| content |
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 18-MAY-15 4ZV9
TITLE 2.00 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF AN UNCHARACTERIZED
TITLE 2 PROTEIN FROM ESCHERICHIA COLI O157:H7 STR. SAKAI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UNCHARACTERIZED PROTEIN;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI O157:H7;
SOURCE 3 ORGANISM_TAXID: 83334;
SOURCE 4 STRAIN: SAKAI;
SOURCE 5 GENE: ECS3884;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)/PMAGIC;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMCSG73
KEYWDS MCSG, HUMAN MICROBIOME, STRUCTURAL GENOMICS, PSI-BIOLOGY, PROTEIN
KEYWDS 2 STRUCTURE INITIATIVE, MIDWEST CENTER FOR STRUCTURAL GENOMICS,
KEYWDS 3 UNKNOWN FUNCTION
EXPDTA X-RAY DIFFRACTION
AUTHOR A.S.HALAVATY,Z.WAWRZAK,E.V.FILIPPOVA,O.KIRYUKHINA,M.ENDRES,
AUTHOR 2 A.JOACHIMIAK,W.F.ANDERSON,MIDWEST CENTER FOR STRUCTURAL GENOMICS
AUTHOR 3 (MCSG)
REVDAT 1 17-JUN-15 4ZV9 0
JRNL AUTH A.S.HALAVATY,Z.WAWRZAK,E.V.FILIPPOVA,O.KIRYUKHINA,M.ENDRES,
JRNL AUTH 2 A.JOACHIMIAK,W.F.ANDERSON,
JRNL AUTH 3 MIDWEST CENTER FOR STRUCTURAL GENOMICS (MCSG)
JRNL TITL 2.00 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF AN
JRNL TITL 2 UNCHARACTERIZED PROTEIN FROM ESCHERICHIA COLI O157:H7 STR.
JRNL TITL 3 SAKAI
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0029
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.79
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.0
REMARK 3 NUMBER OF REFLECTIONS : 101473
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.169
REMARK 3 R VALUE (WORKING SET) : 0.168
REMARK 3 FREE R VALUE : 0.199
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 5263
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5024
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 62.06
REMARK 3 BIN R VALUE (WORKING SET) : 0.2070
REMARK 3 BIN FREE R VALUE SET COUNT : 270
REMARK 3 BIN FREE R VALUE : 0.2370
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 11136
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 82
REMARK 3 SOLVENT ATOMS : 1312
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.03000
REMARK 3 B22 (A**2) : 0.58000
REMARK 3 B33 (A**2) : -0.57000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.29000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.177
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.148
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.099
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.683
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.960
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 11795 ; 0.008 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 10881 ; 0.005 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 16062 ; 1.362 ; 1.965
REMARK 3 BOND ANGLES OTHERS (DEGREES): 25050 ; 1.123 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1475 ; 3.459 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 567 ;31.966 ;24.039
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1665 ;11.978 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 67 ;13.661 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1651 ; 0.082 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 13780 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 2815 ; 0.005 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 15
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 57 294 B 57 294 14249 0.07 0.05
REMARK 3 2 A 57 294 C 57 294 14227 0.07 0.05
REMARK 3 3 A 57 294 D 57 294 14138 0.07 0.05
REMARK 3 4 A 57 294 E 57 294 14081 0.07 0.05
REMARK 3 5 A 57 294 F 57 294 14255 0.07 0.05
REMARK 3 6 B 57 294 C 57 294 13958 0.08 0.05
REMARK 3 7 B 57 294 D 57 294 14165 0.07 0.05
REMARK 3 8 B 57 294 E 57 294 13967 0.08 0.05
REMARK 3 9 B 57 294 F 57 294 14276 0.06 0.05
REMARK 3 10 C 57 294 D 57 294 13766 0.09 0.05
REMARK 3 11 C 57 294 E 57 294 13797 0.09 0.05
REMARK 3 12 C 57 294 F 57 294 14032 0.08 0.05
REMARK 3 13 D 57 294 E 57 294 14123 0.08 0.05
REMARK 3 14 D 57 294 F 57 294 14177 0.08 0.05
REMARK 3 15 E 57 294 F 57 294 14084 0.08 0.05
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 12
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 57 A 94
REMARK 3 ORIGIN FOR THE GROUP (A): 63.9883 57.4593 85.7259
REMARK 3 T TENSOR
REMARK 3 T11: 0.0615 T22: 0.1287
REMARK 3 T33: 0.1207 T12: -0.0256
REMARK 3 T13: 0.0080 T23: -0.0167
REMARK 3 L TENSOR
REMARK 3 L11: 3.3660 L22: 2.3821
REMARK 3 L33: 2.3202 L12: -0.6882
REMARK 3 L13: 0.1818 L23: -1.0987
REMARK 3 S TENSOR
REMARK 3 S11: 0.2260 S12: -0.0072 S13: 0.2235
REMARK 3 S21: -0.2424 S22: -0.2063 S23: -0.1262
REMARK 3 S31: -0.0233 S32: 0.1884 S33: -0.0197
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 95 A 294
REMARK 3 ORIGIN FOR THE GROUP (A): 71.4544 58.2393 99.9434
REMARK 3 T TENSOR
REMARK 3 T11: 0.0371 T22: 0.2521
REMARK 3 T33: 0.0716 T12: -0.0412
REMARK 3 T13: -0.0035 T23: -0.0521
REMARK 3 L TENSOR
REMARK 3 L11: 2.9470 L22: 0.4235
REMARK 3 L33: 1.2976 L12: -0.2241
REMARK 3 L13: -0.1438 L23: -0.2191
REMARK 3 S TENSOR
REMARK 3 S11: 0.0625 S12: -0.5685 S13: 0.1674
REMARK 3 S21: 0.1123 S22: -0.0145 S23: -0.0339
REMARK 3 S31: -0.0655 S32: 0.2843 S33: -0.0480
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 57 B 94
