HIS ASP ARG ASN THR TYR GLU LYS TYR
SEQRES 51 B 679 LEU GLY GLU GLU TYR VAL LYS ALA VAL GLY ASN LEU ARG
SEQRES 52 B 679 LYS CYS SER THR SER SER LEU LEU GLU ALA CYS THR PHE
SEQRES 53 B 679 ARG ARG PRO
SEQRES 1 C 658 GLY SER LYS ASP GLN GLY GLY TYR GLY PHE ALA MET ARG
SEQRES 2 C 658 LEU LYS ARG ARG ASN TRP TYR PRO GLY ALA GLU GLU SER
SEQRES 3 C 658 GLU VAL LYS LEU ASN GLU SER ASP TRP GLU ALA THR GLY
SEQRES 4 C 658 LEU PRO THR LYS PRO LYS GLU LEU PRO LYS ARG GLN LYS
SEQRES 5 C 658 SER VAL ILE GLU LYS VAL GLU THR ASP GLY ASP SER ASP
SEQRES 6 C 658 ILE TYR SER SER PRO TYR LEU THR PRO SER ASN HIS GLN
SEQRES 7 C 658 ASN GLY SER ALA GLY ASN GLY VAL ASN GLN PRO LYS ASN
SEQRES 8 C 658 GLN ALA THR GLY HIS GLU ASN PHE GLN TYR VAL TYR SER
SEQRES 9 C 658 GLY TRP PHE TYR LYS HIS ALA ALA SER GLU LYS ASP PHE
SEQRES 10 C 658 SER ASN LYS LYS ILE LYS SER GLY ASP ASP GLY TYR ILE
SEQRES 11 C 658 PHE TYR HIS GLY GLU LYS PRO SER ARG GLN LEU PRO ALA
SEQRES 12 C 658 SER GLY LYS VAL ILE TYR LYS GLY VAL TRP HIS PHE VAL
SEQRES 13 C 658 THR ASP THR LYS LYS GLY GLN ASP PHE ARG GLU ILE ILE
SEQRES 14 C 658 GLN PRO SER LYS LYS GLN GLY ASP ARG TYR SER GLY PHE
SEQRES 15 C 658 SER GLY ASP GLY SER GLU GLU TYR SER ASN LYS ASN GLU
SEQRES 16 C 658 SER THR LEU LYS ASP ASP HIS GLU GLY TYR GLY PHE THR
SEQRES 17 C 658 SER ASN LEU GLU VAL ASP PHE GLY ASN LYS LYS LEU THR
SEQRES 18 C 658 GLY LYS LEU ILE ARG ASN ASN ALA SER LEU ASN ASN ASN
SEQRES 19 C 658 THR ASN ASN ASP LYS HIS THR THR GLN TYR TYR SER LEU
SEQRES 20 C 658 ASP ALA GLN ILE THR GLY ASN ARG PHE ASN GLY THR ALA
SEQRES 21 C 658 THR ALA THR ASP LYS LYS GLU ASN GLU THR LYS LEU HIS
SEQRES 22 C 658 PRO PHE VAL SER ASP SER SER SER LEU SER GLY GLY PHE
SEQRES 23 C 658 PHE GLY PRO GLN GLY GLU GLU LEU GLY PHE ARG PHE LEU
SEQRES 24 C 658 SER ASP ASP GLN LYS VAL ALA VAL VAL GLY SER ALA LYS
SEQRES 25 C 658 THR LYS ASP LYS LEU GLU ASN GLY ALA ALA ALA SER GLY
SEQRES 26 C 658 SER THR GLY ALA ALA ALA SER GLY GLY ALA ALA GLY THR
SEQRES 27 C 658 SER SER GLU ASN SER LYS LEU THR THR VAL LEU ASP ALA
SEQRES 28 C 658 VAL GLU LEU THR LEU ASN ASP LYS LYS ILE LYS ASN LEU
SEQRES 29 C 658 ASP ASN PHE SER ASN ALA ALA GLN LEU VAL VAL ASP GLY
SEQRES 30 C 658 ILE MET ILE PRO LEU LEU PRO LYS ASP SER GLU SER GLY
SEQRES 31 C 658 ASN THR GLN ALA ASP LYS GLY LYS ASN GLY GLY THR GLU
SEQRES 32 C 658 PHE THR ARG LYS PHE GLU HIS THR PRO GLU SER ASP LYS
SEQRES 33 C 658 LYS ASP ALA GLN ALA GLY THR GLN THR ASN GLY ALA GLN
SEQRES 34 C 658 THR ALA SER ASN THR ALA GLY ASP THR ASN GLY LYS THR
SEQRES 35 C 658 LYS THR TYR GLU VAL GLU VAL CYS CYS SER ASN LEU ASN
SEQRES 36 C 658 TYR LEU LYS TYR GLY MET LEU THR ARG LYS ASN SER LYS
SEQRES 37 C 658 SER ALA MET GLN ALA GLY GLY ASN SER SER GLN ALA ASP
SEQRES 38 C 658 ALA LYS THR GLU GLN VAL GLU GLN SER MET PHE LEU GLN
SEQRES 39 C 658 GLY GLU ARG THR ASP GLU LYS GLU ILE PRO THR ASP GLN
SEQRES 40 C 658 ASN VAL VAL TYR ARG GLY SER TRP TYR GLY HIS ILE ALA
