HEADER OXIDOREDUCTASE 22-FEB-13 4JCO
TITLE 1.7 A RESOLUTION STRUCTURE OF WILD TYPE MALATE DEHYDROGENASE FROM
TITLE 2 HALOARCULA MARISMORTUI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MALATE DEHYDROGENASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 EC: 1.1.1.37;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HALOARCULA MARISMORTUI;
SOURCE 3 ORGANISM_TAXID: 2238;
SOURCE 4 STRAIN: HMS174;
SOURCE 5 GENE: MDH, RRNAC2706;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET11A
KEYWDS HALOPHILE, OXIDOREDUCTASE, MALATE DEHYDROGENASE TRICARBOXYLIC ACID
KEYWDS 2 CYCLE
EXPDTA X-RAY DIFFRACTION
AUTHOR F.M.D.VELLIEUX
REVDAT 3 08-NOV-23 4JCO 1 REMARK LINK
REVDAT 2 20-NOV-19 4JCO 1 REMARK
REVDAT 1 20-MAR-13 4JCO 0
JRNL AUTH F.M.D.VELLIEUX
JRNL TITL 1.7 A RESOLUTION STRUCTURE OF WILD TYPE MALATE DEHYDROGENASE
JRNL TITL 2 FROM HALOARCULA MARISMORTUI
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH E.FIORAVANTI,F.M.VELLIEUX,P.AMARA,D.MADERN,M.WEIK
REMARK 1 TITL SPECIFIC RADIATION DAMAGE TO ACIDIC RESIDUES AND ITS
REMARK 1 TITL 2 RELATION TO THEIR CHEMICAL AND STRUCTURAL ENVIRONMENT.
REMARK 1 REF J SYNCHROTRON RADIAT V. 14 84 2007
REMARK 1 REFN ISSN 0909-0495
REMARK 1 PMID 17211074
REMARK 1 DOI 10.1107/S0909049506038623
REMARK 1 REFERENCE 2
REMARK 1 AUTH A.IRIMIA,C.EBEL,D.MADERN,S.B.RICHARD,L.W.COSENZA,G.ZACCAI,
REMARK 1 AUTH 2 F.M.VELLIEUX
REMARK 1 TITL THE OLIGOMERIC STATES OF HALOARCULA MARISMORTUI MALATE
REMARK 1 TITL 2 DEHYDROGENASE ARE MODULATED BY SOLVENT COMPONENTS AS SHOWN
REMARK 1 TITL 3 BY CRYSTALLOGRAPHIC AND BIOCHEMICAL STUDIES.
REMARK 1 REF J.MOL.BIOL. V. 326 859 2003
REMARK 1 REFN ISSN 0022-2836
REMARK 1 PMID 12581646
REMARK 1 DOI 10.1016/S0022-2836(02)01450-X
REMARK 1 REFERENCE 3
REMARK 1 AUTH S.B.RICHARD,D.MADERN,E.GARCIN,G.ZACCAI
REMARK 1 TITL HALOPHILIC ADAPTATION: NOVEL SOLVENT PROTEIN INTERACTIONS
REMARK 1 TITL 2 OBSERVED IN THE 2.9 AND 2.6 A RESOLUTION STRUCTURES OF THE
REMARK 1 TITL 3 WILD TYPE AND A MUTANT OF MALATE DEHYDROGENASE FROM
REMARK 1 TITL 4 HALOARCULA MARISMORTUI.
REMARK 1 REF BIOCHEMISTRY V. 39 992 2000
REMARK 1 REFN ISSN 0006-2960
REMARK 1 PMID 10653643
REMARK 1 DOI 10.1021/BI991001A
REMARK 1 REFERENCE 4
REMARK 1 AUTH O.DYM,M.MEVARECH,J.L.SUSSMAN
REMARK 1 TITL STRUCTURAL FEATURES THAT STABILIZE HALOPHILIC MALATE
REMARK 1 TITL 2 DEHYDROGENASE FROM AN ARCHAEBACTERIUM.
REMARK 1 REF SCIENCE V. 267 1344 1995
REMARK 1 REFN ISSN 0036-8075
REMARK 1 PMID 17812611
REMARK 1 DOI 10.1126/SCIENCE.267.5202.1344
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.1_1168)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.96
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.990
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 192185
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.226
REMARK 3 R VALUE (WORKING SET) : 0.224
REMARK 3 FREE R VALUE : 0.257
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 9607
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 42.9778 - 5.2791 0.99 6161 323 0.2102 0.2180
REMARK 3 2 5.2791 - 4.1913 0.99 6147 324 0.1756 0.1900
REMARK 3 3 4.1913 - 3.6619 1.00 6116 322 0.1818 0.1949
REMARK 3 4 3.6619 - 3.3272 1.00 6132 322 0.2006 0.2401
REMARK 3 5 3.3272 - 3.0888 1.00 6107 322 0.2129 0.2482
REMARK 3 6 3.0888 - 2.9067 0.99 6083 320 0.2095 0.2510
REMARK 3 7 2.9067 - 2.7612 1.00 6088 320 0.2177 0.2715
REMARK 3 8 2.7612 - 2.6410 0.99 6089 321 0.2223 0.2501
REMARK 3 9 2.6410 - 2.5393 0.99 6068 319 0.2250 0.2556
REMARK 3 10 2.5393 - 2.4517 0.99 6043 318 0.2265 0.2725
REMARK 3 11 2.4517 - 2.3751 0.99 6044 318 0.2284 0.2566
REMARK 3 12 2.3751 - 2.3072 0.99 6095 321 0.2288 0.2554
REMARK 3 13 2.3072 - 2.2464 0.99 6073 319 0.2256 0.2572
REMARK 3 14 2.2464 - 2.1916 1.00 6062 319 0.2286 0.2792
REMARK 3 15 2.1916 - 2.1418 0.99 6086 320 0.2293 0.2854
REMARK 3 16 2.1418 - 2.0962 1.00 6120 322 0.2311 0.2938
REMARK 3 17 2.0962 - 2.0543 1.00 6045 319 0.2348 0.2965
REMARK 3 18 2.0543 - 2.0155 1.00 6099 321 0.2395 0.2759
REMARK 3 19 2.0155 - 1.9795 1.00 6049 318 0.2402 0.2694
REMARK 3 20 1.9795 - 1.9460 1.00 6086 320 0.2391 0.2788
REMARK 3 21 1.9460 - 1.9146 1.00 6100 321 0.2544 0.3072
REMARK 3 22 1.9146 - 1.8851 1.00 6088 321 0.2662 0.2965
REMARK 3 23 1.8851 - 1.8574 1.00 6045 318 0.2736 0.3215
REMARK 3 24 1.8574 - 1.8313 1.00 6131 323 0.2853 0.3318
REMARK 3 25 1.8313 - 1.8065 1.00 5994 315 0.2926 0.3400
REMARK 3 26 1.8065 - 1.7830 1.00 6127 323 0.3025 0.3394
REMARK 3 27 1.7830 - 1.7608 1.00 6090 320 0.3006 0.3117
REMARK 3 28 1.7608 - 1.7395 1.00 6014 317 0.3087 0.3248
REMARK 3 29 1.7395 - 1.7193 1.00 6106 321 0.3250 0.3444
REMARK 3 30 1.7193 - 1.7000 1.00 6090 320 0.3274 0.3698
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.240
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.350
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) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
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 : 0.008 9505
REMARK 3 ANGLE : 1.175 12955
REMARK 3 CHIRALITY : 0.080 1437
REMARK 3 PLANARITY : 0.006 1792
REMARK 3 DIHEDRAL : 13.617 3517
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 28
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID 22:119)
REMARK 3 ORIGIN FOR THE GROUP (A): 13.4566 20.6785 35.4858
REMARK 3 T TENSOR
REMARK 3 T11: 0.2680 T22: 0.1753
REMARK 3 T33: 0.1562 T12: 0.0119
REMARK 3 T13: -0.0238 T23: -0.0567
REMARK 3 L TENSOR
REMARK 3 L11: 0.7705 L22: 0.6359
REMARK 3 L33: 2.2034 L12: -0.3442
REMARK 3 L13: -1.0941 L23: 0.5116
REMARK 3 S TENSOR
REMARK 3 S11: 0.0525 S12: 0.0458 S13: 0.0738
REMARK 3 S21: -0.1138 S22: -0.1042 S23: 0.0491
REMARK 3 S31: -0.4446 S32: -0.1564 S33: 0.0577
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 120:132)
REMARK 3 ORIGIN FOR THE GROUP (A): -0.7133 19.0139 39.4854
REMARK 3 T TENSOR
REMARK 3 T11: 0.2202 T22: 0.3298
REMARK 3 T33: 0.2166 T12: 0.0347
REMARK 3 T13: -0.0082 T23: -0.1035
REMARK 3 L TENSOR
REMARK 3 L11: 7.2169 L22: 2.0690
REMARK 3 L33: 5.3094 L12: -0.7722
REMARK 3 L13: 1.1153 L23: 1.5460
REMARK 3 S TENSOR
REMARK 3 S11: -0.0196 S12: 0.2628 S13: 0.0560
REMARK 3 S21: 0.1467 S22: -0.1049 S23: 0.3651
REMARK 3 S31: 0.0668 S32: -0.5201 S33: 0.0650
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN A AND RESID 133:212)
REMARK 3 ORIGIN FOR THE GROUP (A): 19.1552 9.0375 52.0984
REMARK 3 T TENSOR
REMARK 3 T11: 0.2226 T22: 0.1675
REMARK 3 T33: 0.0980 T12: -0.0299
REMARK 3 T13: 0.0228 T23: -0.0668
REMARK 3 L TENSOR
REMARK 3 L11: 1.0390 L22: 1.3056
REMARK 3 L33: 1.0758 L12: -0.6784
REMARK 3 L13: 0.1284 L23: -0.1000
REMARK 3 S TENSOR
REMARK 3 S11: -0.0427 S12: -0.0076 S13: -0.0041
REMARK 3 S21: 0.1507 S22: -0.0651 S23: 0.0489
REMARK 3 S31: -0.0709 S32: -0.0672 S33: 0.0889
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN A AND RESID 219:238)