REMARK 3 ORIGIN FOR THE GROUP (A): 18.7221 8.5808 87.6796
REMARK 3 T TENSOR
REMARK 3 T11: 0.0718 T22: 0.0933
REMARK 3 T33: 0.0998 T12: 0.0009
REMARK 3 T13: -0.0211 T23: -0.0031
REMARK 3 L TENSOR
REMARK 3 L11: 1.2250 L22: 1.1986
REMARK 3 L33: 2.0268 L12: 0.4480
REMARK 3 L13: 0.3064 L23: 0.8873
REMARK 3 S TENSOR
REMARK 3 S11: 0.1327 S12: -0.2597 S13: -0.1393
REMARK 3 S21: 0.2138 S22: -0.1003 S23: -0.0094
REMARK 3 S31: 0.3394 S32: 0.0607 S33: -0.0324
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 95 B 294
REMARK 3 ORIGIN FOR THE GROUP (A): 9.7384 12.1070 74.7709
REMARK 3 T TENSOR
REMARK 3 T11: 0.0170 T22: 0.0290
REMARK 3 T33: 0.0746 T12: -0.0023
REMARK 3 T13: -0.0189 T23: -0.0283
REMARK 3 L TENSOR
REMARK 3 L11: 1.5006 L22: 0.1857
REMARK 3 L33: 1.2336 L12: -0.0630
REMARK 3 L13: 0.2270 L23: 0.0609
REMARK 3 S TENSOR
REMARK 3 S11: 0.0393 S12: -0.0546 S13: -0.0476
REMARK 3 S21: 0.0123 S22: -0.0442 S23: -0.0023
REMARK 3 S31: 0.1203 S32: -0.0810 S33: 0.0049
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 57 C 157
REMARK 3 ORIGIN FOR THE GROUP (A): 71.5236 19.2725 126.2282
REMARK 3 T TENSOR
REMARK 3 T11: 0.3387 T22: 0.1708
REMARK 3 T33: 0.6139 T12: 0.1871
REMARK 3 T13: -0.1110 T23: 0.0271
REMARK 3 L TENSOR
REMARK 3 L11: 2.7527 L22: 5.4563
REMARK 3 L33: 2.3584 L12: 1.7792
REMARK 3 L13: -0.0773 L23: -0.8693
REMARK 3 S TENSOR
REMARK 3 S11: 0.0915 S12: 0.2344 S13: -0.5276
REMARK 3 S21: 0.0209 S22: -0.2559 S23: -1.5871
REMARK 3 S31: 0.3938 S32: 0.4625 S33: 0.1644
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 158 C 294
REMARK 3 ORIGIN FOR THE GROUP (A): 80.3984 27.9845 136.5857
REMARK 3 T TENSOR
REMARK 3 T11: 0.5394 T22: 0.3390
REMARK 3 T33: 0.9630 T12: 0.0048
REMARK 3 T13: -0.5032 T23: 0.2211
REMARK 3 L TENSOR
REMARK 3 L11: 3.7398 L22: 5.0708
REMARK 3 L33: 2.5751 L12: 1.3194
REMARK 3 L13: -0.5197 L23: -0.6013
REMARK 3 S TENSOR
REMARK 3 S11: 0.4012 S12: -0.1789 S13: -0.4011
REMARK 3 S21: 1.0936 S22: -0.6548 S23: -2.0608
REMARK 3 S31: -0.0697 S32: 0.6882 S33: 0.2536
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 57 D 95
REMARK 3 ORIGIN FOR THE GROUP (A): 56.4452 5.8638 130.5288
REMARK 3 T TENSOR
REMARK 3 T11: 0.5762 T22: 0.1575
REMARK 3 T33: 0.1879 T12: 0.0921
REMARK 3 T13: -0.2106 T23: 0.0709
REMARK 3 L TENSOR
REMARK 3 L11: 2.8058 L22: 4.8847
REMARK 3 L33: 2.9266 L12: 0.4054
REMARK 3 L13: -1.0722 L23: 2.0357
REMARK 3 S TENSOR
REMARK 3 S11: 0.4117 S12: -0.3086 S13: -0.2946
REMARK 3 S21: 0.6181 S22: -0.3187 S23: -0.4027
REMARK 3 S31: 0.3810 S32: 0.1251 S33: -0.0930
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 96 D 294
REMARK 3 ORIGIN FOR THE GROUP (A): 44.2173 8.4020 119.6988
REMARK 3 T TENSOR
REMARK 3 T11: 0.4405 T22: 0.1027
REMARK 3 T33: 0.0695 T12: 0.1105
REMARK 3 T13: -0.0970 T23: 0.0284
REMARK 3 L TENSOR
REMARK 3 L11: 2.0061 L22: 2.2010
REMARK 3 L33: 0.7679 L12: 0.2992
REMARK 3 L13: 0.3049 L23: -0.3363
REMARK 3 S TENSOR
REMARK 3 S11: 0.2694 S12: 0.0275 S13: -0.1788
REMARK 3 S21: 0.2850 S22: -0.0543 S23: -0.0413
REMARK 3 S31: 0.2803 S32: -0.0737 S33: -0.2152
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 57 E 95
REMARK 3 ORIGIN FOR THE GROUP (A): 38.8242 13.1074 76.2319
REMARK 3 T TENSOR
REMARK 3 T11: 0.0196 T22: 0.1078
REMARK 3 T33: 0.0481 T12: -0.0084
REMARK 3 T13: -0.0133 T23: -0.0163
REMARK 3 L TENSOR
REMARK 3 L11: 3.8032 L22: 3.4653
REMARK 3 L33: 2.7519 L12: -1.7390
REMARK 3 L13: 0.9453 L23: -1.4978
REMARK 3 S TENSOR
REMARK 3 S11: 0.0974 S12: 0.2757 S13: 0.0725
REMARK 3 S21: -0.1690 S22: -0.0749 S23: 0.0262
REMARK 3 S31: 0.1779 S32: -0.0285 S33: -0.0225
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 96 E 294
REMARK 3 ORIGIN FOR THE GROUP (A): 46.7562 18.1632 89.7741
REMARK 3 T TENSOR
REMARK 3 T11: 0.0301 T22: 0.0668
REMARK 3 T33: 0.0513 T12: 0.0119
REMARK 3 T13: -0.0312 T23: -0.0073
REMARK 3 L TENSOR
REMARK 3 L11: 1.4785 L22: 0.6403
REMARK 3 L33: 1.2132 L12: -0.0511
REMARK 3 L13: -0.0767 L23: 0.2239
REMARK 3 S TENSOR
REMARK 3 S11: -0.0228 S12: 0.0374 S13: 0.0133
REMARK 3 S21: 0.1094 S22: 0.1143 S23: -0.0904
REMARK 3 S31: 0.0091 S32: 0.1995 S33: -0.0915
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 57 F 95
REMARK 3 ORIGIN FOR THE GROUP (A): 43.4893 50.1863 95.5994
REMARK 3 T TENSOR
REMARK 3 T11: 0.0506 T22: 0.1585
REMARK 3 T33: 0.0656 T12: -0.0117
REMARK 3 T13: 0.0129 T23: 0.0183
REMARK 3 L TENSOR
REMARK 3 L11: 1.4246 L22: 2.4246
REMARK 3 L33: 2.2361 L12: 0.0996
REMARK 3 L13: -0.4266 L23: 2.1039
REMARK 3 S TENSOR
REMARK 3 S11: 0.0618 S12: -0.4108 S13: 0.0518
REMARK 3 S21: 0.1623 S22: -0.0741 S23: 0.1176
REMARK 3 S31: 0.0836 S32: 0.0181 S33: 0.0122
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 96 F 294
REMARK 3 ORIGIN FOR THE GROUP (A): 34.6087 56.6529 83.6926
REMARK 3 T TENSOR
REMARK 3 T11: 0.0178 T22: 0.0324
REMARK 3 T33: 0.0460 T12: 0.0075
REMARK 3 T13: 0.0263 T23: 0.0003
REMARK 3 L TENSOR
REMARK 3 L11: 1.6520 L22: 0.4374
REMARK 3 L33: 0.8126 L12: -0.0109
REMARK 3 L13: -0.0794 L23: -0.0674
REMARK 3 S TENSOR
REMARK 3 S11: 0.0678 S12: -0.1320 S13: 0.1302
REMARK 3 S21: -0.0065 S22: -0.0196 S23: 0.0164
REMARK 3 S31: -0.0524 S32: -0.1017 S33: -0.0482
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4ZV9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-MAY-15.