SEQRES 41 C 658 ASN GLY THR SER TRP SER GLY ASN ALA SER ASP LYS GLU
SEQRES 42 C 658 GLY GLY ASN ARG ALA GLU PHE THR VAL ASN PHE ALA ASP
SEQRES 43 C 658 LYS LYS ILE THR GLY LYS LEU THR ALA GLU ASN ARG GLN
SEQRES 44 C 658 ALA GLN THR PHE THR ILE GLU GLY MET ILE GLN GLY ASN
SEQRES 45 C 658 GLY PHE GLU GLY THR ALA LYS THR ALA GLU SER GLY PHE
SEQRES 46 C 658 ASP LEU ASP GLN LYS ASN THR THR ARG THR PRO LYS ALA
SEQRES 47 C 658 TYR ILE THR ASP ALA LYS VAL LYS GLY GLY PHE TYR GLY
SEQRES 48 C 658 PRO LYS ALA GLU GLU LEU GLY GLY TRP PHE ALA TYR PRO
SEQRES 49 C 658 GLY ASP LYS GLN THR GLU LYS ALA THR ALA THR SER SER
SEQRES 50 C 658 ASP GLY ASN SER ALA SER SER ALA THR VAL VAL PHE GLY
SEQRES 51 C 658 ALA LYS ARG GLN GLN PRO VAL GLN
SEQRES 1 D 679 VAL PRO ASP LYS THR VAL ARG TRP CYS ALA VAL SER GLU
SEQRES 2 D 679 HIS GLU ALA THR LYS CYS GLN SER PHE ARG ASP HIS MET
SEQRES 3 D 679 LYS SER VAL ILE PRO SER ASP GLY PRO SER VAL ALA CYS
SEQRES 4 D 679 VAL LYS LYS ALA SER TYR LEU ASP CYS ILE ARG ALA ILE
SEQRES 5 D 679 ALA ALA ASN GLU ALA ASP ALA VAL THR LEU ASP ALA GLY
SEQRES 6 D 679 LEU VAL TYR ASP ALA TYR LEU ALA PRO ASN ASN LEU LYS
SEQRES 7 D 679 PRO VAL VAL ALA GLU PHE TYR GLY SER LYS GLU ASP PRO
SEQRES 8 D 679 GLN THR PHE TYR TYR ALA VAL ALA VAL VAL LYS LYS ASP
SEQRES 9 D 679 SER GLY PHE GLN MET ASN GLN LEU ARG GLY LYS LYS SER
SEQRES 10 D 679 CYS HIS THR GLY LEU GLY ARG SER ALA GLY TRP ASN ILE
SEQRES 11 D 679 PRO ILE GLY LEU LEU TYR CYS ASP LEU PRO GLU PRO ARG
SEQRES 12 D 679 LYS PRO LEU GLU LYS ALA VAL ALA ASN PHE PHE SER GLY
SEQRES 13 D 679 SER CYS ALA PRO CYS ALA ASP GLY THR ASP PHE PRO GLN
SEQRES 14 D 679 LEU CYS GLN LEU CYS PRO GLY CYS GLY CYS SER THR LEU
SEQRES 15 D 679 ASN GLN TYR PHE GLY TYR SER GLY ALA PHE LYS CYS LEU
SEQRES 16 D 679 LYS ASP GLY ALA GLY ASP VAL ALA PHE VAL LYS HIS SER
SEQRES 17 D 679 THR ILE PHE GLU ASN LEU ALA ASN LYS ALA ASP ARG ASP
SEQRES 18 D 679 GLN TYR GLU LEU LEU CYS LEU ASP ASN THR ARG LYS PRO
SEQRES 19 D 679 VAL ASP GLU TYR LYS ASP CYS HIS LEU ALA GLN VAL PRO
SEQRES 20 D 679 SER HIS THR VAL VAL ALA ARG SER MET GLY GLY LYS GLU
SEQRES 21 D 679 ASP LEU ILE TRP GLU LEU LEU ASN GLN ALA GLN GLU HIS
SEQRES 22 D 679 PHE GLY LYS ASP LYS SER LYS GLU PHE GLN LEU PHE SER
SEQRES 23 D 679 SER PRO HIS GLY LYS ASP LEU LEU PHE LYS ASP SER ALA
SEQRES 24 D 679 HIS GLY PHE LEU LYS VAL PRO PRO ARG MET ASP ALA LYS
SEQRES 25 D 679 MET TYR LEU GLY TYR GLU TYR VAL THR ALA ILE ARG ASN
SEQRES 26 D 679 LEU ARG GLU GLY THR CYS PRO GLU ALA PRO THR ASP GLU
SEQRES 27 D 679 CYS LYS PRO VAL LYS TRP CYS ALA LEU SER HIS HIS GLU
SEQRES 28 D 679 ARG LEU LYS CYS ASP GLU TRP SER VAL ASN SER VAL GLY
SEQRES 29 D 679 LYS ILE GLU CYS VAL SER ALA GLU THR THR GLU ASP CYS
SEQRES 30 D 679 ILE ALA LYS ILE MET ASN GLY GLU ALA ASP ALA MET SER
SEQRES 31 D 679 LEU ASP GLY GLY PHE VAL TYR ILE ALA GLY LYS CYS GLY
SEQRES 32 D 679 LEU VAL PRO VAL LEU ALA GLU ASN TYR ASP LYS SER ASP
