HEADER OXIDOREDUCTASE 26-APR-17 5VM2
TITLE CRYSTAL STRUCTURE OF ECK1772, AN OXIDOREDUCTASE/DEHYDROGENASE OF
TITLE 2 UNKNOWN SPECIFICITY INVOLVED IN MEMBRANE BIOGENESIS FROM ESCHERICHIA
TITLE 3 COLI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALCOHOL DEHYDROGENASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: PUTATIVE OXIDOREDUCTASE;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: ARC77_00615, AU473_19815, BFL24_13020, ECS2483;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-MAGIC;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PMCSG53
KEYWDS NAD(H) OR NADP(H)-DEPENDENT OXIDOREDUCTASE, DEHYDROGENASE, ROSSMAN
KEYWDS 2 FOLD, STRUCTURAL GENOMICS, CSGID, CENTER FOR STRUCTURAL GENOMICS OF
KEYWDS 3 INFECTIOUS DISEASES, NIAID, NATIONAL INSTITUTE OF ALLERGY AND
KEYWDS 4 INFECTIOUS DISEASES, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.J.STOGIOS,T.SKARINA,C.MCCHESNEY,R.DI LEO,A.SAVCHENKO,W.F.ANDERSON,
AUTHOR 2 CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES (CSGID)
REVDAT 6 23-OCT-24 5VM2 1 REMARK
REVDAT 5 15-NOV-23 5VM2 1 REMARK
REVDAT 4 04-OCT-23 5VM2 1 LINK
REVDAT 3 11-DEC-19 5VM2 1 REMARK
REVDAT 2 13-SEP-17 5VM2 1 REMARK
REVDAT 1 07-JUN-17 5VM2 0
JRNL AUTH P.J.STOGIOS
JRNL TITL CRYSTAL STRUCTURE OF ECK1772, AN
JRNL TITL 2 OXIDOREDUCTASE/DEHYDROGENASE OF UNKNOWN SPECIFICITY INVOLVED
JRNL TITL 3 IN MEMBRANE BIOGENESIS FROM ESCHERICHIA COLI
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.98 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX DEV_2733
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.98
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.31
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.3
REMARK 3 NUMBER OF REFLECTIONS : 46646
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.183
REMARK 3 R VALUE (WORKING SET) : 0.181
REMARK 3 FREE R VALUE : 0.225
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.180
REMARK 3 FREE R VALUE TEST SET COUNT : 1950
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 39.3193 - 4.7765 0.99 3465 151 0.1713 0.2141
REMARK 3 2 4.7765 - 3.7922 1.00 3341 147 0.1423 0.1763
REMARK 3 3 3.7922 - 3.3132 1.00 3314 145 0.1608 0.2011
REMARK 3 4 3.3132 - 3.0104 0.99 3277 141 0.1827 0.2125
REMARK 3 5 3.0104 - 2.7946 1.00 3262 144 0.2046 0.2540
REMARK 3 6 2.7946 - 2.6299 0.99 3252 142 0.2077 0.2756
REMARK 3 7 2.6299 - 2.4982 0.99 3216 141 0.2104 0.2591
REMARK 3 8 2.4982 - 2.3895 0.98 3182 139 0.2082 0.2726
REMARK 3 9 2.3895 - 2.2975 0.98 3166 138 0.2049 0.2407
REMARK 3 10 2.2975 - 2.2182 0.97 3143 140 0.2064 0.2680
REMARK 3 11 2.2182 - 2.1489 0.96 3124 139 0.2103 0.2690
REMARK 3 12 2.1489 - 2.0875 0.94 3063 133 0.2246 0.2644
REMARK 3 13 2.0875 - 2.0325 0.93 3014 127 0.2340 0.3309
REMARK 3 14 2.0325 - 1.9829 0.89 2877 123 0.2455 0.2672