REMARK 100 THE DEPOSITION ID IS D_1000209978.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-AUG-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.3
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-G
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97856
REMARK 200 MONOCHROMATOR : DIAMOND
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 115793
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 39.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : 0.05200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 21.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : 0.55000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.35
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.75
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALLIZATION: THE JCSG+ SUITE
REMARK 280 (D12): 0.04 M POTASIUM PHOSPHATE, 16% (W/V) PEG 8000, 20% (V/V)
REMARK 280 GLYCEROL PROTEIN: 8.7 MG/ML IN 10 MM TRIS-HCL PH 8.3, 0.25 M
REMARK 280 NACL, 5 MM BME FREEZING: CRYSTALLIZATION CONDITION, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 48.17050
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350
REMARK 350 BIOMOLECULE: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E
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: 6
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F
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 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 E 416 O HOH E 543 2.06
REMARK 500 O HOH A 500 O HOH A 547 2.14
REMARK 500 O HOH B 466 O HOH E 630 2.15
REMARK 500 O HOH B 557 O HOH B 695 2.17
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 B 690 O HOH F 408 2646 2.09
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 GLU A 106 -147.33 -85.94
REMARK 500 ARG A 108 31.05 -141.49
REMARK 500 CME A 186 -119.09 60.37
REMARK 500 TYR A 209 61.97 31.46
REMARK 500 GLU B 106 -148.29 -87.76
REMARK 500 CME B 186 -113.08 51.97
REMARK 500 TYR B 209 60.12 32.86
REMARK 500 GLU C 106 -147.99 -87.15
REMARK 500 ARG C 108 31.32 -141.29
REMARK 500 CME C 186 -118.64 59.81
REMARK 500 TYR C 209 62.18 31.22
REMARK 500 ASN D 58 78.33 -152.26
REMARK 500 GLU D 106 -147.38 -87.06
REMARK 500 ARG D 108 31.28 -141.89
REMARK 500 CME D 186 -116.17 57.35
REMARK 500 TYR D 209 62.12 31.69
REMARK 500 GLU E 106 -147.26 -88.08
REMARK 500 ARG E 108 31.31 -140.38
REMARK 500 CME E 186 -115.01 58.07
REMARK 500 CME E 186 -114.88 58.15
REMARK 500 TYR E 209 61.91 32.12
REMARK 500 GLU F 106 -147.48 -85.59
REMARK 500 CME F 186 -117.51 57.26
REMARK 500 TYR F 209 60.38 33.32
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 B 729 DISTANCE = 5.81 ANGSTROMS
REMARK 525 HOH B 730 DISTANCE = 5.97 ANGSTROMS
REMARK 525 HOH B 731 DISTANCE = 6.39 ANGSTROMS
REMARK 525 HOH B 732 DISTANCE = 7.41 ANGSTROMS
REMARK 525 HOH B 733 DISTANCE = 7.66 ANGSTROMS
REMARK 525 HOH F 708 DISTANCE = 6.01 ANGSTROMS
REMARK 525 HOH F 709 DISTANCE = 6.08 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL E 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL E 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE E 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL F 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL F 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL F 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG F 304
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: MCSG-APC113081 RELATED DB: TARGETTRACK
DBREF 4ZV9 A 60 294 UNP Q7AAT4 Q7AAT4_ECO57 60 294
DBREF 4ZV9 B 60 294 UNP Q7AAT4 Q7AAT4_ECO57 60 294
DBREF 4ZV9 C 60 294 UNP Q7AAT4 Q7AAT4_ECO57 60 294
DBREF 4ZV9 D 60 294 UNP Q7AAT4 Q7AAT4_ECO57 60 294
DBREF 4ZV9 E 60 294 UNP Q7AAT4 Q7AAT4_ECO57 60 294
DBREF 4ZV9 F 60 294 UNP Q7AAT4 Q7AAT4_ECO57 60 294
SEQADV 4ZV9 SER A -2 UNP Q7AAT4 EXPRESSION TAG