SEQRES 33 D 679 ASN CYS GLU ASP THR PRO GLU ALA GLY TYR PHE ALA VAL
SEQRES 34 D 679 ALA VAL VAL LYS LYS SER ALA SER ASP LEU THR TRP ASP
SEQRES 35 D 679 ASN LEU LYS GLY LYS LYS SER CYS HIS THR ALA VAL GLY
SEQRES 36 D 679 ARG THR ALA GLY TRP ASN ILE PRO MET GLY LEU LEU TYR
SEQRES 37 D 679 ASN LYS ILE ASN HIS CYS ARG PHE ASP GLU PHE PHE SER
SEQRES 38 D 679 GLU GLY CYS ALA PRO GLY SER LYS LYS ASP SER SER LEU
SEQRES 39 D 679 CYS LYS LEU CYS MET GLY SER GLY LEU ASN LEU CYS GLU
SEQRES 40 D 679 PRO ASN ASN LYS GLU GLY TYR TYR GLY TYR THR GLY ALA
SEQRES 41 D 679 PHE ARG CYS LEU VAL GLU LYS GLY ASP VAL ALA PHE VAL
SEQRES 42 D 679 LYS HIS GLN THR VAL PRO GLN ASN THR GLY GLY LYS ASN
SEQRES 43 D 679 PRO ASP PRO TRP ALA LYS ASN LEU ASN GLU LYS ASP TYR
SEQRES 44 D 679 GLU LEU LEU CYS LEU ASP GLY THR ARG LYS PRO VAL GLU
SEQRES 45 D 679 GLU TYR ALA ASN CYS HIS LEU ALA ARG ALA PRO ASN HIS
SEQRES 46 D 679 ALA VAL VAL THR ARG LYS ASP LYS GLU ALA CYS VAL HIS
SEQRES 47 D 679 LYS ILE LEU ARG GLN GLN GLN HIS LEU PHE GLY SER ASP
SEQRES 48 D 679 VAL THR ASP CYS SER GLY ASN PHE CYS LEU PHE ARG SER
SEQRES 49 D 679 GLU THR LYS ASP LEU LEU PHE ARG ASP ASP THR VAL CYS
SEQRES 50 D 679 LEU ALA LYS LEU HIS ASP ARG ASN THR TYR GLU LYS TYR
SEQRES 51 D 679 LEU GLY GLU GLU TYR VAL LYS ALA VAL GLY ASN LEU ARG
SEQRES 52 D 679 LYS CYS SER THR SER SER LEU LEU GLU ALA CYS THR PHE
SEQRES 53 D 679 ARG ARG PRO
HET GOL A 701 6
HET GOL A 702 6
HET CO3 B 701 4
HET FE B 702 1
HET GOL B 703 6
HET GOL B 704 6
HET GOL B 705 6
HET GOL B 706 6
HET GOL B 707 6
HET GOL B 708 6
HET GOL C 701 6
HET CO3 D 701 4
HET FE D 702 1
HET GOL D 703 6
HET GOL D 704 6
HET GOL D 705 6
HET GOL D 706 6
HETNAM GOL GLYCEROL
HETNAM CO3 CARBONATE ION
HETNAM FE FE (III) ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 GOL 13(C3 H8 O3)
FORMUL 7 CO3 2(C O3 2-)
FORMUL 8 FE 2(FE 3+)
FORMUL 22 HOH *203(H2 O)
HELIX 1 1 ASN A 64 TRP A 68 5 5
HELIX 2 2 PRO A 81 LYS A 90 1 10
HELIX 3 3 ASN A 267 ASP A 271 5 5
HELIX 4 4 GLY A 644 ALA A 647 5 4
HELIX 5 5 SER B 12 SER B 28 1 17
HELIX 6 6 SER B 44 ALA B 54 1 11
HELIX 7 7 ASP B 63 LEU B 72 1 10
HELIX 8 8 GLN B 108 LEU B 112 5 5
HELIX 9 9 TRP B 128 TYR B 136 1 9
HELIX 10 10 CYS B 137 LEU B 139 5 3
HELIX 11 11 PRO B 145 PHE B 154 1 10
HELIX 12 12 PHE B 167 CYS B 171 5 5
HELIX 13 13 PHE B 186 ASP B 197 1 12
HELIX 14 14 HIS B 207 LEU B 214 1 8
HELIX 15 15 ASP B 219 ASP B 221 5 3
HELIX 16 16 ASP B 236 TYR B 238 5 3
HELIX 17 17 LYS B 259 GLY B 275 1 17
HELIX 18 18 ASP B 310 GLY B 316 1 7
HELIX 19 19 GLY B 316 GLU B 328 1 13
HELIX 20 20 SER B 348 SER B 362 1 15
HELIX 21 21 THR B 373 GLY B 384 1 12
HELIX 22 22 ASP B 392 CYS B 402 1 11
HELIX 23 23 ASN B 417 THR B 421 5 5
HELIX 24 24 TRP B 460 ASN B 472 1 13
HELIX 25 25 ARG B 475 PHE B 480 1 6
HELIX 26 26 SER B 492 LYS B 496 5 5
HELIX 27 27 SER B 501 LEU B 505 5 5
HELIX 28 28 TYR B 515 LYS B 527 1 13
HELIX 29 29 GLN B 536 THR B 542 1 7