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.210
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.630
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 : 0.005 5418
REMARK 3 ANGLE : 0.927 7340
REMARK 3 CHIRALITY : 0.063 843
REMARK 3 PLANARITY : 0.006 956
REMARK 3 DIHEDRAL : 21.913 2056
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 12
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID 1:76)
REMARK 3 ORIGIN FOR THE GROUP (A): 1.5310 -2.2675 35.0954
REMARK 3 T TENSOR
REMARK 3 T11: 0.6395 T22: 0.4611
REMARK 3 T33: 0.3586 T12: 0.0001
REMARK 3 T13: -0.0704 T23: 0.0105
REMARK 3 L TENSOR
REMARK 3 L11: 6.8986 L22: 3.3472
REMARK 3 L33: 1.6035 L12: -0.5022
REMARK 3 L13: -0.8181 L23: 1.1131
REMARK 3 S TENSOR
REMARK 3 S11: 0.0645 S12: -0.0435 S13: 0.5384
REMARK 3 S21: 0.7248 S22: 0.1956 S23: -0.4312
REMARK 3 S31: -0.3662 S32: 0.3862 S33: -0.2688
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 77:189)
REMARK 3 ORIGIN FOR THE GROUP (A): -8.9090 -5.3856 22.1246
REMARK 3 T TENSOR
REMARK 3 T11: 0.2334 T22: 0.3117
REMARK 3 T33: 0.3020 T12: 0.0277
REMARK 3 T13: 0.0096 T23: 0.0065
REMARK 3 L TENSOR
REMARK 3 L11: 0.4935 L22: 2.5403
REMARK 3 L33: 2.9069 L12: -0.3701
REMARK 3 L13: 0.0179 L23: 0.9755
REMARK 3 S TENSOR
REMARK 3 S11: -0.1215 S12: -0.1476 S13: 0.0685
REMARK 3 S21: 0.4208 S22: 0.1236 S23: 0.1346
REMARK 3 S31: -0.0407 S32: -0.0706 S33: -0.0077
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN A AND RESID 190:235)
REMARK 3 ORIGIN FOR THE GROUP (A): 2.2808 -22.7611 4.4283
REMARK 3 T TENSOR
REMARK 3 T11: 0.2899 T22: 0.2279
REMARK 3 T33: 0.3815 T12: 0.0258
REMARK 3 T13: -0.0415 T23: -0.0282
REMARK 3 L TENSOR
REMARK 3 L11: 7.6732 L22: 3.9735
REMARK 3 L33: 3.6303 L12: -2.2299
REMARK 3 L13: -3.0057 L23: 0.1440
REMARK 3 S TENSOR
REMARK 3 S11: 0.0823 S12: 0.1356 S13: -0.4105
REMARK 3 S21: -0.1869 S22: -0.2181 S23: -0.2651
REMARK 3 S31: 0.3510 S32: 0.2617 S33: 0.1539
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN A AND RESID 236:274)
REMARK 3 ORIGIN FOR THE GROUP (A): 3.1605 -8.9534 1.7506
REMARK 3 T TENSOR
REMARK 3 T11: 0.1738 T22: 0.3654
REMARK 3 T33: 0.3627 T12: -0.0144
REMARK 3 T13: -0.0020 T23: 0.0189
REMARK 3 L TENSOR
REMARK 3 L11: 8.1601 L22: 7.1510
REMARK 3 L33: 5.9935 L12: -1.0250
REMARK 3 L13: -0.9870 L23: -1.7727
REMARK 3 S TENSOR
REMARK 3 S11: -0.0248 S12: -0.3020 S13: 0.1571
REMARK 3 S21: -0.0141 S22: -0.0176 S23: -0.6927
REMARK 3 S31: -0.3712 S32: 1.1607 S33: -0.1051
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN A AND RESID 275:321)
REMARK 3 ORIGIN FOR THE GROUP (A): -4.1546 -10.5947 13.5065
REMARK 3 T TENSOR
REMARK 3 T11: 0.2562 T22: 0.2800
REMARK 3 T33: 0.3233 T12: 0.0325
REMARK 3 T13: -0.0276 T23: -0.0209
REMARK 3 L TENSOR
REMARK 3 L11: 0.6105 L22: 1.8849
REMARK 3 L33: 4.7143 L12: 0.4235