SEQADV 4ZV9 ASN A -1 UNP Q7AAT4 EXPRESSION TAG
SEQADV 4ZV9 ALA A 0 UNP Q7AAT4 EXPRESSION TAG
SEQADV 4ZV9 SER B 57 UNP Q7AAT4 EXPRESSION TAG
SEQADV 4ZV9 ASN B 58 UNP Q7AAT4 EXPRESSION TAG
SEQADV 4ZV9 ALA B 59 UNP Q7AAT4 EXPRESSION TAG
SEQADV 4ZV9 SER C 57 UNP Q7AAT4 EXPRESSION TAG
SEQADV 4ZV9 ASN C 58 UNP Q7AAT4 EXPRESSION TAG
SEQADV 4ZV9 ALA C 59 UNP Q7AAT4 EXPRESSION TAG
SEQADV 4ZV9 SER D 57 UNP Q7AAT4 EXPRESSION TAG
SEQADV 4ZV9 ASN D 58 UNP Q7AAT4 EXPRESSION TAG
SEQADV 4ZV9 ALA D 59 UNP Q7AAT4 EXPRESSION TAG
SEQADV 4ZV9 SER E 57 UNP Q7AAT4 EXPRESSION TAG
SEQADV 4ZV9 ASN E 58 UNP Q7AAT4 EXPRESSION TAG
SEQADV 4ZV9 ALA E 59 UNP Q7AAT4 EXPRESSION TAG
SEQADV 4ZV9 SER F 57 UNP Q7AAT4 EXPRESSION TAG
SEQADV 4ZV9 ASN F 58 UNP Q7AAT4 EXPRESSION TAG
SEQADV 4ZV9 ALA F 59 UNP Q7AAT4 EXPRESSION TAG
SEQRES 1 A 238 SER ASN ALA GLN VAL GLU PHE THR ASP PRO GLU ILE PHE
SEQRES 2 A 238 ALA GLU TYR ILE THR TYR PRO SER PRO ASN GLY HIS GLY
SEQRES 3 A 238 GLU VAL ARG GLY TYR LEU VAL LYS PRO ALA LYS MSE SER
SEQRES 4 A 238 GLY LYS THR PRO ALA VAL VAL VAL VAL HIS GLU ASN ARG
SEQRES 5 A 238 GLY LEU ASN PRO TYR ILE GLU ASP VAL ALA ARG ARG VAL
SEQRES 6 A 238 ALA LYS ALA GLY TYR ILE ALA LEU ALA PRO ASP GLY LEU
SEQRES 7 A 238 ASN SER VAL GLY GLY TYR PRO GLY ASN ASP ASP LYS GLY
SEQRES 8 A 238 ARG GLU LEU GLN GLN GLN VAL ASP PRO THR LYS LEU MSE
SEQRES 9 A 238 ASN ASP PHE PHE ALA ALA ILE GLU PHE MSE GLN ARG TYR
SEQRES 10 A 238 PRO GLN ALA THR GLY LYS VAL GLY ILE THR GLY PHE CME
SEQRES 11 A 238 TYR GLY GLY GLY VAL SER ASN ALA ALA ALA VAL ALA TYR
SEQRES 12 A 238 PRO GLU LEU ALA CYS ALA VAL PRO PHE TYR GLY ARG GLN
SEQRES 13 A 238 ALA PRO THR ALA ASP VAL ALA LYS ILE GLU ALA PRO LEU
SEQRES 14 A 238 LEU LEU HIS PHE ALA GLU LEU ASP THR ARG ILE ASN GLU
SEQRES 15 A 238 GLY TRP PRO ALA TYR GLU ALA ALA LEU LYS ALA ASN ASN
SEQRES 16 A 238 LYS VAL TYR GLU ALA TYR ILE TYR PRO GLY VAL ASN HIS
SEQRES 17 A 238 GLY PHE HIS ASN ASP SER THR PRO ARG TYR ASP LYS SER
SEQRES 18 A 238 ALA ALA ASP LEU ALA TRP GLN ARG THR LEU LYS TRP PHE
SEQRES 19 A 238 ASP LYS TYR LEU
SEQRES 1 B 238 SER ASN ALA GLN VAL GLU PHE THR ASP PRO GLU ILE PHE
SEQRES 2 B 238 ALA GLU TYR ILE THR TYR PRO SER PRO ASN GLY HIS GLY
SEQRES 3 B 238 GLU VAL ARG GLY TYR LEU VAL LYS PRO ALA LYS MSE SER
SEQRES 4 B 238 GLY LYS THR PRO ALA VAL VAL VAL VAL HIS GLU ASN ARG
SEQRES 5 B 238 GLY LEU ASN PRO TYR ILE GLU ASP VAL ALA ARG ARG VAL
SEQRES 6 B 238 ALA LYS ALA GLY TYR ILE ALA LEU ALA PRO ASP GLY LEU
SEQRES 7 B 238 ASN SER VAL GLY GLY TYR PRO GLY ASN ASP ASP LYS GLY
SEQRES 8 B 238 ARG GLU LEU GLN GLN GLN VAL ASP PRO THR LYS LEU MSE
SEQRES 9 B 238 ASN ASP PHE PHE ALA ALA ILE GLU PHE MSE GLN ARG TYR
SEQRES 10 B 238 PRO GLN ALA THR GLY LYS VAL GLY ILE THR GLY PHE CME
SEQRES 11 B 238 TYR GLY GLY GLY VAL SER ASN ALA ALA ALA VAL ALA TYR
SEQRES 12 B 238 PRO GLU LEU ALA CYS ALA VAL PRO PHE TYR GLY ARG GLN
SEQRES 13 B 238 ALA PRO THR ALA ASP VAL ALA LYS ILE GLU ALA PRO LEU
SEQRES 14 B 238 LEU LEU HIS PHE ALA GLU LEU ASP THR ARG ILE ASN GLU
SEQRES 15 B 238 GLY TRP PRO ALA TYR GLU ALA ALA LEU LYS ALA ASN ASN
SEQRES 16 B 238 LYS VAL TYR GLU ALA TYR ILE TYR PRO GLY VAL ASN HIS
SEQRES 17 B 238 GLY PHE HIS ASN ASP SER THR PRO ARG TYR ASP LYS SER
SEQRES 18 B 238 ALA ALA ASP LEU ALA TRP GLN ARG THR LEU LYS TRP PHE
SEQRES 19 B 238 ASP LYS TYR LEU
SEQRES 1 C 238 SER ASN ALA GLN VAL GLU PHE THR ASP PRO GLU ILE PHE
SEQRES 2 C 238 ALA GLU TYR ILE THR TYR PRO SER PRO ASN GLY HIS GLY
SEQRES 3 C 238 GLU VAL ARG GLY TYR LEU VAL LYS PRO ALA LYS MSE SER
SEQRES 4 C 238 GLY LYS THR PRO ALA VAL VAL VAL VAL HIS GLU ASN ARG
SEQRES 5 C 238 GLY LEU ASN PRO TYR ILE GLU ASP VAL ALA ARG ARG VAL
SEQRES 6 C 238 ALA LYS ALA GLY TYR ILE ALA LEU ALA PRO ASP GLY LEU
SEQRES 7 C 238 ASN SER VAL GLY GLY TYR PRO GLY ASN ASP ASP LYS GLY