HELIX 30 30 ASN B 555 LYS B 557 5 3
HELIX 31 31 GLU B 572 ASN B 576 5 5
HELIX 32 32 LYS B 593 GLY B 609 1 17
HELIX 33 33 HIS B 642 ASN B 645 5 4
HELIX 34 34 THR B 646 GLY B 652 1 7
HELIX 35 35 GLY B 652 LEU B 662 1 11
HELIX 36 36 ARG B 663 SER B 666 5 4
HELIX 37 37 SER B 668 ARG B 678 1 11
HELIX 38 38 ASN C 64 TRP C 68 5 5
HELIX 39 39 PRO C 81 LYS C 90 1 10
HELIX 40 40 GLY C 644 ALA C 647 5 4
HELIX 41 41 SER D 12 SER D 28 1 17
HELIX 42 42 SER D 44 ALA D 54 1 11
HELIX 43 43 ASP D 63 LEU D 72 1 10
HELIX 44 44 GLN D 108 LEU D 112 5 5
HELIX 45 45 TRP D 128 TYR D 136 1 9
HELIX 46 46 CYS D 137 LEU D 139 5 3
HELIX 47 47 PRO D 145 PHE D 154 1 10
HELIX 48 48 PHE D 167 GLN D 172 5 6
HELIX 49 49 PHE D 186 ASP D 197 1 12
HELIX 50 50 HIS D 207 LEU D 214 1 8
HELIX 51 51 ASP D 219 ASP D 221 5 3
HELIX 52 52 ASP D 236 TYR D 238 5 3
HELIX 53 53 LYS D 259 GLY D 275 1 17
HELIX 54 54 ASP D 310 GLY D 316 1 7
HELIX 55 55 GLY D 316 GLY D 329 1 14
HELIX 56 56 SER D 348 SER D 362 1 15
HELIX 57 57 THR D 373 GLY D 384 1 12
HELIX 58 58 ASP D 392 CYS D 402 1 11
HELIX 59 59 ASN D 417 THR D 421 5 5
HELIX 60 60 TRP D 460 ASN D 472 1 13
HELIX 61 61 ARG D 475 PHE D 480 1 6
HELIX 62 62 SER D 492 LYS D 496 5 5
HELIX 63 63 SER D 501 LEU D 505 5 5
HELIX 64 64 TYR D 515 LYS D 527 1 13
HELIX 65 65 GLN D 536 THR D 542 1 7
HELIX 66 66 ASN D 555 LYS D 557 5 3
HELIX 67 67 GLU D 572 ASN D 576 5 5
HELIX 68 68 ARG D 590 ASP D 592 5 3
HELIX 69 69 LYS D 593 GLY D 609 1 17
HELIX 70 70 HIS D 642 ASN D 645 5 4
HELIX 71 71 THR D 646 LEU D 662 1 17
HELIX 72 72 ARG D 663 SER D 666 5 4
HELIX 73 73 SER D 668 ARG D 678 1 11
SHEET 1 A 5 GLU A 69 ALA A 70 0
SHEET 2 A 5 GLY A 42 ARG A 46 -1 N ALA A 44 O GLU A 69
SHEET 3 A 5 ASP A 160 GLY A 167 -1 O ILE A 163 N MET A 45
SHEET 4 A 5 VAL A 135 LYS A 142 -1 N TYR A 136 O HIS A 166
SHEET 5 A 5 TYR A 100 SER A 101 -1 N TYR A 100 O TYR A 141
SHEET 1 B 2 GLU A 60 VAL A 61 0
SHEET 2 B 2 THR A 192 LYS A 193 -1 O THR A 192 N VAL A 61
SHEET 1 C 2 GLN A 125 ALA A 126 0
SHEET 2 C 2 GLY A 237 TYR A 238 -1 O TYR A 238 N GLN A 125
SHEET 1 D 2 GLU A 147 ASP A 149 0
SHEET 2 D 2 LYS A 154 LYS A 156 -1 O LYS A 156 N GLU A 147
SHEET 1 E 2 GLN A 173 PRO A 175 0
SHEET 2 E 2 LEU A 378 THR A 380 -1 O THR A 379 N LEU A 174
SHEET 1 F 9 LYS A 179 THR A 190 0
SHEET 2 F 9 PHE A 240 ASP A 247 -1 O LEU A 244 N TYR A 182
SHEET 3 F 9 LYS A 252 ASN A 260 -1 O THR A 254 N GLU A 245
SHEET 4 F 9 THR A 274 THR A 285 -1 O THR A 275 N ARG A 259
SHEET 5 F 9 ARG A 288 ALA A 295 -1 O ASN A 290 N GLN A 283
SHEET 6 F 9 SER A 312 PHE A 320 -1 O SER A 312 N ALA A 293
SHEET 7 F 9 GLU A 326 LEU A 332 -1 O GLU A 326 N PHE A 320
SHEET 8 F 9 VAL A 338 LYS A 345 -1 O VAL A 340 N PHE A 331
SHEET 9 F 9 LYS A 179 THR A 190 -1 N LYS A 183 O LYS A 345
SHEET 1 G 6 LYS A 393 ASN A 396 0
SHEET 2 G 6 LEU A 382 THR A 388 -1 N GLU A 386 O LYS A 395
SHEET 3 G 6 GLU A 521 GLU A 529 -1 O MET A 524 N LEU A 387