REMARK 3 ORIGIN FOR THE GROUP (A): 32.1807 12.1719 61.5350
REMARK 3 T TENSOR
REMARK 3 T11: 0.4081 T22: 0.3376
REMARK 3 T33: 0.2389 T12: -0.0407
REMARK 3 T13: -0.0486 T23: -0.0863
REMARK 3 L TENSOR
REMARK 3 L11: 0.2448 L22: 2.4835
REMARK 3 L33: 3.3768 L12: -0.2173
REMARK 3 L13: 0.2092 L23: -0.5740
REMARK 3 S TENSOR
REMARK 3 S11: -0.1057 S12: -0.2844 S13: 0.1144
REMARK 3 S21: 0.9161 S22: 0.0339 S23: -0.4259
REMARK 3 S31: -0.5358 S32: 0.2568 S33: 0.0770
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN A AND RESID 239:266)
REMARK 3 ORIGIN FOR THE GROUP (A): 21.4018 12.8225 41.9997
REMARK 3 T TENSOR
REMARK 3 T11: 0.2651 T22: 0.1504
REMARK 3 T33: 0.0959 T12: -0.0106
REMARK 3 T13: 0.0090 T23: -0.0293
REMARK 3 L TENSOR
REMARK 3 L11: 2.1113 L22: 3.1571
REMARK 3 L33: 0.9975 L12: 1.4743
REMARK 3 L13: 0.3615 L23: 1.0561
REMARK 3 S TENSOR
REMARK 3 S11: -0.0262 S12: 0.0411 S13: 0.1373
REMARK 3 S21: 0.1272 S22: 0.0704 S23: 0.0399
REMARK 3 S31: -0.3051 S32: 0.0767 S33: 0.0006
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (CHAIN A AND RESID 267:325)
REMARK 3 ORIGIN FOR THE GROUP (A): 11.4085 5.3055 57.8331
REMARK 3 T TENSOR
REMARK 3 T11: 0.3207 T22: 0.2573
REMARK 3 T33: 0.1508 T12: -0.0467
REMARK 3 T13: 0.0593 T23: -0.0462
REMARK 3 L TENSOR
REMARK 3 L11: 1.7911 L22: 2.1196
REMARK 3 L33: 2.1032 L12: -0.6095
REMARK 3 L13: -0.0078 L23: -0.0022
REMARK 3 S TENSOR
REMARK 3 S11: -0.0402 S12: -0.2204 S13: -0.1009
REMARK 3 S21: 0.4329 S22: -0.0409 S23: 0.1286
REMARK 3 S31: 0.2870 S32: -0.1806 S33: 0.1084
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (CHAIN A AND RESID 326:330)
REMARK 3 ORIGIN FOR THE GROUP (A): 1.7565 21.6352 60.2490
REMARK 3 T TENSOR
REMARK 3 T11: 0.5052 T22: 0.3835
REMARK 3 T33: 0.5118 T12: -0.0668
REMARK 3 T13: 0.2483 T23: -0.2787
REMARK 3 L TENSOR
REMARK 3 L11: 0.5041 L22: 2.4920
REMARK 3 L33: 3.4045 L12: -0.8192
REMARK 3 L13: -0.6566 L23: 2.7880
REMARK 3 S TENSOR
REMARK 3 S11: 0.1067 S12: -0.0478 S13: 0.0841
REMARK 3 S21: 0.1732 S22: -0.1118 S23: 0.1945
REMARK 3 S31: -0.3057 S32: -0.3100 S33: 0.8073
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: (CHAIN B AND RESID 22:98)
REMARK 3 ORIGIN FOR THE GROUP (A): 38.6442 17.3094 39.1604
REMARK 3 T TENSOR
REMARK 3 T11: 0.2172 T22: 0.1816
REMARK 3 T33: 0.1526 T12: -0.0679
REMARK 3 T13: -0.0428 T23: -0.0111
REMARK 3 L TENSOR
REMARK 3 L11: 1.9131 L22: 0.7365
REMARK 3 L33: 0.6990 L12: 0.8671
REMARK 3 L13: -0.4207 L23: -0.1951
REMARK 3 S TENSOR
REMARK 3 S11: 0.0698 S12: -0.1688 S13: 0.1300
REMARK 3 S21: 0.2402 S22: -0.1404 S23: -0.0205
REMARK 3 S31: -0.3199 S32: 0.2511 S33: 0.0615
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: (CHAIN B AND RESID 99:106)
REMARK 3 ORIGIN FOR THE GROUP (A): 34.6662 38.4483 26.8648
REMARK 3 T TENSOR
REMARK 3 T11: 1.6279 T22: 1.0351
REMARK 3 T33: 0.6987 T12: 0.4932
REMARK 3 T13: 0.3651 T23: 0.0354
REMARK 3 L TENSOR
REMARK 3 L11: 5.7693 L22: 1.2727
REMARK 3 L33: 3.6681 L12: -2.5876
REMARK 3 L13: 2.1625 L23: -0.9512
REMARK 3 S TENSOR
REMARK 3 S11: -0.0711 S12: 0.2612 S13: 0.4070
REMARK 3 S21: 0.7586 S22: 0.3225 S23: 0.1515
REMARK 3 S31: -0.7834 S32: -0.6811 S33: 0.0744
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: (CHAIN B AND RESID 107:128)
REMARK 3 ORIGIN FOR THE GROUP (A): 46.2186 32.5306 25.7495
REMARK 3 T TENSOR
REMARK 3 T11: 0.5360 T22: 0.3188
REMARK 3 T33: 0.2881 T12: -0.1572
REMARK 3 T13: 0.0113 T23: 0.0116
REMARK 3 L TENSOR
REMARK 3 L11: 6.3117 L22: 6.2468
REMARK 3 L33: 8.9365 L12: -3.9364
REMARK 3 L13: 3.3976 L23: -4.3356
REMARK 3 S TENSOR
REMARK 3 S11: 0.0253 S12: -0.5957 S13: 0.5025
REMARK 3 S21: 0.1681 S22: -0.1576 S23: -0.5157
REMARK 3 S31: -1.2968 S32: 0.0121 S33: 0.1102
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: (CHAIN B AND RESID 129:132)
REMARK 3 ORIGIN FOR THE GROUP (A): 55.6181 17.9726 33.8611
REMARK 3 T TENSOR
REMARK 3 T11: 0.3236 T22: 0.7446
REMARK 3 T33: 0.6910 T12: -0.1631
REMARK 3 T13: 0.0882 T23: -0.1057
REMARK 3 L TENSOR
REMARK 3 L11: 7.0034 L22: 0.8189
REMARK 3 L33: 3.7092 L12: 1.8060
REMARK 3 L13: 3.7586 L23: 0.1955
REMARK 3 S TENSOR
REMARK 3 S11: 0.4231 S12: 0.5762 S13: -0.2421
REMARK 3 S21: -0.0677 S22: 0.4594 S23: -1.0525
REMARK 3 S31: -0.2220 S32: 1.0372 S33: -0.5067
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: (CHAIN B AND RESID 133:212)
REMARK 3 ORIGIN FOR THE GROUP (A): 33.7325 18.3016 15.7540
REMARK 3 T TENSOR
REMARK 3 T11: 0.2170 T22: 0.1239
REMARK 3 T33: 0.1529 T12: -0.0356
REMARK 3 T13: 0.0061 T23: 0.0211
REMARK 3 L TENSOR
REMARK 3 L11: 1.3825 L22: 0.4267
REMARK 3 L33: 1.2497 L12: 0.6629
REMARK 3 L13: 0.4617 L23: 0.4731
REMARK 3 S TENSOR
REMARK 3 S11: -0.0024 S12: -0.0586 S13: 0.0696
REMARK 3 S21: -0.0507 S22: -0.0492 S23: -0.0726
REMARK 3 S31: -0.1216 S32: 0.1207 S33: 0.0645
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: (CHAIN B AND RESID 219:259)
REMARK 3 ORIGIN FOR THE GROUP (A): 24.4206 22.8272 17.7367
REMARK 3 T TENSOR
REMARK 3 T11: 0.3358 T22: 0.1568
REMARK 3 T33: 0.2233 T12: -0.0214
REMARK 3 T13: -0.0076 T23: 0.0085
REMARK 3 L TENSOR
REMARK 3 L11: 0.5322 L22: 1.7683
REMARK 3 L33: 2.2908 L12: -0.0703
REMARK 3 L13: -0.1364 L23: -0.2191
REMARK 3 S TENSOR
REMARK 3 S11: -0.0430 S12: 0.0163 S13: 0.1899
REMARK 3 S21: -0.0497 S22: 0.0130 S23: 0.0862
REMARK 3 S31: -0.5210 S32: -0.2166 S33: 0.0636
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: (CHAIN B AND RESID 260:330)
REMARK 3 ORIGIN FOR THE GROUP (A): 42.3058 18.2813 10.9969
REMARK 3 T TENSOR
REMARK 3 T11: 0.2293 T22: 0.1869
REMARK 3 T33: 0.1821 T12: -0.0455
REMARK 3 T13: 0.0270 T23: 0.0156
REMARK 3 L TENSOR
REMARK 3 L11: 0.3855 L22: 1.9134
REMARK 3 L33: 1.7224 L12: 0.2627
REMARK 3 L13: -0.1545 L23: -0.6075
REMARK 3 S TENSOR
REMARK 3 S11: -0.0141 S12: 0.0342 S13: 0.0589
REMARK 3 S21: -0.0210 S22: -0.0228 S23: -0.2027
REMARK 3 S31: -0.2427 S32: 0.2850 S33: 0.0363
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: (CHAIN C AND RESID 22:100)
REMARK 3 ORIGIN FOR THE GROUP (A): 15.4070 -19.2851 29.2082
REMARK 3 T TENSOR
REMARK 3 T11: 0.2154 T22: 0.1461
REMARK 3 T33: 0.1248 T12: -0.0253
REMARK 3 T13: 0.0529 T23: -0.0268
REMARK 3 L TENSOR
REMARK 3 L11: 2.0556 L22: 1.0355
REMARK 3 L33: 2.2727 L12: 0.3988
REMARK 3 L13: 0.8941 L23: 0.3398
REMARK 3 S TENSOR
REMARK 3 S11: 0.0136 S12: -0.1129 S13: -0.1248
REMARK 3 S21: 0.1720 S22: -0.0809 S23: 0.0529
REMARK 3 S31: 0.2567 S32: -0.1832 S33: 0.0664
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: (CHAIN C AND RESID 101:132)
REMARK 3 ORIGIN FOR THE GROUP (A): 9.2519 -26.0873 12.2141
REMARK 3 T TENSOR
REMARK 3 T11: 0.3003 T22: 0.1827
REMARK 3 T33: 0.2236 T12: -0.0601
REMARK 3 T13: 0.0122 T23: -0.0432
REMARK 3 L TENSOR
REMARK 3 L11: 3.6445 L22: 2.8428
REMARK 3 L33: 7.8304 L12: -1.4128