SEQRES 8 C 238 ARG GLU LEU GLN GLN GLN VAL ASP PRO THR LYS LEU MSE
SEQRES 9 C 238 ASN ASP PHE PHE ALA ALA ILE GLU PHE MSE GLN ARG TYR
SEQRES 10 C 238 PRO GLN ALA THR GLY LYS VAL GLY ILE THR GLY PHE CME
SEQRES 11 C 238 TYR GLY GLY GLY VAL SER ASN ALA ALA ALA VAL ALA TYR
SEQRES 12 C 238 PRO GLU LEU ALA CYS ALA VAL PRO PHE TYR GLY ARG GLN
SEQRES 13 C 238 ALA PRO THR ALA ASP VAL ALA LYS ILE GLU ALA PRO LEU
SEQRES 14 C 238 LEU LEU HIS PHE ALA GLU LEU ASP THR ARG ILE ASN GLU
SEQRES 15 C 238 GLY TRP PRO ALA TYR GLU ALA ALA LEU LYS ALA ASN ASN
SEQRES 16 C 238 LYS VAL TYR GLU ALA TYR ILE TYR PRO GLY VAL ASN HIS
SEQRES 17 C 238 GLY PHE HIS ASN ASP SER THR PRO ARG TYR ASP LYS SER
SEQRES 18 C 238 ALA ALA ASP LEU ALA TRP GLN ARG THR LEU LYS TRP PHE
SEQRES 19 C 238 ASP LYS TYR LEU
SEQRES 1 D 238 SER ASN ALA GLN VAL GLU PHE THR ASP PRO GLU ILE PHE
SEQRES 2 D 238 ALA GLU TYR ILE THR TYR PRO SER PRO ASN GLY HIS GLY
SEQRES 3 D 238 GLU VAL ARG GLY TYR LEU VAL LYS PRO ALA LYS MSE SER
SEQRES 4 D 238 GLY LYS THR PRO ALA VAL VAL VAL VAL HIS GLU ASN ARG
SEQRES 5 D 238 GLY LEU ASN PRO TYR ILE GLU ASP VAL ALA ARG ARG VAL
SEQRES 6 D 238 ALA LYS ALA GLY TYR ILE ALA LEU ALA PRO ASP GLY LEU
SEQRES 7 D 238 ASN SER VAL GLY GLY TYR PRO GLY ASN ASP ASP LYS GLY
SEQRES 8 D 238 ARG GLU LEU GLN GLN GLN VAL ASP PRO THR LYS LEU MSE
SEQRES 9 D 238 ASN ASP PHE PHE ALA ALA ILE GLU PHE MSE GLN ARG TYR
SEQRES 10 D 238 PRO GLN ALA THR GLY LYS VAL GLY ILE THR GLY PHE CME
SEQRES 11 D 238 TYR GLY GLY GLY VAL SER ASN ALA ALA ALA VAL ALA TYR
SEQRES 12 D 238 PRO GLU LEU ALA CYS ALA VAL PRO PHE TYR GLY ARG GLN
SEQRES 13 D 238 ALA PRO THR ALA ASP VAL ALA LYS ILE GLU ALA PRO LEU
SEQRES 14 D 238 LEU LEU HIS PHE ALA GLU LEU ASP THR ARG ILE ASN GLU
SEQRES 15 D 238 GLY TRP PRO ALA TYR GLU ALA ALA LEU LYS ALA ASN ASN
SEQRES 16 D 238 LYS VAL TYR GLU ALA TYR ILE TYR PRO GLY VAL ASN HIS
SEQRES 17 D 238 GLY PHE HIS ASN ASP SER THR PRO ARG TYR ASP LYS SER
SEQRES 18 D 238 ALA ALA ASP LEU ALA TRP GLN ARG THR LEU LYS TRP PHE
SEQRES 19 D 238 ASP LYS TYR LEU
SEQRES 1 E 238 SER ASN ALA GLN VAL GLU PHE THR ASP PRO GLU ILE PHE
SEQRES 2 E 238 ALA GLU TYR ILE THR TYR PRO SER PRO ASN GLY HIS GLY
SEQRES 3 E 238 GLU VAL ARG GLY TYR LEU VAL LYS PRO ALA LYS MSE SER
SEQRES 4 E 238 GLY LYS THR PRO ALA VAL VAL VAL VAL HIS GLU ASN ARG
SEQRES 5 E 238 GLY LEU ASN PRO TYR ILE GLU ASP VAL ALA ARG ARG VAL
SEQRES 6 E 238 ALA LYS ALA GLY TYR ILE ALA LEU ALA PRO ASP GLY LEU
SEQRES 7 E 238 ASN SER VAL GLY GLY TYR PRO GLY ASN ASP ASP LYS GLY
SEQRES 8 E 238 ARG GLU LEU GLN GLN GLN VAL ASP PRO THR LYS LEU MSE
SEQRES 9 E 238 ASN ASP PHE PHE ALA ALA ILE GLU PHE MSE GLN ARG TYR
SEQRES 10 E 238 PRO GLN ALA THR GLY LYS VAL GLY ILE THR GLY PHE CME
SEQRES 11 E 238 TYR GLY GLY GLY VAL SER ASN ALA ALA ALA VAL ALA TYR
SEQRES 12 E 238 PRO GLU LEU ALA CYS ALA VAL PRO PHE TYR GLY ARG GLN
SEQRES 13 E 238 ALA PRO THR ALA ASP VAL ALA LYS ILE GLU ALA PRO LEU
SEQRES 14 E 238 LEU LEU HIS PHE ALA GLU LEU ASP THR ARG ILE ASN GLU
SEQRES 15 E 238 GLY TRP PRO ALA TYR GLU ALA ALA LEU LYS ALA ASN ASN
SEQRES 16 E 238 LYS VAL TYR GLU ALA TYR ILE TYR PRO GLY VAL ASN HIS
SEQRES 17 E 238 GLY PHE HIS ASN ASP SER THR PRO ARG TYR ASP LYS SER
SEQRES 18 E 238 ALA ALA ASP LEU ALA TRP GLN ARG THR LEU LYS TRP PHE
SEQRES 19 E 238 ASP LYS TYR LEU
SEQRES 1 F 238 SER ASN ALA GLN VAL GLU PHE THR ASP PRO GLU ILE PHE
SEQRES 2 F 238 ALA GLU TYR ILE THR TYR PRO SER PRO ASN GLY HIS GLY
SEQRES 3 F 238 GLU VAL ARG GLY TYR LEU VAL LYS PRO ALA LYS MSE SER
SEQRES 4 F 238 GLY LYS THR PRO ALA VAL VAL VAL VAL HIS GLU ASN ARG
SEQRES 5 F 238 GLY LEU ASN PRO TYR ILE GLU ASP VAL ALA ARG ARG VAL
SEQRES 6 F 238 ALA LYS ALA GLY TYR ILE ALA LEU ALA PRO ASP GLY LEU
SEQRES 7 F 238 ASN SER VAL GLY GLY TYR PRO GLY ASN ASP ASP LYS GLY