REMARK 3 L13: -0.9069 L23: -1.5776
REMARK 3 S TENSOR
REMARK 3 S11: 0.0622 S12: -0.0487 S13: -0.0579
REMARK 3 S21: 0.0987 S22: 0.0184 S23: -0.0021
REMARK 3 S31: 0.1194 S32: 0.2255 S33: -0.0590
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (CHAIN A AND RESID 322:347)
REMARK 3 ORIGIN FOR THE GROUP (A): 8.2279 -16.1757 30.5421
REMARK 3 T TENSOR
REMARK 3 T11: 0.4789 T22: 0.4375
REMARK 3 T33: 0.4703 T12: 0.1079
REMARK 3 T13: -0.1776 T23: -0.0809
REMARK 3 L TENSOR
REMARK 3 L11: 7.1080 L22: 8.0462
REMARK 3 L33: 6.7349 L12: 2.8667
REMARK 3 L13: 5.6924 L23: 1.4626
REMARK 3 S TENSOR
REMARK 3 S11: 0.0302 S12: 0.0828 S13: -0.1489
REMARK 3 S21: 1.1351 S22: 0.5118 S23: -1.1786
REMARK 3 S31: 0.7295 S32: 1.0652 S33: -0.4334
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (CHAIN B AND RESID 1:88)
REMARK 3 ORIGIN FOR THE GROUP (A): -31.9893 -26.3905 -22.8345
REMARK 3 T TENSOR
REMARK 3 T11: 0.5991 T22: 0.2286
REMARK 3 T33: 0.2929 T12: 0.0665
REMARK 3 T13: -0.0670 T23: 0.0062
REMARK 3 L TENSOR
REMARK 3 L11: 6.4765 L22: 3.7038
REMARK 3 L33: 4.1498 L12: 0.2409
REMARK 3 L13: -0.9466 L23: 0.5226
REMARK 3 S TENSOR
REMARK 3 S11: -0.1011 S12: 0.4624 S13: 0.3969
REMARK 3 S21: -0.9264 S22: -0.0929 S23: 0.1401
REMARK 3 S31: -0.2256 S32: -0.3042 S33: 0.1176
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: (CHAIN B AND RESID 89:122)
REMARK 3 ORIGIN FOR THE GROUP (A): -27.1087 -11.0992 -19.6038
REMARK 3 T TENSOR
REMARK 3 T11: 0.3776 T22: 0.2376
REMARK 3 T33: 0.2367 T12: 0.0519
REMARK 3 T13: -0.0167 T23: 0.0235
REMARK 3 L TENSOR
REMARK 3 L11: 8.1722 L22: 7.6504
REMARK 3 L33: 6.5628 L12: 4.8043
REMARK 3 L13: -0.0083 L23: 0.7246
REMARK 3 S TENSOR
REMARK 3 S11: -0.2880 S12: 0.2209 S13: 0.2835
REMARK 3 S21: -1.0112 S22: 0.1055 S23: 0.3954
REMARK 3 S31: -0.1950 S32: -0.1035 S33: 0.1927
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: (CHAIN B AND RESID 123:194)
REMARK 3 ORIGIN FOR THE GROUP (A): -25.1234 -21.6463 -5.0877
REMARK 3 T TENSOR
REMARK 3 T11: 0.2736 T22: 0.2321
REMARK 3 T33: 0.2822 T12: 0.0177
REMARK 3 T13: 0.0210 T23: 0.0322
REMARK 3 L TENSOR
REMARK 3 L11: 0.6477 L22: 2.4223
REMARK 3 L33: 3.0099 L12: -0.1292
REMARK 3 L13: -0.7142 L23: 1.2101
REMARK 3 S TENSOR
REMARK 3 S11: -0.0466 S12: 0.0496 S13: -0.0096
REMARK 3 S21: -0.1262 S22: 0.0345 S23: -0.2287
REMARK 3 S31: 0.0991 S32: 0.1631 S33: 0.0052
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: (CHAIN B AND RESID 195:236)
REMARK 3 ORIGIN FOR THE GROUP (A): -36.9642 -18.9466 13.4679
REMARK 3 T TENSOR
REMARK 3 T11: 0.2607 T22: 0.1562
REMARK 3 T33: 0.1576 T12: -0.0185
REMARK 3 T13: 0.0226 T23: 0.0337
REMARK 3 L TENSOR
REMARK 3 L11: 7.4520 L22: 5.9157
REMARK 3 L33: 4.1158 L12: -0.9756
REMARK 3 L13: -1.9864 L23: 1.7519
REMARK 3 S TENSOR
REMARK 3 S11: 0.0911 S12: -0.2909 S13: -0.1050
REMARK 3 S21: 0.4511 S22: -0.1310 S23: 0.0784