REMARK 3 L13: -3.3329 L23: 2.8195
REMARK 3 S TENSOR
REMARK 3 S11: -0.0356 S12: -0.0383 S13: -0.0275
REMARK 3 S21: -0.1637 S22: 0.0139 S23: 0.0535
REMARK 3 S31: 0.4571 S32: 0.0436 S33: 0.0471
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: (CHAIN C AND RESID 133:212)
REMARK 3 ORIGIN FOR THE GROUP (A): 21.4135 -9.5580 8.6454
REMARK 3 T TENSOR
REMARK 3 T11: 0.1708 T22: 0.1380
REMARK 3 T33: 0.1099 T12: -0.0017
REMARK 3 T13: 0.0117 T23: -0.0442
REMARK 3 L TENSOR
REMARK 3 L11: 1.1071 L22: 0.9072
REMARK 3 L33: 0.6757 L12: 0.6544
REMARK 3 L13: -0.3256 L23: -0.3184
REMARK 3 S TENSOR
REMARK 3 S11: -0.0729 S12: 0.1427 S13: -0.0388
REMARK 3 S21: -0.1664 S22: 0.0022 S23: 0.0122
REMARK 3 S31: 0.0281 S32: -0.0722 S33: 0.0687
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: (CHAIN C AND RESID 219:244)
REMARK 3 ORIGIN FOR THE GROUP (A): 35.1393 -14.6391 3.0663
REMARK 3 T TENSOR
REMARK 3 T11: 0.4033 T22: 0.2287
REMARK 3 T33: 0.1809 T12: 0.0413
REMARK 3 T13: 0.0686 T23: -0.0406
REMARK 3 L TENSOR
REMARK 3 L11: 0.6912 L22: 2.1308
REMARK 3 L33: 3.9205 L12: 0.5706
REMARK 3 L13: -0.6603 L23: -2.5856
REMARK 3 S TENSOR
REMARK 3 S11: -0.0325 S12: 0.1305 S13: -0.1411
REMARK 3 S21: -0.6721 S22: -0.0525 S23: -0.1765
REMARK 3 S31: 0.5017 S32: 0.3663 S33: 0.0944
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: (CHAIN C AND RESID 245:270)
REMARK 3 ORIGIN FOR THE GROUP (A): 20.1220 -8.5990 19.5633
REMARK 3 T TENSOR
REMARK 3 T11: 0.2149 T22: 0.1422
REMARK 3 T33: 0.0920 T12: -0.0142
REMARK 3 T13: 0.0239 T23: -0.0384
REMARK 3 L TENSOR
REMARK 3 L11: 1.8616 L22: 1.8539
REMARK 3 L33: 0.9565 L12: -1.2751
REMARK 3 L13: 1.1134 L23: -1.2990
REMARK 3 S TENSOR
REMARK 3 S11: -0.0160 S12: -0.0149 S13: -0.0212
REMARK 3 S21: 0.1274 S22: -0.0456 S23: 0.0907
REMARK 3 S31: -0.0347 S32: -0.0738 S33: 0.0465
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: (CHAIN C AND RESID 271:319)
REMARK 3 ORIGIN FOR THE GROUP (A): 14.0649 -5.0975 2.0285
REMARK 3 T TENSOR
REMARK 3 T11: 0.1914 T22: 0.1593
REMARK 3 T33: 0.1131 T12: 0.0131
REMARK 3 T13: -0.0251 T23: -0.0396
REMARK 3 L TENSOR
REMARK 3 L11: 2.1309 L22: 2.0476
REMARK 3 L33: 3.5442 L12: 0.6912
REMARK 3 L13: -0.6041 L23: -0.3498
REMARK 3 S TENSOR
REMARK 3 S11: -0.0902 S12: 0.2531 S13: -0.0067
REMARK 3 S21: -0.3140 S22: -0.0274 S23: 0.1031
REMARK 3 S31: -0.3304 S32: -0.1429 S33: 0.0847
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: (CHAIN C AND RESID 320:330)
REMARK 3 ORIGIN FOR THE GROUP (A): 9.6792 -20.5665 -2.8873
REMARK 3 T TENSOR
REMARK 3 T11: 0.4813 T22: 0.2787
REMARK 3 T33: 0.1964 T12: -0.0267
REMARK 3 T13: 0.0094 T23: -0.1065
REMARK 3 L TENSOR
REMARK 3 L11: 3.3799 L22: 2.8525
REMARK 3 L33: 5.1726 L12: -1.1466
REMARK 3 L13: -0.2943 L23: 2.1510
REMARK 3 S TENSOR
REMARK 3 S11: 0.1499 S12: -0.0030 S13: -0.2345
REMARK 3 S21: -0.5273 S22: -0.4205 S23: 0.3960
REMARK 3 S31: 0.4078 S32: -0.2911 S33: 0.2891
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: (CHAIN D AND RESID 22:76)
REMARK 3 ORIGIN FOR THE GROUP (A): 38.0485 -16.0553 22.6680
REMARK 3 T TENSOR
REMARK 3 T11: 0.1232 T22: 0.1389
REMARK 3 T33: 0.1029 T12: 0.0063
REMARK 3 T13: 0.0367 T23: 0.0089
REMARK 3 L TENSOR
REMARK 3 L11: 2.3774 L22: 1.9026
REMARK 3 L33: 2.0084 L12: -1.1299
REMARK 3 L13: 1.2314 L23: -0.7490
REMARK 3 S TENSOR
REMARK 3 S11: -0.0135 S12: 0.1108 S13: -0.0978
REMARK 3 S21: -0.0688 S22: -0.0660 S23: -0.0805
REMARK 3 S31: 0.1216 S32: 0.2102 S33: 0.0737
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: (CHAIN D AND RESID 77:95)
REMARK 3 ORIGIN FOR THE GROUP (A): 47.9549 -15.5027 23.9826
REMARK 3 T TENSOR
REMARK 3 T11: 0.1297 T22: 0.2577
REMARK 3 T33: 0.2177 T12: 0.0338
REMARK 3 T13: 0.0627 T23: 0.0680
REMARK 3 L TENSOR
REMARK 3 L11: 3.5364 L22: 0.0304
REMARK 3 L33: 3.0736 L12: 0.2080
REMARK 3 L13: 0.5616 L23: 0.2691
REMARK 3 S TENSOR
REMARK 3 S11: -0.1152 S12: 0.5703 S13: 0.1106
REMARK 3 S21: -0.1810 S22: -0.1008 S23: -0.2526
REMARK 3 S31: 0.0784 S32: 0.6038 S33: 0.1156
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: (CHAIN D AND RESID 96:106)
REMARK 3 ORIGIN FOR THE GROUP (A): 39.1317 -33.8843 34.7596
REMARK 3 T TENSOR
REMARK 3 T11: 0.8526 T22: 0.3959
REMARK 3 T33: 0.5366 T12: -0.1595
REMARK 3 T13: -0.2426 T23: 0.1214
REMARK 3 L TENSOR
REMARK 3 L11: 1.4270 L22: 4.3192
REMARK 3 L33: 5.2122 L12: 2.4824
REMARK 3 L13: -2.7276 L23: -4.7447
REMARK 3 S TENSOR
REMARK 3 S11: 0.5539 S12: -0.3690 S13: -0.5160
REMARK 3 S21: 0.0018 S22: -0.0593 S23: 0.6682
REMARK 3 S31: 1.7908 S32: -1.0282 S33: -0.3296
REMARK 3 TLS GROUP : 25
REMARK 3 SELECTION: (CHAIN D AND RESID 107:132)
REMARK 3 ORIGIN FOR THE GROUP (A): 49.5423 -28.8828 35.8071
REMARK 3 T TENSOR
REMARK 3 T11: 0.3708 T22: 0.3766
REMARK 3 T33: 0.2845 T12: 0.0902
REMARK 3 T13: 0.0311 T23: 0.0388
REMARK 3 L TENSOR
REMARK 3 L11: 3.0387 L22: 4.2307
REMARK 3 L33: 3.6265 L12: 0.4599
REMARK 3 L13: -1.7395 L23: -1.6393
REMARK 3 S TENSOR
REMARK 3 S11: -0.1472 S12: 0.4859 S13: -0.2553
REMARK 3 S21: 0.1341 S22: 0.2229 S23: 0.1712
REMARK 3 S31: 0.9125 S32: 0.1262 S33: 0.2327
REMARK 3 TLS GROUP : 26
REMARK 3 SELECTION: (CHAIN D AND RESID 132:233)
REMARK 3 ORIGIN FOR THE GROUP (A): 31.9984 -18.6329 47.3347
REMARK 3 T TENSOR
REMARK 3 T11: 0.2327 T22: 0.1157
REMARK 3 T33: 0.1359 T12: -0.0171
REMARK 3 T13: 0.0090 T23: 0.0299
REMARK 3 L TENSOR
REMARK 3 L11: 1.5200 L22: 1.0809
REMARK 3 L33: 1.3246 L12: -0.9338
REMARK 3 L13: 0.0833 L23: 0.1436
REMARK 3 S TENSOR
REMARK 3 S11: -0.0604 S12: -0.0306 S13: -0.0930
REMARK 3 S21: 0.1609 S22: -0.0015 S23: -0.0297
REMARK 3 S31: 0.1329 S32: 0.0795 S33: 0.0587
REMARK 3 TLS GROUP : 27
REMARK 3 SELECTION: (CHAIN D AND RESID 234:270)
REMARK 3 ORIGIN FOR THE GROUP (A): 31.3330 -17.5059 37.1911
REMARK 3 T TENSOR
REMARK 3 T11: 0.1567 T22: 0.1015
REMARK 3 T33: 0.1308 T12: 0.0343
REMARK 3 T13: 0.0324 T23: 0.0234
REMARK 3 L TENSOR
REMARK 3 L11: 1.8715 L22: 1.8771
REMARK 3 L33: 1.7955 L12: 0.7609
REMARK 3 L13: 0.6919 L23: 0.4953
REMARK 3 S TENSOR
REMARK 3 S11: -0.0711 S12: -0.0018 S13: -0.0929
REMARK 3 S21: 0.0178 S22: 0.0636 S23: -0.0087
REMARK 3 S31: 0.2806 S32: 0.0915 S33: 0.0516
REMARK 3 TLS GROUP : 28
REMARK 3 SELECTION: (CHAIN D AND RESID 271:330)
REMARK 3 ORIGIN FOR THE GROUP (A): 42.5441 -19.5548 53.4432
REMARK 3 T TENSOR
REMARK 3 T11: 0.2313 T22: 0.2191
REMARK 3 T33: 0.1660 T12: -0.0079
REMARK 3 T13: -0.0230 T23: 0.0504
REMARK 3 L TENSOR
REMARK 3 L11: 1.2047 L22: 2.5392
REMARK 3 L33: 2.6002 L12: -0.8679
REMARK 3 L13: -0.1984 L23: -0.7807
REMARK 3 S TENSOR
REMARK 3 S11: -0.1016 S12: -0.1834 S13: -0.0109
REMARK 3 S21: 0.2066 S22: -0.0745 S23: -0.1910
REMARK 3 S31: 0.1305 S32: 0.3273 S33: 0.1463
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4JCO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-FEB-13.