SHEET 4 G 6 LEU A 490 LYS A 498 -1 N GLY A 493 O PHE A 525
SHEET 5 G 6 THR A 477 CYS A 483 -1 N THR A 477 O LYS A 498
SHEET 6 G 6 ARG A 439 HIS A 443 -1 N ARG A 439 O VAL A 482
SHEET 1 H 2 GLN A 405 VAL A 408 0
SHEET 2 H 2 ILE A 411 PRO A 414 -1 O ILE A 413 N LEU A 406
SHEET 1 I10 SER A 557 GLY A 560 0
SHEET 2 I10 VAL A 542 ALA A 553 -1 N ILE A 552 O TRP A 558
SHEET 3 I10 SER A 677 ARG A 686 -1 O LYS A 685 N ARG A 545
SHEET 4 I10 GLU A 649 TYR A 656 -1 N LEU A 650 O ALA A 684
SHEET 5 I10 ALA A 636 TYR A 643 -1 N TYR A 643 O GLU A 649
SHEET 6 I10 GLY A 606 LYS A 612 -1 N GLY A 609 O VAL A 638
SHEET 7 I10 THR A 595 GLN A 603 -1 N GLN A 603 O GLY A 606
SHEET 8 I10 LYS A 581 THR A 587 -1 N GLY A 584 O ILE A 598
SHEET 9 I10 ARG A 570 ASN A 576 -1 N ARG A 570 O THR A 587
SHEET 10 I10 VAL A 542 ALA A 553 -1 N GLY A 546 O ALA A 571
SHEET 1 J 2 THR B 5 ALA B 10 0
SHEET 2 J 2 SER B 36 LYS B 41 1 O VAL B 40 N TRP B 8
SHEET 1 K 4 VAL B 60 LEU B 62 0
SHEET 2 K 4 THR B 250 ARG B 254 -1 O THR B 250 N LEU B 62
SHEET 3 K 4 LEU B 77 TYR B 85 -1 N LYS B 78 O ALA B 253
SHEET 4 K 4 ALA B 299 LYS B 304 -1 O LEU B 303 N ALA B 82
SHEET 1 L 6 GLY B 156 CYS B 158 0
SHEET 2 L 6 LYS B 116 HIS B 119 1 N HIS B 119 O CYS B 158
SHEET 3 L 6 VAL B 202 LYS B 206 1 O PHE B 204 N CYS B 118
SHEET 4 L 6 PHE B 94 LYS B 102 -1 N VAL B 98 O VAL B 205
SHEET 5 L 6 TYR B 223 LEU B 226 -1 O LEU B 226 N ALA B 99
SHEET 6 L 6 ARG B 232 PRO B 234 -1 O LYS B 233 N LEU B 225
SHEET 1 M 5 GLY B 156 CYS B 158 0
SHEET 2 M 5 LYS B 116 HIS B 119 1 N HIS B 119 O CYS B 158
SHEET 3 M 5 VAL B 202 LYS B 206 1 O PHE B 204 N CYS B 118
SHEET 4 M 5 PHE B 94 LYS B 102 -1 N VAL B 98 O VAL B 205
SHEET 5 M 5 ALA B 244 PRO B 247 -1 O VAL B 246 N TYR B 95
SHEET 1 N 2 VAL B 342 LEU B 347 0
SHEET 2 N 2 ILE B 366 ALA B 371 1 O VAL B 369 N ALA B 346
SHEET 1 O 4 ALA B 388 LEU B 391 0
SHEET 2 O 4 ALA B 586 THR B 589 -1 O ALA B 586 N LEU B 391
SHEET 3 O 4 VAL B 405 ASN B 411 -1 N VAL B 405 O THR B 589
SHEET 4 O 4 CYS B 637 LYS B 640 -1 O ALA B 639 N ALA B 409
SHEET 1 P 6 GLU B 482 CYS B 484 0
SHEET 2 P 6 LYS B 448 HIS B 451 1 N HIS B 451 O CYS B 484
SHEET 3 P 6 VAL B 530 LYS B 534 1 O PHE B 532 N CYS B 450
SHEET 4 P 6 TYR B 426 LYS B 433 -1 N VAL B 431 O ALA B 531
SHEET 5 P 6 TYR B 559 LEU B 562 -1 O LEU B 562 N ALA B 430
SHEET 6 P 6 ARG B 568 PRO B 570 -1 O LYS B 569 N LEU B 561
SHEET 1 Q 5 GLU B 482 CYS B 484 0
SHEET 2 Q 5 LYS B 448 HIS B 451 1 N HIS B 451 O CYS B 484
SHEET 3 Q 5 VAL B 530 LYS B 534 1 O PHE B 532 N CYS B 450
SHEET 4 Q 5 TYR B 426 LYS B 433 -1 N VAL B 431 O ALA B 531
SHEET 5 Q 5 ALA B 580 ALA B 582 -1 O ALA B 582 N TYR B 426
SHEET 1 R 5 GLU C 69 ALA C 70 0
SHEET 2 R 5 GLY C 42 ARG C 46 -1 N ALA C 44 O GLU C 69
SHEET 3 R 5 ASP C 160 GLY C 167 -1 O ILE C 163 N MET C 45
SHEET 4 R 5 VAL C 135 LYS C 142 -1 N TYR C 136 O HIS C 166
SHEET 5 R 5 TYR C 100 SER C 101 -1 N TYR C 100 O TYR C 141
SHEET 1 S 2 GLU C 60 VAL C 61 0