REMARK 3 S31: 0.0076 S32: 0.0372 S33: 0.0698
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: (CHAIN B AND RESID 237:288)
REMARK 3 ORIGIN FOR THE GROUP (A): -36.5986 -4.7367 5.1537
REMARK 3 T TENSOR
REMARK 3 T11: 0.1901 T22: 0.2190
REMARK 3 T33: 0.3035 T12: -0.0030
REMARK 3 T13: -0.0205 T23: -0.0086
REMARK 3 L TENSOR
REMARK 3 L11: 7.7233 L22: 6.8548
REMARK 3 L33: 5.2186 L12: 0.1594
REMARK 3 L13: -1.5354 L23: -0.7523
REMARK 3 S TENSOR
REMARK 3 S11: 0.1926 S12: 0.1912 S13: -0.1658
REMARK 3 S21: -0.1999 S22: -0.1644 S23: 0.8497
REMARK 3 S31: -0.0267 S32: -0.6742 S33: -0.0154
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: (CHAIN B AND RESID 289:347)
REMARK 3 ORIGIN FOR THE GROUP (A): -33.3399 -28.4102 -7.7552
REMARK 3 T TENSOR
REMARK 3 T11: 0.2278 T22: 0.2232
REMARK 3 T33: 0.2114 T12: 0.0268
REMARK 3 T13: 0.0311 T23: -0.0336
REMARK 3 L TENSOR
REMARK 3 L11: 3.3822 L22: 5.3933
REMARK 3 L33: 3.0109 L12: 1.5892
REMARK 3 L13: 0.8229 L23: 0.5063
REMARK 3 S TENSOR
REMARK 3 S11: 0.1194 S12: -0.0076 S13: -0.2695
REMARK 3 S21: -0.1376 S22: -0.1772 S23: 0.1902
REMARK 3 S31: 0.2598 S32: -0.3110 S33: 0.0277
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 5VM2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-MAY-17.
REMARK 100 THE DEPOSITION ID IS D_1000227612.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-APR-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97860
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 X 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 47841
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.980
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 (%) : 99.7
REMARK 200 DATA REDUNDANCY : 6.300
REMARK 200 R MERGE (I) : 0.10600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.98
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.01
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.4
REMARK 200 DATA REDUNDANCY IN SHELL : 4.70
REMARK 200 R MERGE FOR SHELL (I) : 0.58200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: 1E3J
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.22
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.25
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M SODIUM CHLORIDE, 0.1 M SODIUM
REMARK 280 CITRATE PH 5.6, 1 MM MAGNESIUM CHLORIDE, 25% (W/V) PEG3350,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 2 21 21
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,Y+1/2,-Z+1/2
REMARK 290 4555 -X,-Y+1/2,Z+1/2
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 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.44400
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 74.73000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 35.44400