REMARK 100 THE DEPOSITION ID IS D_1000077879.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-FEB-05
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.00
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.939
REMARK 200 MONOCHROMATOR : SILICON (1 1 1) CHANNEL-CUT
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 192220
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 123.792
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 3.790
REMARK 200 R MERGE (I) : 0.10900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.5200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.74
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.79
REMARK 200 R MERGE FOR SHELL (I) : 1.22400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER, DIFFERENCE
REMARK 200 FOURIER
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: PDB ENTRY 2J5K
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.91
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.41
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 58% MPD, PH 7.00, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 63.40650
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 57.03250
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 63.40650
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 57.03250
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 17580 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 41780 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -441.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH C 760 LIES ON A SPECIAL POSITION.
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 21
REMARK 465 MET B 21
REMARK 465 MET C 21
REMARK 465 MET D 21
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 O HOH A 592 O HOH A 803 2.02
REMARK 500 O HOH D 749 O HOH D 805 2.14
REMARK 500 NH1 ARG A 292 OD2 ASP D 209 2.15
REMARK 500 OE2 GLU B 48 NH1 ARG B 79 2.16
REMARK 500 O HOH D 595 O HOH D 806 2.16
REMARK 500 O HOH B 660 O HOH B 748 2.19
REMARK 500 O HOH B 809 O HOH B 853 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 793 O HOH D 719 4556 2.19
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 ASP A 132A -74.03 -79.02
REMARK 500 ASP A 211 79.04 -118.53
REMARK 500 GLU A 247 -71.21 -145.48
REMARK 500 PHE A 279 15.28 59.56
REMARK 500 ASP B 47 -29.88 82.59
REMARK 500 ARG B 102 -72.29 -156.32
REMARK 500 GLN B 103 101.32 62.58
REMARK 500 ASP B 132A -76.25 -77.03
REMARK 500 ALA B 198 48.43 -87.94
REMARK 500 GLU B 247 -69.13 -143.65
REMARK 500 PHE B 279 14.68 58.43
REMARK 500 ALA C 198 49.06 -88.70
REMARK 500 ASP C 211 79.11 -118.97
REMARK 500 GLU C 247 -69.94 -142.97
REMARK 500 PHE C 279 15.51 59.39
REMARK 500 ARG D 102 -31.07 43.36
REMARK 500 GLN D 103 -102.90 -10.06
REMARK 500 ASP D 132A -71.07 -83.01
REMARK 500 ALA D 198 49.07 -87.39
REMARK 500 GLU D 247 -68.97 -145.11
REMARK 500 PHE D 279 14.53 59.37
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 GLN D 103 PRO D 105 -148.30
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 NA A 405 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 47 OD2
REMARK 620 2 ASP C 264 OD2 116.5
REMARK 620 3 HOH C 818 O 104.0 109.8
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 410 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 67 OD1
REMARK 620 2 THR A 76 O 83.8
REMARK 620 3 HOH A 530 O 106.9 121.2
REMARK 620 4 HOH B 591 O 136.7 109.8 100.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 406 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 91 O
REMARK 620 2 ASN A 131 OD1 83.1
REMARK 620 3 HOH A 577 O 64.9 146.9
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 407 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR A 150 O
REMARK 620 2 HOH A 592 O 130.4
REMARK 620 3 HOH A 594 O 87.1 111.3
REMARK 620 4 HOH A 595 O 103.8 104.2 121.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 408 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 247 OE2
REMARK 620 2 GLU B 247 OE2 100.4
REMARK 620 3 HOH B 556 O 103.4 121.9
REMARK 620 4 HOH B 773 O 120.4 84.2 124.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 409 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 264 O
REMARK 620 2 ASP A 264 OD2 76.7
REMARK 620 3 HOH A 715 O 75.7 84.5
REMARK 620 4 ASP C 47 OD1 151.5 101.8 132.8
REMARK 620 5 HOH C 517 O 101.2 171.4 86.9 84.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 403 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 754 O
REMARK 620 2 SER B 74 O 143.4
REMARK 620 3 THR B 76 O 87.3 116.6
REMARK 620 4 HOH B 701 O 56.4 145.0 86.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 404 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER B 91 O
REMARK 620 2 ASP B 132B O 110.1
REMARK 620 3 HOH B 783 O 103.4 100.0
REMARK 620 4 HOH B 785 O 82.6 162.5 64.5
REMARK 620 5 HOH B 832 O 90.1 85.1 162.7 107.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 407 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 151 O
REMARK 620 2 GLY B 153 O 112.8
REMARK 620 3 HOH B 800 O 105.2 87.5
REMARK 620 4 HOH B 821 O 149.2 80.6 102.9
REMARK 620 5 HOH B 854 O 91.2 155.5 81.8 80.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 405 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY B 196 O
REMARK 620 2 HOH B 604 O 132.8
REMARK 620 3 HOH B 724 O 113.7 113.3
REMARK 620 4 HOH B 805 O 73.7 79.1 119.9
REMARK 620 5 HOH B 858 O 80.6 87.2 111.3 128.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 406 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 264 O
REMARK 620 2 ASP B 264 OD2 88.8
REMARK 620 3 HOH B 642 O 79.6 94.6
REMARK 620 4 ASP D 47 OD1 144.8 118.7 116.4
REMARK 620 5 HOH D 787 O 83.0 133.1 128.6 62.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA C 405 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 111 OD1
REMARK 620 2 ASP C 111 OD2 44.6
REMARK 620 3 ASP C 115 OD1 115.3 98.2
REMARK 620 4 HOH C 530 O 145.4 126.9 98.6
REMARK 620 5 HOH C 892 O 57.8 83.0 69.1 149.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA C 406 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR C 150 O
REMARK 620 2 GLU C 151 O 69.8
REMARK 620 3 GLY C 153 O 70.2 72.6
REMARK 620 4 HOH C 587 O 122.9 93.8 157.2
REMARK 620 5 HOH C 589 O 98.4 151.8 79.3 113.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA C 407 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 151 O