SHEET 2 S 2 THR C 192 LYS C 193 -1 O THR C 192 N VAL C 61
SHEET 1 T 2 GLN C 125 ALA C 126 0
SHEET 2 T 2 GLY C 237 TYR C 238 -1 O TYR C 238 N GLN C 125
SHEET 1 U 2 GLU C 147 ASP C 149 0
SHEET 2 U 2 LYS C 154 LYS C 156 -1 O LYS C 156 N GLU C 147
SHEET 1 V 2 GLN C 173 PRO C 175 0
SHEET 2 V 2 LEU C 378 THR C 380 -1 O THR C 379 N LEU C 174
SHEET 1 W 9 LYS C 179 THR C 190 0
SHEET 2 W 9 PHE C 240 ASP C 247 -1 O LEU C 244 N TYR C 182
SHEET 3 W 9 LYS C 252 ASN C 260 -1 O THR C 254 N GLU C 245
SHEET 4 W 9 THR C 274 THR C 285 -1 O THR C 275 N ARG C 259
SHEET 5 W 9 ARG C 288 ALA C 295 -1 O ASN C 290 N GLN C 283
SHEET 6 W 9 SER C 312 PHE C 320 -1 O SER C 312 N ALA C 293
SHEET 7 W 9 GLU C 326 LEU C 332 -1 O GLU C 326 N PHE C 320
SHEET 8 W 9 VAL C 338 LYS C 345 -1 O VAL C 340 N PHE C 331
SHEET 9 W 9 LYS C 179 THR C 190 -1 N LYS C 183 O LYS C 345
SHEET 1 X 6 LYS C 393 ASN C 396 0
SHEET 2 X 6 LEU C 382 THR C 388 -1 N GLU C 386 O LYS C 395
SHEET 3 X 6 GLU C 521 GLU C 529 -1 O MET C 524 N LEU C 387
SHEET 4 X 6 LEU C 490 LYS C 498 -1 N GLY C 493 O PHE C 525
SHEET 5 X 6 THR C 477 CYS C 483 -1 N THR C 477 O LYS C 498
SHEET 6 X 6 ARG C 439 HIS C 443 -1 N ARG C 439 O VAL C 482
SHEET 1 Y 2 GLN C 405 VAL C 408 0
SHEET 2 Y 2 ILE C 411 PRO C 414 -1 O ILE C 413 N LEU C 406
SHEET 1 Z10 SER C 557 GLY C 560 0
SHEET 2 Z10 VAL C 542 ALA C 553 -1 N ILE C 552 O TRP C 558
SHEET 3 Z10 SER C 677 ARG C 686 -1 O LYS C 685 N ARG C 545
SHEET 4 Z10 GLU C 649 TYR C 656 -1 N LEU C 650 O ALA C 684
SHEET 5 Z10 ALA C 636 TYR C 643 -1 N TYR C 643 O GLU C 649
SHEET 6 Z10 GLY C 606 LYS C 612 -1 N GLY C 609 O VAL C 638
SHEET 7 Z10 THR C 595 GLN C 603 -1 N GLN C 603 O GLY C 606
SHEET 8 Z10 LYS C 581 THR C 587 -1 N GLY C 584 O ILE C 598
SHEET 9 Z10 ARG C 570 ASN C 576 -1 N ARG C 570 O THR C 587
SHEET 10 Z10 VAL C 542 ALA C 553 -1 N GLY C 546 O ALA C 571
SHEET 1 AA 2 THR D 5 ALA D 10 0
SHEET 2 AA 2 SER D 36 LYS D 41 1 O VAL D 40 N ALA D 10
SHEET 1 AB 4 VAL D 60 LEU D 62 0
SHEET 2 AB 4 THR D 250 ARG D 254 -1 O THR D 250 N LEU D 62
SHEET 3 AB 4 LEU D 77 TYR D 85 -1 N VAL D 81 O VAL D 251
SHEET 4 AB 4 ALA D 299 LYS D 304 -1 O HIS D 300 N PHE D 84
SHEET 1 AC 6 GLY D 156 CYS D 158 0
SHEET 2 AC 6 LYS D 116 HIS D 119 1 N HIS D 119 O CYS D 158
SHEET 3 AC 6 VAL D 202 LYS D 206 1 O PHE D 204 N CYS D 118
SHEET 4 AC 6 PHE D 94 LYS D 102 -1 N VAL D 98 O VAL D 205
SHEET 5 AC 6 TYR D 223 LEU D 226 -1 O LEU D 226 N ALA D 99
SHEET 6 AC 6 ARG D 232 PRO D 234 -1 O LYS D 233 N LEU D 225
SHEET 1 AD 5 GLY D 156 CYS D 158 0
SHEET 2 AD 5 LYS D 116 HIS D 119 1 N HIS D 119 O CYS D 158
SHEET 3 AD 5 VAL D 202 LYS D 206 1 O PHE D 204 N CYS D 118
SHEET 4 AD 5 PHE D 94 LYS D 102 -1 N VAL D 98 O VAL D 205
SHEET 5 AD 5 ALA D 244 PRO D 247 -1 O VAL D 246 N TYR D 95
SHEET 1 AE 2 VAL D 342 LEU D 347 0
SHEET 2 AE 2 ILE D 366 ALA D 371 1 O VAL D 369 N ALA D 346
SHEET 1 AF 4 MET D 389 LEU D 391 0