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 74.73000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3240 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28530 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3380 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28340 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 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 CL CL B 403 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 711 LIES ON A SPECIAL POSITION.
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 NZ LYS B 335 O HOH B 501 1.40
REMARK 500 O HOH B 575 O HOH B 809 2.08
REMARK 500 OE2 GLU B 203 O HOH B 502 2.14
REMARK 500 O HOH B 748 O HOH B 845 2.15
REMARK 500 O HOH A 632 O HOH A 662 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 OH TYR B 35 OE1 GLN B 211 2545 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO A 119 C - N - CA ANGL. DEV. = -11.0 DEGREES
REMARK 500 ILE B 52 N - CA - C ANGL. DEV. = -18.0 DEGREES
REMARK 500 PRO B 53 C - N - CA ANGL. DEV. = 9.9 DEGREES
REMARK 500 PRO B 54 C - N - CA ANGL. DEV. = -12.2 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 THR A 269 -129.82 64.96
REMARK 500 VAL A 270 78.19 62.22
REMARK 500 ARG A 292 -116.61 53.08
REMARK 500 ASP A 323 31.23 -92.06
REMARK 500 ASN A 334 47.91 -104.48
REMARK 500 GLN B 9 -75.10 -73.92
REMARK 500 SER B 48 23.61 -143.57
REMARK 500 ILE B 52 67.45 63.51
REMARK 500 LYS B 55 16.96 -69.89
REMARK 500 ASP B 56 103.95 -161.08
REMARK 500 GLN B 118 -53.76 -23.18
REMARK 500 ARG B 292 -116.27 52.63
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 794 DISTANCE = 6.09 ANGSTROMS
REMARK 525 HOH A 795 DISTANCE = 6.44 ANGSTROMS
REMARK 525 HOH B 857 DISTANCE = 6.71 ANGSTROMS
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 MG A 401 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 66 OE1
REMARK 620 2 GLU A 152 OE1 98.8
REMARK 620 3 HOH A 705 O 108.6 107.4
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 402 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 95 SG
REMARK 620 2 CYS A 98 SG 109.0
REMARK 620 3 CYS A 101 SG 118.6 106.2
REMARK 620 4 CYS A 109 SG 103.9 114.5 105.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 401 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 66 OE1
REMARK 620 2 GLU B 152 OE1 97.7
REMARK 620 3 HOH B 650 O 103.4 108.4
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 402 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 95 SG
REMARK 620 2 CYS B 98 SG 111.3
REMARK 620 3 CYS B 101 SG 116.0 105.8
REMARK 620 4 CYS B 109 SG 102.2 113.3 108.5
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 403
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: CSGID-IDP95672 RELATED DB: TARGETTRACK
REMARK 900 RELATED ID: IDP95672 RELATED DB: TARGETTRACK
DBREF 5VM2 A 1 347 UNP C3T6X7 C3T6X7_ECOLX 1 347
DBREF 5VM2 B 1 347 UNP C3T6X7 C3T6X7_ECOLX 1 347