SEQRES 8 F 238 ARG GLU LEU GLN GLN GLN VAL ASP PRO THR LYS LEU MSE
SEQRES 9 F 238 ASN ASP PHE PHE ALA ALA ILE GLU PHE MSE GLN ARG TYR
SEQRES 10 F 238 PRO GLN ALA THR GLY LYS VAL GLY ILE THR GLY PHE CME
SEQRES 11 F 238 TYR GLY GLY GLY VAL SER ASN ALA ALA ALA VAL ALA TYR
SEQRES 12 F 238 PRO GLU LEU ALA CYS ALA VAL PRO PHE TYR GLY ARG GLN
SEQRES 13 F 238 ALA PRO THR ALA ASP VAL ALA LYS ILE GLU ALA PRO LEU
SEQRES 14 F 238 LEU LEU HIS PHE ALA GLU LEU ASP THR ARG ILE ASN GLU
SEQRES 15 F 238 GLY TRP PRO ALA TYR GLU ALA ALA LEU LYS ALA ASN ASN
SEQRES 16 F 238 LYS VAL TYR GLU ALA TYR ILE TYR PRO GLY VAL ASN HIS
SEQRES 17 F 238 GLY PHE HIS ASN ASP SER THR PRO ARG TYR ASP LYS SER
SEQRES 18 F 238 ALA ALA ASP LEU ALA TRP GLN ARG THR LEU LYS TRP PHE
SEQRES 19 F 238 ASP LYS TYR LEU
MODRES 4ZV9 MSE A 94 MET MODIFIED RESIDUE
MODRES 4ZV9 MSE A 160 MET MODIFIED RESIDUE
MODRES 4ZV9 MSE A 170 MET MODIFIED RESIDUE
MODRES 4ZV9 CME A 186 CYS MODIFIED RESIDUE
MODRES 4ZV9 MSE B 94 MET MODIFIED RESIDUE
MODRES 4ZV9 MSE B 160 MET MODIFIED RESIDUE
MODRES 4ZV9 MSE B 170 MET MODIFIED RESIDUE
MODRES 4ZV9 CME B 186 CYS MODIFIED RESIDUE
MODRES 4ZV9 MSE C 94 MET MODIFIED RESIDUE
MODRES 4ZV9 MSE C 160 MET MODIFIED RESIDUE
MODRES 4ZV9 MSE C 170 MET MODIFIED RESIDUE
MODRES 4ZV9 CME C 186 CYS MODIFIED RESIDUE
MODRES 4ZV9 MSE D 94 MET MODIFIED RESIDUE
MODRES 4ZV9 MSE D 160 MET MODIFIED RESIDUE
MODRES 4ZV9 MSE D 170 MET MODIFIED RESIDUE
MODRES 4ZV9 CME D 186 CYS MODIFIED RESIDUE
MODRES 4ZV9 MSE E 94 MET MODIFIED RESIDUE
MODRES 4ZV9 MSE E 160 MET MODIFIED RESIDUE
MODRES 4ZV9 MSE E 170 MET MODIFIED RESIDUE
MODRES 4ZV9 CME E 186 CYS MODIFIED RESIDUE
MODRES 4ZV9 MSE F 94 MET MODIFIED RESIDUE
MODRES 4ZV9 MSE F 160 MET MODIFIED RESIDUE
MODRES 4ZV9 MSE F 170 MET MODIFIED RESIDUE
MODRES 4ZV9 CME F 186 CYS MODIFIED RESIDUE
HET MSE A 94 8
HET MSE A 160 16
HET MSE A 170 16
HET CME A 186 10
HET MSE B 94 8
HET MSE B 160 16
HET MSE B 170 8
HET CME B 186 10
HET MSE C 94 8
HET MSE C 160 8
HET MSE C 170 8
HET CME C 186 10
HET MSE D 94 8
HET MSE D 160 16
HET MSE D 170 16
HET CME D 186 10
HET MSE E 94 16
HET MSE E 160 16
HET MSE E 170 8
HET CME E 186 20
HET MSE F 94 8
HET MSE F 160 16
HET MSE F 170 8
HET CME F 186 10
HET GOL A 301 6
HET GOL A 302 6
HET GOL A 303 6
HET PO4 B 301 5
HET GOL B 302 6
HET GOL D 301 6
HET GOL E 301 6
HET GOL E 302 6
HET PGE E 303 10
HET GOL F 301 6
HET GOL F 302 6
HET GOL F 303 6
HET PEG F 304 7
HETNAM MSE SELENOMETHIONINE
HETNAM CME S,S-(2-HYDROXYETHYL)THIOCYSTEINE
HETNAM GOL GLYCEROL
HETNAM PO4 PHOSPHATE ION
HETNAM PGE TRIETHYLENE GLYCOL
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 1 MSE 18(C5 H11 N O2 SE)
FORMUL 1 CME 6(C5 H11 N O3 S2)
FORMUL 7 GOL 10(C3 H8 O3)
FORMUL 10 PO4 O4 P 3-
FORMUL 15 PGE C6 H14 O4
FORMUL 19 PEG C4 H10 O3
FORMUL 20 HOH *1312(H2 O)
HELIX 1 AA1 ASN A 111 ALA A 124 1 14
HELIX 2 AA2 LEU A 134 GLY A 138 5 5
HELIX 3 AA3 ASN A 143 VAL A 154 1 12
HELIX 4 AA4 ASP A 155 TYR A 173 1 19
HELIX 5 AA5 CME A 186 TYR A 199 1 14
HELIX 6 AA6 PRO A 214 ILE A 221 5 8
HELIX 7 AA7 ASP A 233 GLU A 238 1 6
HELIX 8 AA8 GLY A 239 ASN A 250 1 12
HELIX 9 AA9 ASP A 275 LEU A 294 1 20
HELIX 10 AB1 ASN B 111 ALA B 124 1 14
HELIX 11 AB2 LEU B 134 GLY B 138 5 5
HELIX 12 AB3 ASN B 143 VAL B 154 1 12
HELIX 13 AB4 ASP B 155 TYR B 173 1 19
HELIX 14 AB5 CME B 186 TYR B 199 1 14
HELIX 15 AB6 PRO B 214 ILE B 221 5 8
HELIX 16 AB7 ASP B 233 GLU B 238 1 6
HELIX 17 AB8 GLY B 239 ASN B 250 1 12
HELIX 18 AB9 ASP B 275 LEU B 294 1 20
HELIX 19 AC1 ASN C 111 ALA C 124 1 14
HELIX 20 AC2 LEU C 134 GLY C 138 5 5
HELIX 21 AC3 ASN C 143 VAL C 154 1 12
HELIX 22 AC4 ASP C 155 TYR C 173 1 19
HELIX 23 AC5 CME C 186 TYR C 199 1 14
HELIX 24 AC6 PRO C 214 ILE C 221 5 8
HELIX 25 AC7 ASP C 233 GLU C 238 1 6
HELIX 26 AC8 GLY C 239 ASN C 250 1 12