REMARK 620 2 GLY C 153 O 98.8
REMARK 620 3 HOH C 761 O 47.9 143.5
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA C 410 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY C 153 O
REMARK 620 2 ASP C 154 OD1 89.6
REMARK 620 3 ASP C 154 OD2 73.6 43.0
REMARK 620 4 HOH C 763 O 82.0 54.6 92.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA C 408 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER C 177 OG
REMARK 620 2 GLU C 178 OE2 117.0
REMARK 620 3 HOH C 599 O 99.1 112.2
REMARK 620 4 HOH C 604 O 111.9 98.2 119.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA C 409 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 211 O
REMARK 620 2 GLU C 219 OE2 115.0
REMARK 620 3 HOH C 552 O 115.6 97.0
REMARK 620 4 HOH C 622 O 121.8 114.7 85.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA D 405 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH C 599 O
REMARK 620 2 ASN D 67 OD1 115.2
REMARK 620 3 THR D 76 O 87.2 83.5
REMARK 620 4 HOH D 540 O 113.2 114.2 140.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA D 410 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH C 649 O
REMARK 620 2 HOH C 817 O 46.6
REMARK 620 3 THR D 31 O 138.7 119.3
REMARK 620 4 GLU D 247 OE2 110.8 97.4 109.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA D 411 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH C 733 O
REMARK 620 2 SER D 177 OG 84.0
REMARK 620 3 GLU D 178 OE2 145.0 117.7
REMARK 620 4 HOH D 722 O 98.1 97.7 105.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA D 404 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR D 22 OG1
REMARK 620 2 HOH D 520 O 111.6
REMARK 620 3 HOH D 708 O 109.5 105.9
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA D 412 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 53 OD2
REMARK 620 2 HOH D 527 O 98.6
REMARK 620 3 HOH D 533 O 106.4 99.8
REMARK 620 4 HOH D 558 O 150.7 57.6 95.2
REMARK 620 5 HOH D 731 O 140.5 113.0 91.5 55.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA D 406 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER D 91 O
REMARK 620 2 ASP D 132B O 101.4
REMARK 620 3 HOH D 553 O 63.6 77.3
REMARK 620 4 HOH D 554 O 157.5 95.3 135.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA D 407 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR D 150 O
REMARK 620 2 HOH D 597 O 104.8
REMARK 620 3 HOH D 806 O 112.6 118.3
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA D 408 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU D 151 O
REMARK 620 2 GLY D 153 O 98.7
REMARK 620 3 HOH D 752 O 81.7 111.4
REMARK 620 4 HOH D 807 O 73.6 159.6 86.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA D 409 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL D 206 O
REMARK 620 2 PRO D 212 O 111.0
REMARK 620 3 HOH D 621 O 139.7 105.7
REMARK 620 4 HOH D 629 O 126.6 54.9 64.6
REMARK 620 5 HOH D 630 O 153.8 80.8 48.1 79.5
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA C 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA C 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA C 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA C 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA C 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA C 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA D 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA D 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA D 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA D 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA D 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA D 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA D 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA D 411
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA D 412
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1D3A RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE WILD TYPE HALOPHILIC MALATE DEHYDROGENASE
REMARK 900 IN THE APO FORM
REMARK 900 RELATED ID: 1GT2 RELATED DB: PDB
REMARK 900 R207S,R292S MUTANT OF MALATE DEHYDROGENASE FROM THE HALOPHILIC
REMARK 900 ARCHAEON HALOARCULA MARISMORTUI (HOLO FORM)
REMARK 900 RELATED ID: 1HLP RELATED DB: PDB
REMARK 900 MALATE DEHYDROGENASE (HALOPHILIC) COMPLEXED WITH NICOTINAMIDE
REMARK 900 ADENINE DINUCLEOTIDE (NAD)
REMARK 900 RELATED ID: 1O6Z RELATED DB: PDB
REMARK 900 1.95 A RESOLUTION STRUCTURE OF (R207S, R292S) MUTANT OF MALATE
REMARK 900 DEHYDROGENASE FROM THE HALOPHILIC ARCHAEON HALOARCULA MARISMORTUI
REMARK 900 (HOLO FORM)
REMARK 900 RELATED ID: 2HLP RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE E267R MUTANT OF A HALOPHILIC MALATE
REMARK 900 DEHYDROGENASE IN THE APO FORM
REMARK 900 RELATED ID: 2J5K RELATED DB: PDB
REMARK 900 2.0 A RESOLUTION STRUCTURE OF THE WILD TYPE MALATE DEHYDROGENASE
REMARK 900 FROM HALOARCULA MARISMORTUI (RADIATION DAMAGE SERIES)
REMARK 900 RELATED ID: 2J5Q RELATED DB: PDB
REMARK 900 2.15 A RESOLUTION STRUCTURE OF THE WILD TYPE MALATE DEHYDROGENASE
REMARK 900 FROM HALOARCULA MARISMORTUI AFTER FIRST RADIATION BURN ( RADIATION
REMARK 900 DAMAGE SERIES)
REMARK 900 RELATED ID: 2J5R RELATED DB: PDB
REMARK 900 2.25 A RESOLUTION STRUCTURE OF THE WILD TYPE MALATE DEHYDROGENASE
REMARK 900 FROM HALOARCULA MARISMORTUI AFTER SECOND RADIATION BURN ( RADIATION
REMARK 900 DAMAGE SERIES)
DBREF 4JCO A 21 330 UNP Q07841 MDH_HALMA 1 304
DBREF 4JCO B 21 330 UNP Q07841 MDH_HALMA 1 304
DBREF 4JCO C 21 330 UNP Q07841 MDH_HALMA 1 304
DBREF 4JCO D 21 330 UNP Q07841 MDH_HALMA 1 304
SEQRES 1 A 304 MET THR LYS VAL SER VAL VAL GLY ALA ALA GLY THR VAL
SEQRES 2 A 304 GLY ALA ALA ALA GLY TYR ASN ILE ALA LEU ARG ASP ILE
SEQRES 3 A 304 ALA ASP GLU VAL VAL PHE VAL ASP ILE PRO ASP LYS GLU
SEQRES 4 A 304 ASP ASP THR VAL GLY GLN ALA ALA ASP THR ASN HIS GLY
SEQRES 5 A 304 ILE ALA TYR ASP SER ASN THR ARG VAL ARG GLN GLY GLY
SEQRES 6 A 304 TYR GLU ASP THR ALA GLY SER ASP VAL VAL VAL ILE THR
SEQRES 7 A 304 ALA GLY ILE PRO ARG GLN PRO GLY GLN THR ARG ILE ASP
SEQRES 8 A 304 LEU ALA GLY ASP ASN ALA PRO ILE MET GLU ASP ILE GLN
SEQRES 9 A 304 SER SER LEU ASP GLU HIS ASN ASP ASP TYR ILE SER LEU
SEQRES 10 A 304 THR THR SER ASN PRO VAL ASP LEU LEU ASN ARG HIS LEU
SEQRES 11 A 304 TYR GLU ALA GLY ASP ARG SER ARG GLU GLN VAL ILE GLY