SEQRES 1 A 347 MET LYS ASN SER LYS ALA ILE LEU GLN VAL PRO GLY THR
SEQRES 2 A 347 MET LYS ILE ILE SER ALA GLU ILE PRO VAL PRO LYS GLU
SEQRES 3 A 347 ASP GLU VAL LEU ILE LYS VAL GLU TYR VAL GLY ILE CSO
SEQRES 4 A 347 GLY SER ASP VAL HIS GLY PHE GLU SER GLY PRO PHE ILE
SEQRES 5 A 347 PRO PRO LYS ASP PRO ASN GLN GLU ILE GLY LEU GLY HIS
SEQRES 6 A 347 GLU CYS ALA GLY THR VAL VAL ALA VAL GLY SER ARG VAL
SEQRES 7 A 347 ARG LYS PHE LYS PRO GLY ASP ARG VAL ASN ILE GLU PRO
SEQRES 8 A 347 GLY VAL PRO CYS GLY HIS CYS ARG TYR CYS LEU GLU GLY
SEQRES 9 A 347 LYS TYR ASN ILE CYS PRO ASP VAL ASP PHE MET ALA THR
SEQRES 10 A 347 GLN PRO ASN TYR ARG GLY ALA LEU THR HIS TYR LEU CYS
SEQRES 11 A 347 HIS PRO GLU SER PHE THR TYR LYS LEU PRO ASP ASN MET
SEQRES 12 A 347 ASP THR MET GLU GLY THR LEU VAL GLU PRO ALA ALA VAL
SEQRES 13 A 347 GLY MET HIS ALA ALA MET LEU ALA ASP VAL LYS PRO GLY
SEQRES 14 A 347 LYS LYS ILE ILE ILE LEU GLY ALA GLY CYS ILE GLY LEU
SEQRES 15 A 347 MET THR LEU GLN ALA CYS LYS CYS LEU GLY ALA THR GLU
SEQRES 16 A 347 ILE ALA VAL VAL ASP VAL LEU GLU LYS ARG LEU ALA MET
SEQRES 17 A 347 ALA GLU GLN LEU GLY ALA THR VAL VAL ILE ASN GLY ALA
SEQRES 18 A 347 LYS GLU ASP THR ILE ALA ARG CYS GLN GLN PHE THR GLU
SEQRES 19 A 347 ASP MET GLY ALA ASP ILE VAL PHE GLU THR ALA GLY SER
SEQRES 20 A 347 ALA VAL THR VAL LYS GLN ALA PRO TYR LEU VAL MET ARG
SEQRES 21 A 347 GLY GLY LYS ILE MET ILE VAL GLY THR VAL PRO GLY ALA
SEQRES 22 A 347 SER ALA ILE ASN PHE LEU LYS ILE ASN ARG GLU VAL THR
SEQRES 23 A 347 ILE GLN THR VAL PHE ARG TYR ALA ASN ARG TYR PRO VAL
SEQRES 24 A 347 THR ILE GLU ALA ILE SER SER GLY ARG PHE ASP VAL LYS
SEQRES 25 A 347 SER MET VAL THR HIS ILE TYR ASP TYR ARG ASP VAL GLN
SEQRES 26 A 347 GLN ALA PHE GLU GLU SER VAL ASN ASN LYS ARG ASP ILE
SEQRES 27 A 347 ILE LYS GLY VAL ILE LYS ILE SER ASP
SEQRES 1 B 347 MET LYS ASN SER LYS ALA ILE LEU GLN VAL PRO GLY THR
SEQRES 2 B 347 MET LYS ILE ILE SER ALA GLU ILE PRO VAL PRO LYS GLU
SEQRES 3 B 347 ASP GLU VAL LEU ILE LYS VAL GLU TYR VAL GLY ILE CSO
SEQRES 4 B 347 GLY SER ASP VAL HIS GLY PHE GLU SER GLY PRO PHE ILE
SEQRES 5 B 347 PRO PRO LYS ASP PRO ASN GLN GLU ILE GLY LEU GLY HIS
SEQRES 6 B 347 GLU CYS ALA GLY THR VAL VAL ALA VAL GLY SER ARG VAL
SEQRES 7 B 347 ARG LYS PHE LYS PRO GLY ASP ARG VAL ASN ILE GLU PRO
SEQRES 8 B 347 GLY VAL PRO CYS GLY HIS CYS ARG TYR CYS LEU GLU GLY
SEQRES 9 B 347 LYS TYR ASN ILE CYS PRO ASP VAL ASP PHE MET ALA THR
SEQRES 10 B 347 GLN PRO ASN TYR ARG GLY ALA LEU THR HIS TYR LEU CYS
SEQRES 11 B 347 HIS PRO GLU SER PHE THR TYR LYS LEU PRO ASP ASN MET
SEQRES 12 B 347 ASP THR MET GLU GLY THR LEU VAL GLU PRO ALA ALA VAL
SEQRES 13 B 347 GLY MET HIS ALA ALA MET LEU ALA ASP VAL LYS PRO GLY
SEQRES 14 B 347 LYS LYS ILE ILE ILE LEU GLY ALA GLY CYS ILE GLY LEU
SEQRES 15 B 347 MET THR LEU GLN ALA CYS LYS CYS LEU GLY ALA THR GLU