SHEET 2 AF 4 ALA D 586 THR D 589 -1 O ALA D 586 N LEU D 391
SHEET 3 AF 4 VAL D 405 ASN D 411 -1 N VAL D 405 O THR D 589
SHEET 4 AF 4 CYS D 637 LYS D 640 -1 O ALA D 639 N ALA D 409
SHEET 1 AG 6 GLU D 482 CYS D 484 0
SHEET 2 AG 6 LYS D 448 HIS D 451 1 N HIS D 451 O CYS D 484
SHEET 3 AG 6 VAL D 530 LYS D 534 1 O PHE D 532 N CYS D 450
SHEET 4 AG 6 TYR D 426 LYS D 433 -1 N VAL D 431 O ALA D 531
SHEET 5 AG 6 TYR D 559 LEU D 562 -1 O LEU D 562 N ALA D 430
SHEET 6 AG 6 ARG D 568 PRO D 570 -1 O LYS D 569 N LEU D 561
SHEET 1 AH 5 GLU D 482 CYS D 484 0
SHEET 2 AH 5 LYS D 448 HIS D 451 1 N HIS D 451 O CYS D 484
SHEET 3 AH 5 VAL D 530 LYS D 534 1 O PHE D 532 N CYS D 450
SHEET 4 AH 5 TYR D 426 LYS D 433 -1 N VAL D 431 O ALA D 531
SHEET 5 AH 5 ALA D 580 ALA D 582 -1 O ALA D 582 N TYR D 426
SSBOND 1 CYS A 483 CYS A 484 1555 1555 2.03
SSBOND 2 CYS B 9 CYS B 48 1555 1555 2.07
SSBOND 3 CYS B 19 CYS B 39 1555 1555 2.06
SSBOND 4 CYS B 118 CYS B 194 1555 1555 2.06
SSBOND 5 CYS B 137 CYS B 331 1555 1555 2.04
SSBOND 6 CYS B 158 CYS B 174 1555 1555 2.04
SSBOND 7 CYS B 161 CYS B 179 1555 1555 2.04
SSBOND 8 CYS B 171 CYS B 177 1555 1555 2.02
SSBOND 9 CYS B 227 CYS B 241 1555 1555 2.04
SSBOND 10 CYS B 339 CYS B 596 1555 1555 2.04
SSBOND 11 CYS B 345 CYS B 377 1555 1555 2.02
SSBOND 12 CYS B 355 CYS B 368 1555 1555 2.05
SSBOND 13 CYS B 402 CYS B 674 1555 1555 2.04
SSBOND 14 CYS B 418 CYS B 637 1555 1555 2.05
SSBOND 15 CYS B 450 CYS B 523 1555 1555 2.05
SSBOND 16 CYS B 474 CYS B 665 1555 1555 2.03
SSBOND 17 CYS B 484 CYS B 498 1555 1555 2.06
SSBOND 18 CYS B 495 CYS B 506 1555 1555 2.06
SSBOND 19 CYS B 563 CYS B 577 1555 1555 2.04
SSBOND 20 CYS B 615 CYS B 620 1555 1555 2.04
SSBOND 21 CYS C 483 CYS C 484 1555 1555 2.04
SSBOND 22 CYS D 9 CYS D 48 1555 1555 2.05
SSBOND 23 CYS D 19 CYS D 39 1555 1555 2.04
SSBOND 24 CYS D 118 CYS D 194 1555 1555 2.05
SSBOND 25 CYS D 137 CYS D 331 1555 1555 2.04
SSBOND 26 CYS D 158 CYS D 174 1555 1555 2.03
SSBOND 27 CYS D 161 CYS D 179 1555 1555 2.01
SSBOND 28 CYS D 171 CYS D 177 1555 1555 2.03
SSBOND 29 CYS D 227 CYS D 241 1555 1555 2.02
SSBOND 30 CYS D 339 CYS D 596 1555 1555 2.05
SSBOND 31 CYS D 345 CYS D 377 1555 1555 2.04
SSBOND 32 CYS D 355 CYS D 368 1555 1555 2.07
SSBOND 33 CYS D 402 CYS D 674 1555 1555 2.01
SSBOND 34 CYS D 418 CYS D 637 1555 1555 2.04
SSBOND 35 CYS D 450 CYS D 523 1555 1555 2.04
SSBOND 36 CYS D 474 CYS D 665 1555 1555 2.03
SSBOND 37 CYS D 484 CYS D 498 1555 1555 2.05
SSBOND 38 CYS D 495 CYS D 506 1555 1555 2.03
SSBOND 39 CYS D 563 CYS D 577 1555 1555 2.05
SSBOND 40 CYS D 615 CYS D 620 1555 1555 2.04
LINK OD1 ASP D 392 FE FE D 702 1555 1555 2.01
LINK OH TYR B 517 FE FE B 702 1555 1555 2.05
LINK OD1 ASP B 392 FE FE B 702 1555 1555 2.09
LINK O3 CO3 B 701 FE FE B 702 1555 1555 2.15
LINK NE2 HIS D 585 FE FE D 702 1555 1555 2.18
LINK OH TYR D 426 FE FE D 702 1555 1555 2.20
LINK O1 CO3 D 701 FE FE D 702 1555 1555 2.20
LINK OH TYR D 517 FE FE D 702 1555 1555 2.22