SEQRES 12 A 304 PHE GLY GLY ARG LEU ASP SER ALA ARG PHE ARG TYR VAL
SEQRES 13 A 304 LEU SER GLU GLU PHE ASP ALA PRO VAL GLN ASN VAL GLU
SEQRES 14 A 304 GLY THR ILE LEU GLY GLU HIS GLY ASP ALA GLN VAL PRO
SEQRES 15 A 304 VAL PHE SER LYS VAL ARG VAL ASP GLY THR ASP PRO GLU
SEQRES 16 A 304 PHE SER GLY ASP GLU LYS GLU GLN LEU LEU GLY ASP LEU
SEQRES 17 A 304 GLN GLU SER ALA MET ASP VAL ILE GLU ARG LYS GLY ALA
SEQRES 18 A 304 THR GLU TRP GLY PRO ALA ARG GLY VAL ALA HIS MET VAL
SEQRES 19 A 304 GLU ALA ILE LEU HIS ASP THR GLY GLU VAL LEU PRO ALA
SEQRES 20 A 304 SER VAL LYS LEU GLU GLY GLU PHE GLY HIS GLU ASP THR
SEQRES 21 A 304 ALA PHE GLY VAL PRO VAL ARG LEU GLY SER ASN GLY VAL
SEQRES 22 A 304 GLU GLU ILE VAL GLU TRP ASP LEU ASP ASP TYR GLU GLN
SEQRES 23 A 304 ASP LEU MET ALA ASP ALA ALA GLU LYS LEU SER ASP GLN
SEQRES 24 A 304 TYR ASP LYS ILE SER
SEQRES 1 B 304 MET THR LYS VAL SER VAL VAL GLY ALA ALA GLY THR VAL
SEQRES 2 B 304 GLY ALA ALA ALA GLY TYR ASN ILE ALA LEU ARG ASP ILE
SEQRES 3 B 304 ALA ASP GLU VAL VAL PHE VAL ASP ILE PRO ASP LYS GLU
SEQRES 4 B 304 ASP ASP THR VAL GLY GLN ALA ALA ASP THR ASN HIS GLY
SEQRES 5 B 304 ILE ALA TYR ASP SER ASN THR ARG VAL ARG GLN GLY GLY
SEQRES 6 B 304 TYR GLU ASP THR ALA GLY SER ASP VAL VAL VAL ILE THR
SEQRES 7 B 304 ALA GLY ILE PRO ARG GLN PRO GLY GLN THR ARG ILE ASP
SEQRES 8 B 304 LEU ALA GLY ASP ASN ALA PRO ILE MET GLU ASP ILE GLN
SEQRES 9 B 304 SER SER LEU ASP GLU HIS ASN ASP ASP TYR ILE SER LEU
SEQRES 10 B 304 THR THR SER ASN PRO VAL ASP LEU LEU ASN ARG HIS LEU
SEQRES 11 B 304 TYR GLU ALA GLY ASP ARG SER ARG GLU GLN VAL ILE GLY
SEQRES 12 B 304 PHE GLY GLY ARG LEU ASP SER ALA ARG PHE ARG TYR VAL
SEQRES 13 B 304 LEU SER GLU GLU PHE ASP ALA PRO VAL GLN ASN VAL GLU
SEQRES 14 B 304 GLY THR ILE LEU GLY GLU HIS GLY ASP ALA GLN VAL PRO
SEQRES 15 B 304 VAL PHE SER LYS VAL ARG VAL ASP GLY THR ASP PRO GLU
SEQRES 16 B 304 PHE SER GLY ASP GLU LYS GLU GLN LEU LEU GLY ASP LEU
SEQRES 17 B 304 GLN GLU SER ALA MET ASP VAL ILE GLU ARG LYS GLY ALA
SEQRES 18 B 304 THR GLU TRP GLY PRO ALA ARG GLY VAL ALA HIS MET VAL
SEQRES 19 B 304 GLU ALA ILE LEU HIS ASP THR GLY GLU VAL LEU PRO ALA
SEQRES 20 B 304 SER VAL LYS LEU GLU GLY GLU PHE GLY HIS GLU ASP THR
SEQRES 21 B 304 ALA PHE GLY VAL PRO VAL ARG LEU GLY SER ASN GLY VAL
SEQRES 22 B 304 GLU GLU ILE VAL GLU TRP ASP LEU ASP ASP TYR GLU GLN
SEQRES 23 B 304 ASP LEU MET ALA ASP ALA ALA GLU LYS LEU SER ASP GLN
SEQRES 24 B 304 TYR ASP LYS ILE SER
SEQRES 1 C 304 MET THR LYS VAL SER VAL VAL GLY ALA ALA GLY THR VAL
SEQRES 2 C 304 GLY ALA ALA ALA GLY TYR ASN ILE ALA LEU ARG ASP ILE
SEQRES 3 C 304 ALA ASP GLU VAL VAL PHE VAL ASP ILE PRO ASP LYS GLU
SEQRES 4 C 304 ASP ASP THR VAL GLY GLN ALA ALA ASP THR ASN HIS GLY
SEQRES 5 C 304 ILE ALA TYR ASP SER ASN THR ARG VAL ARG GLN GLY GLY
SEQRES 6 C 304 TYR GLU ASP THR ALA GLY SER ASP VAL VAL VAL ILE THR
SEQRES 7 C 304 ALA GLY ILE PRO ARG GLN PRO GLY GLN THR ARG ILE ASP
SEQRES 8 C 304 LEU ALA GLY ASP ASN ALA PRO ILE MET GLU ASP ILE GLN
SEQRES 9 C 304 SER SER LEU ASP GLU HIS ASN ASP ASP TYR ILE SER LEU
SEQRES 10 C 304 THR THR SER ASN PRO VAL ASP LEU LEU ASN ARG HIS LEU
SEQRES 11 C 304 TYR GLU ALA GLY ASP ARG SER ARG GLU GLN VAL ILE GLY
SEQRES 12 C 304 PHE GLY GLY ARG LEU ASP SER ALA ARG PHE ARG TYR VAL
SEQRES 13 C 304 LEU SER GLU GLU PHE ASP ALA PRO VAL GLN ASN VAL GLU
SEQRES 14 C 304 GLY THR ILE LEU GLY GLU HIS GLY ASP ALA GLN VAL PRO
SEQRES 15 C 304 VAL PHE SER LYS VAL ARG VAL ASP GLY THR ASP PRO GLU
SEQRES 16 C 304 PHE SER GLY ASP GLU LYS GLU GLN LEU LEU GLY ASP LEU
SEQRES 17 C 304 GLN GLU SER ALA MET ASP VAL ILE GLU ARG LYS GLY ALA
SEQRES 18 C 304 THR GLU TRP GLY PRO ALA ARG GLY VAL ALA HIS MET VAL
SEQRES 19 C 304 GLU ALA ILE LEU HIS ASP THR GLY GLU VAL LEU PRO ALA
SEQRES 20 C 304 SER VAL LYS LEU GLU GLY GLU PHE GLY HIS GLU ASP THR
SEQRES 21 C 304 ALA PHE GLY VAL PRO VAL ARG LEU GLY SER ASN GLY VAL
SEQRES 22 C 304 GLU GLU ILE VAL GLU TRP ASP LEU ASP ASP TYR GLU GLN
SEQRES 23 C 304 ASP LEU MET ALA ASP ALA ALA GLU LYS LEU SER ASP GLN
SEQRES 24 C 304 TYR ASP LYS ILE SER
SEQRES 1 D 304 MET THR LYS VAL SER VAL VAL GLY ALA ALA GLY THR VAL
SEQRES 2 D 304 GLY ALA ALA ALA GLY TYR ASN ILE ALA LEU ARG ASP ILE
SEQRES 3 D 304 ALA ASP GLU VAL VAL PHE VAL ASP ILE PRO ASP LYS GLU
SEQRES 4 D 304 ASP ASP THR VAL GLY GLN ALA ALA ASP THR ASN HIS GLY
SEQRES 5 D 304 ILE ALA TYR ASP SER ASN THR ARG VAL ARG GLN GLY GLY
SEQRES 6 D 304 TYR GLU ASP THR ALA GLY SER ASP VAL VAL VAL ILE THR
SEQRES 7 D 304 ALA GLY ILE PRO ARG GLN PRO GLY GLN THR ARG ILE ASP
SEQRES 8 D 304 LEU ALA GLY ASP ASN ALA PRO ILE MET GLU ASP ILE GLN
SEQRES 9 D 304 SER SER LEU ASP GLU HIS ASN ASP ASP TYR ILE SER LEU
SEQRES 10 D 304 THR THR SER ASN PRO VAL ASP LEU LEU ASN ARG HIS LEU
SEQRES 11 D 304 TYR GLU ALA GLY ASP ARG SER ARG GLU GLN VAL ILE GLY
SEQRES 12 D 304 PHE GLY GLY ARG LEU ASP SER ALA ARG PHE ARG TYR VAL
SEQRES 13 D 304 LEU SER GLU GLU PHE ASP ALA PRO VAL GLN ASN VAL GLU
SEQRES 14 D 304 GLY THR ILE LEU GLY GLU HIS GLY ASP ALA GLN VAL PRO
SEQRES 15 D 304 VAL PHE SER LYS VAL ARG VAL ASP GLY THR ASP PRO GLU
SEQRES 16 D 304 PHE SER GLY ASP GLU LYS GLU GLN LEU LEU GLY ASP LEU
SEQRES 17 D 304 GLN GLU SER ALA MET ASP VAL ILE GLU ARG LYS GLY ALA
SEQRES 18 D 304 THR GLU TRP GLY PRO ALA ARG GLY VAL ALA HIS MET VAL
SEQRES 19 D 304 GLU ALA ILE LEU HIS ASP THR GLY GLU VAL LEU PRO ALA
SEQRES 20 D 304 SER VAL LYS LEU GLU GLY GLU PHE GLY HIS GLU ASP THR
SEQRES 21 D 304 ALA PHE GLY VAL PRO VAL ARG LEU GLY SER ASN GLY VAL
SEQRES 22 D 304 GLU GLU ILE VAL GLU TRP ASP LEU ASP ASP TYR GLU GLN
SEQRES 23 D 304 ASP LEU MET ALA ASP ALA ALA GLU LYS LEU SER ASP GLN
SEQRES 24 D 304 TYR ASP LYS ILE SER
HET CL A 401 1
HET CL A 402 1
HET CL A 403 1
HET CL A 404 1
HET NA A 405 1
HET NA A 406 1
HET NA A 407 1
HET NA A 408 1
HET NA A 409 1
HET NA A 410 1
HET CL B 401 1
HET CL B 402 1
HET NA B 403 1
HET NA B 404 1
HET NA B 405 1
HET NA B 406 1
HET NA B 407 1
HET CL C 401 1
HET CL C 402 1
HET CL C 403 1
HET CL C 404 1
HET NA C 405 1
HET NA C 406 1
HET NA C 407 1
HET NA C 408 1
HET NA C 409 1
HET NA C 410 1
HET CL D 401 1
HET CL D 402 1
HET CL D 403 1
HET NA D 404 1
HET NA D 405 1
HET NA D 406 1
HET NA D 407 1
HET NA D 408 1
HET NA D 409 1
HET NA D 410 1
HET NA D 411 1
HET NA D 412 1
HETNAM CL CHLORIDE ION
HETNAM NA SODIUM ION
FORMUL 5 CL 13(CL 1-)