SEQRES 16 B 347 ILE ALA VAL VAL ASP VAL LEU GLU LYS ARG LEU ALA MET
SEQRES 17 B 347 ALA GLU GLN LEU GLY ALA THR VAL VAL ILE ASN GLY ALA
SEQRES 18 B 347 LYS GLU ASP THR ILE ALA ARG CYS GLN GLN PHE THR GLU
SEQRES 19 B 347 ASP MET GLY ALA ASP ILE VAL PHE GLU THR ALA GLY SER
SEQRES 20 B 347 ALA VAL THR VAL LYS GLN ALA PRO TYR LEU VAL MET ARG
SEQRES 21 B 347 GLY GLY LYS ILE MET ILE VAL GLY THR VAL PRO GLY ALA
SEQRES 22 B 347 SER ALA ILE ASN PHE LEU LYS ILE ASN ARG GLU VAL THR
SEQRES 23 B 347 ILE GLN THR VAL PHE ARG TYR ALA ASN ARG TYR PRO VAL
SEQRES 24 B 347 THR ILE GLU ALA ILE SER SER GLY ARG PHE ASP VAL LYS
SEQRES 25 B 347 SER MET VAL THR HIS ILE TYR ASP TYR ARG ASP VAL GLN
SEQRES 26 B 347 GLN ALA PHE GLU GLU SER VAL ASN ASN LYS ARG ASP ILE
SEQRES 27 B 347 ILE LYS GLY VAL ILE LYS ILE SER ASP
MODRES 5VM2 CSO A 39 CYS MODIFIED RESIDUE
MODRES 5VM2 CSO B 39 CYS MODIFIED RESIDUE
HET CSO A 39 7
HET CSO B 39 14
HET MG A 401 1
HET ZN A 402 1
HET MG B 401 1
HET ZN B 402 1
HET CL B 403 1
HETNAM CSO S-HYDROXYCYSTEINE
HETNAM MG MAGNESIUM ION
HETNAM ZN ZINC ION
HETNAM CL CHLORIDE ION
FORMUL 1 CSO 2(C3 H7 N O3 S)
FORMUL 3 MG 2(MG 2+)
FORMUL 4 ZN 2(ZN 2+)
FORMUL 7 CL CL 1-
FORMUL 8 HOH *652(H2 O)
HELIX 1 AA1 CSO A 39 GLY A 49 1 11
HELIX 2 AA2 CYS A 98 GLU A 103 1 6
HELIX 3 AA3 LYS A 105 CYS A 109 5 5
HELIX 4 AA4 ASP A 144 ALA A 164 1 21
HELIX 5 AA5 GLY A 178 LEU A 191 1 14
HELIX 6 AA6 LEU A 202 LEU A 212 1 11
HELIX 7 AA7 ASP A 224 THR A 233 1 10
HELIX 8 AA8 SER A 247 ALA A 254 1 8
HELIX 9 AA9 ASN A 277 ASN A 282 5 6
HELIX 10 AB1 ARG A 296 SER A 306 1 11
HELIX 11 AB2 VAL A 311 SER A 313 5 3
HELIX 12 AB3 ASP A 323 ASN A 334 1 12
HELIX 13 AB4 LYS A 335 ILE A 338 5 4
HELIX 14 AB5 CSO B 39 GLY B 49 1 11
HELIX 15 AB6 CYS B 98 GLU B 103 1 6
HELIX 16 AB7 LYS B 105 CYS B 109 5 5
HELIX 17 AB8 ASP B 144 ALA B 164 1 21
HELIX 18 AB9 GLY B 178 LEU B 191 1 14
HELIX 19 AC1 LEU B 202 LEU B 212 1 11
HELIX 20 AC2 ASP B 224 THR B 233 1 10
HELIX 21 AC3 SER B 247 ALA B 254 1 8
HELIX 22 AC4 PHE B 278 ASN B 282 5 5
HELIX 23 AC5 ARG B 296 SER B 306 1 11
HELIX 24 AC6 ASP B 323 ASN B 334 1 12
HELIX 25 AC7 LYS B 335 ILE B 338 5 4
SHEET 1 AA1 2 ASN A 3 VAL A 10 0
SHEET 2 AA1 2 THR A 13 ALA A 19 -1 O LYS A 15 N ILE A 7
SHEET 1 AA2 5 TYR A 128 PRO A 132 0
SHEET 2 AA2 5 GLU A 28 ILE A 38 -1 N VAL A 29 O HIS A 131
SHEET 3 AA2 5 CYS A 67 VAL A 74 -1 O VAL A 72 N LEU A 30
SHEET 4 AA2 5 ARG A 86 ILE A 89 -1 O VAL A 87 N GLY A 69
SHEET 5 AA2 5 THR A 136 LYS A 138 -1 O TYR A 137 N ASN A 88
SHEET 1 AA3 4 TYR A 128 PRO A 132 0
SHEET 2 AA3 4 GLU A 28 ILE A 38 -1 N VAL A 29 O HIS A 131
SHEET 3 AA3 4 LYS A 340 LYS A 344 -1 O ILE A 343 N VAL A 36
SHEET 4 AA3 4 VAL A 315 ASP A 320 1 N TYR A 319 O LYS A 344
SHEET 1 AA4 2 GLY A 92 VAL A 93 0
SHEET 2 AA4 2 ASP A 113 PHE A 114 -1 O ASP A 113 N VAL A 93