LINK NE2 HIS B 585 FE FE B 702 1555 1555 2.23
LINK O3 CO3 D 701 FE FE D 702 1555 1555 2.24
LINK O1 CO3 B 701 FE FE B 702 1555 1555 2.29
LINK OH TYR B 426 FE FE B 702 1555 1555 2.38
CISPEP 1 GLU A 300 ASN A 301 0 29.70
CISPEP 2 CYS A 483 CYS A 484 0 1.92
CISPEP 3 LYS A 565 GLU A 566 0 -4.00
CISPEP 4 ARG A 591 GLN A 592 0 -18.33
CISPEP 5 GLN A 592 ALA A 593 0 4.73
CISPEP 6 GLU A 615 SER A 616 0 -17.53
CISPEP 7 TYR A 656 PRO A 657 0 2.39
CISPEP 8 ALA B 73 PRO B 74 0 -7.45
CISPEP 9 GLU B 141 PRO B 142 0 1.67
CISPEP 10 LYS B 144 PRO B 145 0 -8.63
CISPEP 11 CYS C 483 CYS C 484 0 1.71
CISPEP 12 LYS C 565 GLU C 566 0 -23.17
CISPEP 13 ARG C 591 GLN C 592 0 -15.04
CISPEP 14 GLN C 592 ALA C 593 0 -12.29
CISPEP 15 GLU C 615 SER C 616 0 -16.00
CISPEP 16 THR C 628 PRO C 629 0 10.64
CISPEP 17 TYR C 656 PRO C 657 0 2.44
CISPEP 18 ALA D 73 PRO D 74 0 -10.08
CISPEP 19 GLU D 141 PRO D 142 0 1.48
CISPEP 20 LYS D 144 PRO D 145 0 -1.53
CISPEP 21 GLU D 333 ALA D 334 0 -27.74
CISPEP 22 PRO D 335 THR D 336 0 -8.11
SITE 1 AC1 1 PHE B 211
SITE 1 AC2 4 GLY A 286 GLU A 529 ARG A 530 HOH A 809
SITE 1 AC3 10 ASP B 392 TYR B 426 THR B 452 ARG B 456
SITE 2 AC3 10 THR B 457 ALA B 458 GLY B 459 TYR B 517
SITE 3 AC3 10 HIS B 585 FE B 702
SITE 1 AC4 5 ASP B 392 TYR B 426 TYR B 517 HIS B 585
SITE 2 AC4 5 CO3 B 701
SITE 1 AC5 7 ASP B 63 ALA B 64 TYR B 95 SER B 125
SITE 2 AC5 7 PRO B 247 SER B 248 LYS B 296
SITE 1 AC6 7 TYR B 95 THR B 120 ARG B 124 SER B 125
SITE 2 AC6 7 ALA B 126 GLY B 127 TYR B 188
SITE 1 AC7 4 MET B 109 ASN B 110 LEU B 134 ASP B 138
SITE 1 AC8 5 CYS B 227 LEU B 228 ASP B 240 CYS B 241
SITE 2 AC8 5 HIS B 242
SITE 1 AC9 2 GLU B 375 THR B 667
SITE 1 BC1 4 PRO A 122 GLY B 502 LEU B 503 ASN B 504
SITE 1 BC2 11 GLY C 39 GLY C 40 TYR C 165 ARG C 288
SITE 2 BC2 11 SER C 316 GLY C 317 GLY C 318 PHE C 320
SITE 3 BC2 11 PHE C 400 HOH C 820 HOH C 824
SITE 1 BC3 10 ASP D 392 TYR D 426 THR D 452 ARG D 456
SITE 2 BC3 10 THR D 457 ALA D 458 GLY D 459 TYR D 517
SITE 3 BC3 10 HIS D 585 FE D 702
SITE 1 BC4 5 ASP D 392 TYR D 426 TYR D 517 HIS D 585
SITE 2 BC4 5 CO3 D 701
SITE 1 BC5 7 TYR D 95 THR D 120 ARG D 124 SER D 125
SITE 2 BC5 7 ALA D 126 GLY D 127 TYR D 188
SITE 1 BC6 4 GLU D 375 GLY D 487 THR D 667 SER D 668
SITE 1 BC7 4 CYS D 227 LEU D 228 HIS D 242 GLU D 318
SITE 1 BC8 3 LEU D 134 ASP D 138 HOH D 855
CRYST1 128.023 153.509 169.511 90.00 90.00 90.00 P 21 21 21 8
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 0.007811 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006514 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005899 0.00000
MTRIX1 1 -0.999582 -0.015095 -0.024649 61.49030 1
MTRIX2 1 0.013577 -0.998068 0.060633 -78.00640 1
MTRIX3 1 -0.025517 0.060273 0.997856 2.23577 1
MTRIX1 2 -0.997995 -0.023213 -0.058881 59.47580 1
MTRIX2 2 0.019266 -0.997584 0.066740 -77.95300 1
MTRIX3 2 -0.060288 0.065472 0.996032 5.15397 1
(ATOM LINES ARE NOT SHOWN.)
END