FORMUL 9 NA 26(NA 1+)
FORMUL 44 HOH *1468(H2 O)
HELIX 1 1 GLY A 30 ARG A 43 1 14
HELIX 2 2 ILE A 54 ASP A 54B 5 3
HELIX 3 3 LYS A 55 ALA A 71 1 17
HELIX 4 4 GLY A 84 ALA A 89 5 6
HELIX 5 5 THR A 108 GLU A 129 1 22
HELIX 6 6 PRO A 141 GLY A 153 1 13
HELIX 7 7 SER A 156 GLU A 158 5 3
HELIX 8 8 GLY A 164 ASP A 181 1 18
HELIX 9 9 PRO A 183 GLN A 185 5 3
HELIX 10 10 PHE A 203 VAL A 206 5 4
HELIX 11 11 SER A 221 GLU A 241 1 21
HELIX 12 12 GLU A 247 HIS A 263 1 17
HELIX 13 13 GLU A 278 GLY A 280 5 3
HELIX 14 14 ASP A 308 SER A 330 1 23
HELIX 15 15 GLY B 30 ARG B 43 1 14
HELIX 16 16 ILE B 54 ASP B 54B 5 3
HELIX 17 17 LYS B 55 ALA B 71 1 17
HELIX 18 18 GLY B 84 ALA B 89 5 6
HELIX 19 19 THR B 108 GLU B 129 1 22
HELIX 20 20 PRO B 141 GLY B 153 1 13
HELIX 21 21 SER B 156 GLU B 158 5 3
HELIX 22 22 GLY B 164 ASP B 181 1 18
HELIX 23 23 PRO B 183 GLN B 185 5 3
HELIX 24 24 PHE B 203 VAL B 206 5 4
HELIX 25 25 SER B 221 GLU B 241 1 21
HELIX 26 26 GLU B 247 HIS B 263 1 17
HELIX 27 27 GLU B 278 GLY B 280 5 3
HELIX 28 28 ASP B 308 SER B 330 1 23
HELIX 29 29 GLY C 30 ARG C 43 1 14
HELIX 30 30 ILE C 54 ASP C 54B 5 3
HELIX 31 31 LYS C 55 ALA C 71 1 17
HELIX 32 32 GLY C 84 ALA C 89 5 6
HELIX 33 33 THR C 108 GLU C 129 1 22
HELIX 34 34 PRO C 141 GLY C 153 1 13
HELIX 35 35 SER C 156 GLU C 158 5 3
HELIX 36 36 GLY C 164 ASP C 181 1 18
HELIX 37 37 PRO C 183 GLN C 185 5 3
HELIX 38 38 PHE C 203 VAL C 206 5 4
HELIX 39 39 SER C 221 GLU C 241 1 21
HELIX 40 40 GLU C 247 HIS C 263 1 17
HELIX 41 41 GLU C 278 GLY C 280 5 3
HELIX 42 42 ASP C 308 SER C 330 1 23
HELIX 43 43 GLY D 30 ARG D 43 1 14
HELIX 44 44 ILE D 54 ASP D 54B 5 3
HELIX 45 45 LYS D 55 ALA D 71 1 17
HELIX 46 46 GLY D 84 ALA D 89 5 6
HELIX 47 47 THR D 108 GLU D 129 1 22
HELIX 48 48 PRO D 141 GLY D 153 1 13
HELIX 49 49 SER D 156 GLU D 158 5 3
HELIX 50 50 GLY D 164 ASP D 181 1 18
HELIX 51 51 PRO D 183 GLN D 185 5 3
HELIX 52 52 PHE D 203 VAL D 206 5 4
HELIX 53 53 SER D 221 GLU D 241 1 21
HELIX 54 54 GLU D 247 HIS D 263 1 17
HELIX 55 55 GLU D 278 GLY D 280 5 3
HELIX 56 56 ASP D 308 SER D 330 1 23
SHEET 1 A 6 ARG A 77 GLN A 80 0
SHEET 2 A 6 GLU A 48 VAL A 52 1 N PHE A 51 O ARG A 79
SHEET 3 A 6 LYS A 23 VAL A 27 1 N VAL A 26 O VAL A 52
SHEET 4 A 6 VAL A 93 ILE A 96 1 O VAL A 95 N VAL A 27
SHEET 5 A 6 ILE A 134 THR A 137 1 O LEU A 136 N VAL A 94
SHEET 6 A 6 VAL A 160 GLY A 162 1 O ILE A 161 N THR A 137
SHEET 1 B 2 VAL A 187 GLU A 188 0
SHEET 2 B 2 ARG A 207 VAL A 208 -1 O ARG A 207 N GLU A 188
SHEET 1 C 2 ILE A 191 GLY A 193 0
SHEET 2 C 2 GLN A 199 PRO A 201 -1 O VAL A 200 N LEU A 192
SHEET 1 D 3 VAL A 268 GLU A 276 0
SHEET 2 D 3 GLU A 283 GLY A 294 -1 O THR A 285 N LEU A 275
SHEET 3 D 3 GLY A 297 ILE A 302 -1 O GLU A 299 N ARG A 292
SHEET 1 E 6 ARG B 77 GLN B 80 0
SHEET 2 E 6 GLU B 48 VAL B 52 1 N PHE B 51 O ARG B 79
SHEET 3 E 6 LYS B 23 VAL B 27 1 N VAL B 26 O VAL B 52
SHEET 4 E 6 VAL B 93 ILE B 96 1 O VAL B 95 N VAL B 27
SHEET 5 E 6 ILE B 134 THR B 137 1 O LEU B 136 N VAL B 94
SHEET 6 E 6 VAL B 160 GLY B 162 1 O ILE B 161 N THR B 137
SHEET 1 F 2 VAL B 187 GLU B 188 0
SHEET 2 F 2 ARG B 207 VAL B 208 -1 O ARG B 207 N GLU B 188
SHEET 1 G 2 ILE B 191 GLY B 193 0
SHEET 2 G 2 GLN B 199 PRO B 201 -1 O VAL B 200 N LEU B 192
SHEET 1 H 3 VAL B 268 GLU B 276 0
SHEET 2 H 3 GLU B 283 GLY B 294 -1 O THR B 285 N LEU B 275
SHEET 3 H 3 GLY B 297 ILE B 302 -1 O GLU B 299 N ARG B 292
SHEET 1 I 6 ARG C 77 GLN C 80 0
SHEET 2 I 6 GLU C 48 VAL C 52 1 N PHE C 51 O ARG C 79
SHEET 3 I 6 LYS C 23 VAL C 27 1 N VAL C 26 O VAL C 52
SHEET 4 I 6 VAL C 93 ILE C 96 1 O VAL C 95 N SER C 25
SHEET 5 I 6 ILE C 134 THR C 137 1 O LEU C 136 N VAL C 94
SHEET 6 I 6 VAL C 160 GLY C 162 1 O ILE C 161 N SER C 135
SHEET 1 J 2 VAL C 187 GLU C 188 0
SHEET 2 J 2 ARG C 207 VAL C 208 -1 O ARG C 207 N GLU C 188
SHEET 1 K 2 ILE C 191 GLY C 193 0
SHEET 2 K 2 GLN C 199 PRO C 201 -1 O VAL C 200 N LEU C 192
SHEET 1 L 3 VAL C 268 GLU C 276 0
SHEET 2 L 3 GLU C 283 GLY C 294 -1 O THR C 285 N LEU C 275
SHEET 3 L 3 GLY C 297 ILE C 302 -1 O GLU C 299 N ARG C 292
SHEET 1 M 6 ARG D 77 GLN D 80 0
SHEET 2 M 6 GLU D 48 VAL D 52 1 N PHE D 51 O ARG D 79
SHEET 3 M 6 LYS D 23 VAL D 27 1 N VAL D 26 O VAL D 52
SHEET 4 M 6 VAL D 93 ILE D 96 1 O VAL D 95 N VAL D 27
SHEET 5 M 6 ILE D 134 THR D 137 1 O LEU D 136 N ILE D 96
SHEET 6 M 6 VAL D 160 GLY D 162 1 O ILE D 161 N SER D 135
SHEET 1 N 2 VAL D 187 GLU D 188 0
SHEET 2 N 2 ARG D 207 VAL D 208 -1 O ARG D 207 N GLU D 188
SHEET 1 O 2 ILE D 191 GLY D 193 0
SHEET 2 O 2 GLN D 199 PRO D 201 -1 O VAL D 200 N LEU D 192
SHEET 1 P 3 VAL D 268 GLU D 276 0
SHEET 2 P 3 GLU D 283 GLY D 294 -1 O THR D 285 N LEU D 275
SHEET 3 P 3 GLY D 297 ILE D 302 -1 O GLU D 299 N ARG D 292
LINK OD2 ASP A 47 NA NA A 405 1555 1555 2.36
LINK OD1 ASN A 67 NA NA A 410 1555 1555 2.85
LINK O THR A 76 NA NA A 410 1555 1555 3.18
LINK O SER A 91 NA NA A 406 1555 1555 2.84
LINK OD1 ASN A 131 NA NA A 406 1555 1555 3.09
LINK O TYR A 150 NA NA A 407 1555 1555 2.95
LINK OE2 GLU A 247 NA NA A 408 1555 1555 2.71
LINK O ASP A 264 NA NA A 409 1555 1555 2.44
LINK OD2 ASP A 264 NA NA A 409 1555 1555 3.13
LINK NA NA A 405 OD2 ASP C 264 1555 1555 2.71
LINK NA NA A 405 O HOH C 818 1555 1555 2.91
LINK NA NA A 406 O HOH A 577 1555 1555 2.40
LINK NA NA A 407 O HOH A 592 1555 1555 2.57
LINK NA NA A 407 O HOH A 594 1555 1555 2.37
LINK NA NA A 407 O HOH A 595 1555 1555 3.17
LINK NA NA A 408 OE2 GLU B 247 1555 1555 2.67
LINK NA NA A 408 O HOH B 556 1555 1555 2.40
LINK NA NA A 408 O HOH B 773 1555 1555 2.90
LINK NA NA A 409 O HOH A 715 1555 1555 2.96
LINK NA NA A 409 OD1 ASP C 47 1555 1555 2.44
LINK NA NA A 409 O HOH C 517 1555 1555 2.49
LINK NA NA A 410 O HOH A 530 1555 1555 2.50
LINK NA NA A 410 O HOH B 591 1555 1555 2.38
LINK O HOH A 754 NA NA B 403 1555 1555 3.01
LINK O SER B 74 NA NA B 403 1555 1555 2.84
LINK O THR B 76 NA NA B 403 1555 1555 2.53
LINK O SER B 91 NA NA B 404 1555 1555 2.75
LINK O ASP B 132B NA NA B 404 1555 1555 2.53
LINK O GLU B 151 NA NA B 407 1555 1555 2.37
LINK O GLY B 153 NA NA B 407 1555 1555 2.40
LINK O GLY B 196 NA NA B 405 1555 1555 3.11
LINK O ASP B 264 NA NA B 406 1555 1555 2.41
LINK OD2 ASP B 264 NA NA B 406 1555 1555 2.75
LINK NA NA B 403 O HOH B 701 1555 1555 2.55
LINK NA NA B 404 O HOH B 783 1555 1555 2.75
LINK NA NA B 404 O HOH B 785 1555 1555 2.67