HELIX 27 AC9 ASP C 275 LEU C 294 1 20
HELIX 28 AD1 ASN D 111 ALA D 124 1 14
HELIX 29 AD2 LEU D 134 GLY D 138 5 5
HELIX 30 AD3 ASN D 143 VAL D 154 1 12
HELIX 31 AD4 ASP D 155 TYR D 173 1 19
HELIX 32 AD5 CME D 186 TYR D 199 1 14
HELIX 33 AD6 PRO D 214 ILE D 221 5 8
HELIX 34 AD7 ASP D 233 GLU D 238 1 6
HELIX 35 AD8 GLY D 239 ASN D 250 1 12
HELIX 36 AD9 ASP D 275 LEU D 294 1 20
HELIX 37 AE1 ASN E 111 ALA E 124 1 14
HELIX 38 AE2 LEU E 134 GLY E 138 5 5
HELIX 39 AE3 ASN E 143 VAL E 154 1 12
HELIX 40 AE4 ASP E 155 TYR E 173 1 19
HELIX 41 AE5 CME E 186 TYR E 199 1 14
HELIX 42 AE6 PRO E 214 ILE E 221 5 8
HELIX 43 AE7 ASP E 233 GLU E 238 1 6
HELIX 44 AE8 GLY E 239 ASN E 250 1 12
HELIX 45 AE9 ASP E 275 LEU E 294 1 20
HELIX 46 AF1 ASN F 111 ALA F 124 1 14
HELIX 47 AF2 LEU F 134 GLY F 138 5 5
HELIX 48 AF3 ASN F 143 VAL F 154 1 12
HELIX 49 AF4 ASP F 155 ARG F 172 1 18
HELIX 50 AF5 CME F 186 TYR F 199 1 14
HELIX 51 AF6 PRO F 214 ILE F 221 5 8
HELIX 52 AF7 ASP F 233 GLU F 238 1 6
HELIX 53 AF8 GLY F 239 ASN F 250 1 12
HELIX 54 AF9 ASP F 275 LEU F 294 1 20
SHEET 1 AA1 6 ILE A 68 SER A 77 0
SHEET 2 AA1 6 GLY A 82 PRO A 91 -1 O VAL A 84 N TYR A 75
SHEET 3 AA1 6 ILE A 127 PRO A 131 -1 O ALA A 128 N VAL A 89
SHEET 4 AA1 6 THR A 98 VAL A 104 1 N VAL A 101 O ILE A 127
SHEET 5 AA1 6 ALA A 176 PHE A 185 1 O THR A 183 N VAL A 104
SHEET 6 AA1 6 CYS A 204 PHE A 208 1 O PHE A 208 N GLY A 184
SHEET 1 AA2 2 LEU A 225 ALA A 230 0
SHEET 2 AA2 2 TYR A 254 TYR A 259 1 O TYR A 257 N PHE A 229
SHEET 1 AA3 6 ILE B 68 SER B 77 0
SHEET 2 AA3 6 GLY B 82 PRO B 91 -1 O VAL B 84 N TYR B 75
SHEET 3 AA3 6 ILE B 127 PRO B 131 -1 O ALA B 128 N VAL B 89
SHEET 4 AA3 6 THR B 98 VAL B 104 1 N VAL B 101 O ILE B 127
SHEET 5 AA3 6 ALA B 176 PHE B 185 1 O THR B 183 N VAL B 104
SHEET 6 AA3 6 CYS B 204 PHE B 208 1 O PHE B 208 N GLY B 184
SHEET 1 AA4 2 LEU B 225 ALA B 230 0
SHEET 2 AA4 2 TYR B 254 TYR B 259 1 O TYR B 257 N PHE B 229
SHEET 1 AA5 6 ILE C 68 SER C 77 0
SHEET 2 AA5 6 GLY C 82 PRO C 91 -1 O VAL C 84 N TYR C 75
SHEET 3 AA5 6 ILE C 127 PRO C 131 -1 O ALA C 128 N VAL C 89
SHEET 4 AA5 6 THR C 98 VAL C 104 1 N VAL C 101 O ILE C 127
SHEET 5 AA5 6 ALA C 176 PHE C 185 1 O THR C 183 N VAL C 104
SHEET 6 AA5 6 CYS C 204 PHE C 208 1 O PHE C 208 N GLY C 184
SHEET 1 AA6 2 LEU C 225 ALA C 230 0
SHEET 2 AA6 2 TYR C 254 TYR C 259 1 O TYR C 257 N PHE C 229
SHEET 1 AA7 6 ILE D 68 SER D 77 0
SHEET 2 AA7 6 GLY D 82 PRO D 91 -1 O LEU D 88 N GLU D 71
SHEET 3 AA7 6 ILE D 127 PRO D 131 -1 O ALA D 128 N VAL D 89
SHEET 4 AA7 6 THR D 98 VAL D 104 1 N VAL D 101 O ILE D 127
SHEET 5 AA7 6 ALA D 176 PHE D 185 1 O THR D 183 N VAL D 104
SHEET 6 AA7 6 CYS D 204 PHE D 208 1 O PHE D 208 N GLY D 184
SHEET 1 AA8 2 LEU D 225 ALA D 230 0
SHEET 2 AA8 2 TYR D 254 TYR D 259 1 O TYR D 257 N PHE D 229
SHEET 1 AA9 6 ILE E 68 SER E 77 0
SHEET 2 AA9 6 GLY E 82 PRO E 91 -1 O VAL E 84 N TYR E 75
SHEET 3 AA9 6 ILE E 127 PRO E 131 -1 O ALA E 128 N VAL E 89
SHEET 4 AA9 6 THR E 98 VAL E 104 1 N VAL E 101 O ILE E 127
SHEET 5 AA9 6 ALA E 176 PHE E 185 1 O THR E 183 N VAL E 104
SHEET 6 AA9 6 CYS E 204 PHE E 208 1 O PHE E 208 N GLY E 184
SHEET 1 AB1 2 LEU E 225 ALA E 230 0
SHEET 2 AB1 2 TYR E 254 TYR E 259 1 O TYR E 257 N PHE E 229
SHEET 1 AB2 6 ILE F 68 SER F 77 0
SHEET 2 AB2 6 GLY F 82 PRO F 91 -1 O GLY F 82 N SER F 77
SHEET 3 AB2 6 ILE F 127 PRO F 131 -1 O ALA F 128 N VAL F 89
SHEET 4 AB2 6 THR F 98 VAL F 104 1 N VAL F 101 O ILE F 127
SHEET 5 AB2 6 ALA F 176 PHE F 185 1 O THR F 183 N VAL F 104
SHEET 6 AB2 6 CYS F 204 PHE F 208 1 O PHE F 208 N GLY F 184
SHEET 1 AB3 2 LEU F 225 ALA F 230 0
SHEET 2 AB3 2 TYR F 254 TYR F 259 1 O TYR F 257 N PHE F 229
LINK C LYS A 93 N MSE A 94 1555 1555 1.33
LINK C MSE A 94 N SER A 95 1555 1555 1.33
LINK C LEU A 159 N AMSE A 160 1555 1555 1.33