SHEET 1 AA5 6 VAL A 216 ASN A 219 0
SHEET 2 AA5 6 GLU A 195 ASP A 200 1 N VAL A 198 O ILE A 218
SHEET 3 AA5 6 LYS A 171 LEU A 175 1 N ILE A 174 O ALA A 197
SHEET 4 AA5 6 ALA A 238 GLU A 243 1 O PHE A 242 N LEU A 175
SHEET 5 AA5 6 VAL A 258 VAL A 267 1 O MET A 265 N GLU A 243
SHEET 6 AA5 6 THR A 286 VAL A 290 1 O THR A 286 N ILE A 264
SHEET 1 AA6 2 ASN B 3 VAL B 10 0
SHEET 2 AA6 2 THR B 13 ALA B 19 -1 O LYS B 15 N ILE B 7
SHEET 1 AA7 5 TYR B 128 PRO B 132 0
SHEET 2 AA7 5 GLU B 28 ILE B 38 -1 N ILE B 31 O LEU B 129
SHEET 3 AA7 5 GLU B 66 VAL B 74 -1 O ALA B 73 N LEU B 30
SHEET 4 AA7 5 ARG B 86 ILE B 89 -1 O VAL B 87 N GLY B 69
SHEET 5 AA7 5 THR B 136 LYS B 138 -1 O TYR B 137 N ASN B 88
SHEET 1 AA8 4 TYR B 128 PRO B 132 0
SHEET 2 AA8 4 GLU B 28 ILE B 38 -1 N ILE B 31 O LEU B 129
SHEET 3 AA8 4 LYS B 340 LYS B 344 -1 O ILE B 343 N VAL B 36
SHEET 4 AA8 4 VAL B 315 ASP B 320 1 N TYR B 319 O LYS B 344
SHEET 1 AA9 2 GLY B 92 VAL B 93 0
SHEET 2 AA9 2 ASP B 113 PHE B 114 -1 O ASP B 113 N VAL B 93
SHEET 1 AB1 6 VAL B 216 ASN B 219 0
SHEET 2 AB1 6 ILE B 196 ASP B 200 1 N VAL B 198 O ILE B 218
SHEET 3 AB1 6 ILE B 172 LEU B 175 1 N ILE B 172 O ALA B 197
SHEET 4 AB1 6 ALA B 238 GLU B 243 1 O PHE B 242 N LEU B 175
SHEET 5 AB1 6 VAL B 258 VAL B 267 1 O MET B 265 N GLU B 243
SHEET 6 AB1 6 THR B 286 VAL B 290 1 O THR B 286 N ILE B 264
LINK C ILE A 38 N CSO A 39 1555 1555 1.34
LINK C CSO A 39 N GLY A 40 1555 1555 1.33
LINK C ILE B 38 N ACSO B 39 1555 1555 1.33
LINK C ILE B 38 N BCSO B 39 1555 1555 1.33
LINK C ACSO B 39 N GLY B 40 1555 1555 1.33
LINK C BCSO B 39 N GLY B 40 1555 1555 1.34
LINK OE1 GLU A 66 MG MG A 401 1555 1555 2.26
LINK SG CYS A 95 ZN ZN A 402 1555 1555 2.37
LINK SG CYS A 98 ZN ZN A 402 1555 1555 2.34
LINK SG CYS A 101 ZN ZN A 402 1555 1555 2.42
LINK SG CYS A 109 ZN ZN A 402 1555 1555 2.30
LINK OE1 GLU A 152 MG MG A 401 1555 1555 2.03
LINK MG MG A 401 O HOH A 705 1555 1555 1.91
LINK OE1 GLU B 66 MG MG B 401 1555 1555 2.29
LINK SG CYS B 95 ZN ZN B 402 1555 1555 2.37
LINK SG CYS B 98 ZN ZN B 402 1555 1555 2.38
LINK SG CYS B 101 ZN ZN B 402 1555 1555 2.38
LINK SG CYS B 109 ZN ZN B 402 1555 1555 2.31
LINK OE1 GLU B 152 MG MG B 401 1555 1555 2.12
LINK MG MG B 401 O HOH B 650 1555 1555 1.94
SITE 1 AC1 4 HIS A 65 GLU A 66 GLU A 152 HOH A 705
SITE 1 AC2 4 CYS A 95 CYS A 98 CYS A 101 CYS A 109
SITE 1 AC3 5 CSO B 39 HIS B 65 GLU B 66 GLU B 152
SITE 2 AC3 5 HOH B 650
SITE 1 AC4 4 CYS B 95 CYS B 98 CYS B 101 CYS B 109
SITE 1 AC5 3 LYS B 312 SER B 313 VAL B 315
CRYST1 63.994 70.888 149.460 90.00 90.00 90.00 P 2 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 0.015626 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014107 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006691 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