LINK NA NA B 404 O HOH B 832 1555 1555 2.35
LINK NA NA B 405 O HOH B 604 1555 1555 2.83
LINK NA NA B 405 O HOH B 724 1555 1555 2.38
LINK NA NA B 405 O HOH B 805 1555 1555 2.46
LINK NA NA B 405 O HOH B 858 1555 1555 2.88
LINK NA NA B 406 O HOH B 642 1555 1555 2.84
LINK NA NA B 406 OD1 ASP D 47 1555 1555 2.34
LINK NA NA B 406 O HOH D 787 1555 1555 2.35
LINK NA NA B 407 O HOH B 800 1555 1555 2.88
LINK NA NA B 407 O HOH B 821 1555 1555 2.82
LINK NA NA B 407 O HOH B 854 1555 1555 2.58
LINK OD1 ASP C 111 NA NA C 405 1555 1555 2.80
LINK OD2 ASP C 111 NA NA C 405 1555 1555 2.96
LINK OD1 ASP C 115 NA NA C 405 1555 1555 2.86
LINK O TYR C 150 NA NA C 406 1555 1555 2.85
LINK O GLU C 151 NA NA C 406 1555 1555 3.15
LINK O GLU C 151 NA NA C 407 1555 1555 2.35
LINK O GLY C 153 NA NA C 406 1555 1555 3.14
LINK O GLY C 153 NA NA C 407 1555 1555 2.54
LINK O GLY C 153 NA NA C 410 1555 1555 3.19
LINK OD1AASP C 154 NA NA C 410 1555 1555 2.81
LINK OD2AASP C 154 NA NA C 410 1555 1555 3.13
LINK OG SER C 177 NA NA C 408 1555 1555 2.55
LINK OE2 GLU C 178 NA NA C 408 1555 1555 2.92
LINK O ASP C 211 NA NA C 409 1555 1555 2.60
LINK OE2 GLU C 219 NA NA C 409 1555 1555 2.54
LINK NA NA C 405 O HOH C 530 1555 1555 3.02
LINK NA NA C 405 O HOH C 892 1555 1555 3.02
LINK NA NA C 406 O HOH C 587 1555 1555 2.50
LINK NA NA C 406 O HOH C 589 1555 1555 2.87
LINK NA NA C 407 O HOH C 761 1555 1555 3.11
LINK NA NA C 408 O HOH C 599 1555 1555 2.38
LINK NA NA C 408 O HOH C 604 1555 1555 2.63
LINK NA NA C 409 O HOH C 552 1555 1555 2.75
LINK NA NA C 409 O HOH C 622 1555 1555 2.47
LINK NA NA C 410 O HOH C 763 1555 1555 2.86
LINK O HOH C 599 NA NA D 405 1555 1555 2.75
LINK O HOH C 649 NA NA D 410 1555 1555 2.93
LINK O HOH C 733 NA NA D 411 1555 1555 2.71
LINK O HOH C 817 NA NA D 410 1555 1555 2.60
LINK OG1 THR D 22 NA NA D 404 1555 1555 2.39
LINK O THR D 31 NA NA D 410 1555 1555 2.78
LINK OD2 ASP D 53 NA NA D 412 1555 1555 2.59
LINK OD1 ASN D 67 NA NA D 405 1555 1555 2.78
LINK O THR D 76 NA NA D 405 1555 1555 3.15
LINK O SER D 91 NA NA D 406 1555 1555 2.70
LINK O ASP D 132B NA NA D 406 1555 1555 2.40
LINK O TYR D 150 NA NA D 407 1555 1555 2.99
LINK O GLU D 151 NA NA D 408 1555 1555 2.55
LINK O GLY D 153 NA NA D 408 1555 1555 2.44
LINK OG SER D 177 NA NA D 411 1555 1555 3.12
LINK OE2 GLU D 178 NA NA D 411 1555 1555 2.47
LINK O VAL D 206 NA NA D 409 1555 1555 2.84
LINK O PRO D 212 NA NA D 409 1555 1555 2.90
LINK OE2 GLU D 247 NA NA D 410 1555 1555 2.54
LINK NA NA D 404 O HOH D 520 1555 1555 2.48
LINK NA NA D 404 O HOH D 708 1555 1555 2.80
LINK NA NA D 405 O HOH D 540 1555 1555 2.42
LINK NA NA D 406 O HOH D 553 1555 1555 2.52
LINK NA NA D 406 O HOH D 554 1555 1555 2.44
LINK NA NA D 407 O HOH D 597 1555 1555 2.62
LINK NA NA D 407 O HOH D 806 1555 1555 2.70
LINK NA NA D 408 O HOH D 752 1555 1555 2.25
LINK NA NA D 408 O HOH D 807 1555 1555 2.69
LINK NA NA D 409 O HOH D 621 1555 1555 2.32
LINK NA NA D 409 O HOH D 629 1555 1555 3.07
LINK NA NA D 409 O HOH D 630 1555 1555 3.14
LINK NA NA D 411 O HOH D 722 1555 1555 2.67
LINK NA NA D 412 O HOH D 527 1555 1555 2.74
LINK NA NA D 412 O HOH D 533 1555 1555 3.03
LINK NA NA D 412 O HOH D 558 1555 1555 2.60
LINK NA NA D 412 O HOH D 731 1555 1555 2.44
CISPEP 1 ASN A 140 PRO A 141 0 -2.31
CISPEP 2 ASN B 140 PRO B 141 0 1.46
CISPEP 3 ASN C 140 PRO C 141 0 -2.36
CISPEP 4 ASN D 140 PRO D 141 0 1.00
SITE 1 AC1 4 LYS A 205 ASP A 306 THR D 210A ASP D 211
SITE 1 AC2 5 ARG A 166 HIS A 256 TYR B 72 ASP B 73
SITE 2 AC2 5 HOH B 537
SITE 1 AC3 7 GLY A 69 ILE A 70 ALA A 71 TYR A 72
SITE 2 AC3 7 ASP A 73 ARG B 166 ARG B 252
SITE 1 AC4 4 HIS A 68 GLY A 69 ARG B 166 GLY B 249
SITE 1 AC5 3 ASP A 47 ASP C 264 HOH C 818
SITE 1 AC6 4 SER A 91 ASN A 131 ASP A 132B HOH A 577
SITE 1 AC7 5 TYR A 150 GLU A 151 GLY A 153 HOH A 592
SITE 2 AC7 5 HOH A 594
SITE 1 AC8 4 GLU A 247 GLU B 247 HOH B 556 HOH B 773
SITE 1 AC9 4 ASP A 264 HOH A 715 ASP C 47 HOH C 517
SITE 1 BC1 5 ASN A 67 THR A 76 HOH A 530 TYR B 174
SITE 2 BC1 5 HOH B 591
SITE 1 BC2 4 LYS B 205 ASP B 306 THR C 210A ASP C 211
SITE 1 BC3 3 ARG B 171 HOH B 542 HOH B 602
SITE 1 BC4 7 VAL A 184 HOH A 754 ILE B 70 SER B 74
SITE 2 BC4 7 ASN B 75 THR B 76 HOH B 701
SITE 1 BC5 5 SER B 91 ASP B 132B HOH B 783 HOH B 785
SITE 2 BC5 5 HOH B 832
SITE 1 BC6 6 GLY B 196 GLN B 199 HOH B 604 HOH B 724
SITE 2 BC6 6 HOH B 805 HOH B 858
SITE 1 BC7 4 ASP B 264 HOH B 642 ASP D 47 HOH D 787
SITE 1 BC8 5 GLU B 151 GLY B 153 HOH B 800 HOH B 821
SITE 2 BC8 5 HOH B 854
SITE 1 BC9 7 GLY C 69 ILE C 70 ALA C 71 TYR C 72
SITE 2 BC9 7 ASP C 73 ARG D 166 ARG D 252
SITE 1 CC1 4 THR B 210A ASP B 211 LYS C 205 ASP C 306
SITE 1 CC2 6 ARG C 166 ARG C 252 HIS C 256 TYR D 72
SITE 2 CC2 6 ASP D 73 HOH D 544
SITE 1 CC3 2 ARG C 171 THR C 246
SITE 1 CC4 4 ASP C 111 ASP C 115 HOH C 530 HOH C 892
SITE 1 CC5 6 TYR C 150 GLU C 151 GLY C 153 NA C 407
SITE 2 CC5 6 HOH C 587 HOH C 589
SITE 1 CC6 6 GLU C 151 GLY C 153 NA C 406 NA C 410
SITE 2 CC6 6 HOH C 698 HOH C 751
SITE 1 CC7 4 SER C 177 GLU C 178 HOH C 599 HOH C 604
SITE 1 CC8 5 ASP C 211 PRO C 212 GLU C 219 HOH C 552
SITE 2 CC8 5 HOH C 622
SITE 1 CC9 5 GLY C 153 ASP C 154 NA C 407 HOH C 752
SITE 2 CC9 5 HOH C 763
SITE 1 DC1 5 THR A 210A ASP A 211 HOH A 548 LYS D 205
SITE 2 DC1 5 ASP D 306
SITE 1 DC2 4 ARG D 171 THR D 246 HOH D 502 HOH D 649
SITE 1 DC3 7 ARG C 166 ARG C 252 GLY D 69 ILE D 70
SITE 2 DC3 7 ALA D 71 TYR D 72 ASP D 73
SITE 1 DC4 4 THR D 22 ILE D 45 HOH D 520 HOH D 708
SITE 1 DC5 4 HOH C 599 ASN D 67 THR D 76 HOH D 540
SITE 1 DC6 4 SER D 91 ASP D 132B HOH D 553 HOH D 554
SITE 1 DC7 6 TYR D 150 GLU D 151 GLY D 153 NA D 408
SITE 2 DC7 6 HOH D 597 HOH D 806
SITE 1 DC8 5 GLU D 151 GLY D 153 NA D 407 HOH D 752
SITE 2 DC8 5 HOH D 807
SITE 1 DC9 6 SER D 204 VAL D 206 ASP D 211 PRO D 212
SITE 2 DC9 6 HOH D 621 HOH D 629
SITE 1 EC1 5 HOH C 649 HOH C 817 THR D 31 ALA D 35
SITE 2 EC1 5 GLU D 247
SITE 1 EC2 4 HOH C 733 SER D 177 GLU D 178 HOH D 722
SITE 1 EC3 7 GLY D 28 GLY D 30 ASP D 53 HOH D 527
SITE 2 EC3 7 HOH D 533 HOH D 558 HOH D 731
CRYST1 126.813 114.065 124.022 90.00 93.49 90.00 C 1 2 1 16
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 0.007886 0.000000 0.000481 0.00000
SCALE2 0.000000 0.008767 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008078 0.00000
(ATOM LINES ARE NOT SHOWN.)
END