LINK C LEU A 159 N BMSE A 160 1555 1555 1.33
LINK C AMSE A 160 N ASN A 161 1555 1555 1.33
LINK C BMSE A 160 N ASN A 161 1555 1555 1.33
LINK C PHE A 169 N AMSE A 170 1555 1555 1.33
LINK C PHE A 169 N BMSE A 170 1555 1555 1.33
LINK C AMSE A 170 N AGLN A 171 1555 1555 1.33
LINK C BMSE A 170 N BGLN A 171 1555 1555 1.33
LINK C PHE A 185 N CME A 186 1555 1555 1.33
LINK C CME A 186 N TYR A 187 1555 1555 1.33
LINK C LYS B 93 N MSE B 94 1555 1555 1.33
LINK C MSE B 94 N SER B 95 1555 1555 1.33
LINK C LEU B 159 N AMSE B 160 1555 1555 1.33
LINK C LEU B 159 N BMSE B 160 1555 1555 1.33
LINK C AMSE B 160 N ASN B 161 1555 1555 1.33
LINK C BMSE B 160 N ASN B 161 1555 1555 1.33
LINK C PHE B 169 N MSE B 170 1555 1555 1.33
LINK C MSE B 170 N GLN B 171 1555 1555 1.33
LINK C PHE B 185 N CME B 186 1555 1555 1.34
LINK C CME B 186 N TYR B 187 1555 1555 1.34
LINK C LYS C 93 N MSE C 94 1555 1555 1.33
LINK C MSE C 94 N SER C 95 1555 1555 1.33
LINK C LEU C 159 N MSE C 160 1555 1555 1.33
LINK C MSE C 160 N ASN C 161 1555 1555 1.33
LINK C PHE C 169 N MSE C 170 1555 1555 1.33
LINK C MSE C 170 N GLN C 171 1555 1555 1.33
LINK C PHE C 185 N CME C 186 1555 1555 1.33
LINK C CME C 186 N TYR C 187 1555 1555 1.33
LINK C LYS D 93 N MSE D 94 1555 1555 1.33
LINK C MSE D 94 N SER D 95 1555 1555 1.33
LINK C LEU D 159 N AMSE D 160 1555 1555 1.33
LINK C LEU D 159 N BMSE D 160 1555 1555 1.33
LINK C AMSE D 160 N ASN D 161 1555 1555 1.33
LINK C BMSE D 160 N ASN D 161 1555 1555 1.33
LINK C PHE D 169 N AMSE D 170 1555 1555 1.33
LINK C PHE D 169 N BMSE D 170 1555 1555 1.33
LINK C AMSE D 170 N GLN D 171 1555 1555 1.33
LINK C BMSE D 170 N GLN D 171 1555 1555 1.33
LINK C PHE D 185 N CME D 186 1555 1555 1.34
LINK C CME D 186 N TYR D 187 1555 1555 1.34
LINK C LYS E 93 N AMSE E 94 1555 1555 1.33
LINK C LYS E 93 N BMSE E 94 1555 1555 1.33
LINK C AMSE E 94 N SER E 95 1555 1555 1.33
LINK C BMSE E 94 N SER E 95 1555 1555 1.33
LINK C LEU E 159 N AMSE E 160 1555 1555 1.33
LINK C LEU E 159 N BMSE E 160 1555 1555 1.33
LINK C AMSE E 160 N ASN E 161 1555 1555 1.33
LINK C BMSE E 160 N ASN E 161 1555 1555 1.33
LINK C PHE E 169 N MSE E 170 1555 1555 1.33
LINK C MSE E 170 N GLN E 171 1555 1555 1.33
LINK C PHE E 185 N ACME E 186 1555 1555 1.34
LINK C PHE E 185 N BCME E 186 1555 1555 1.34
LINK C ACME E 186 N TYR E 187 1555 1555 1.34
LINK C BCME E 186 N TYR E 187 1555 1555 1.34
LINK C LYS F 93 N MSE F 94 1555 1555 1.33
LINK C MSE F 94 N SER F 95 1555 1555 1.33
LINK C LEU F 159 N AMSE F 160 1555 1555 1.32
LINK C LEU F 159 N BMSE F 160 1555 1555 1.33
LINK C AMSE F 160 N ASN F 161 1555 1555 1.34
LINK C BMSE F 160 N ASN F 161 1555 1555 1.33
LINK C PHE F 169 N MSE F 170 1555 1555 1.33
LINK C MSE F 170 N GLN F 171 1555 1555 1.33
LINK C PHE F 185 N CME F 186 1555 1555 1.34
LINK C CME F 186 N TYR F 187 1555 1555 1.34
SITE 1 AC1 3 GLN A 60 HOH A 401 GLN F 60
SITE 1 AC2 5 ASN A 79 ASN A 161 ALA A 165 GLU A 168
SITE 2 AC2 5 HOH A 404
SITE 1 AC3 5 ARG A 172 ALA F 249 ASN F 250 HOH F 435
SITE 2 AC3 5 HOH F 504
SITE 1 AC4 7 LYS B 97 GLN B 171 ARG B 172 TYR B 173
SITE 2 AC4 7 ALA B 176 THR B 177 GLY B 178
SITE 1 AC5 5 ASN B 79 ASN B 161 GLU B 168 TYR B 199
SITE 2 AC5 5 HOH B 434
SITE 1 AC6 7 SER D 77 PRO D 78 ASN D 79 GLY D 80
SITE 2 AC6 7 ASN D 161 ALA D 165 GLU D 168
SITE 1 AC7 3 HOH B 570 HOH E 451 HOH E 576
SITE 1 AC8 6 PRO E 78 ASN E 79 ASN E 161 ALA E 165
SITE 2 AC8 6 GLU E 168 HOH E 402
SITE 1 AC9 10 ASP E 275 SER E 277 HOH E 420 HOH E 487
SITE 2 AC9 10 PHE F 169 ARG F 172 TYR F 173 PRO F 174
SITE 3 AC9 10 HOH F 473 HOH F 508
SITE 1 AD1 7 ASN F 135 GLY F 138 GLY F 139 HOH F 401
SITE 2 AD1 7 HOH F 407 HOH F 469 HOH F 503
SITE 1 AD2 7 LYS E 276 ASP E 280 PRO F 76 ALA F 165
SITE 2 AD2 7 GLU F 168 PHE F 169 ARG F 172
SITE 1 AD3 7 ASN F 79 ASN F 161 ALA F 165 GLU F 168
SITE 2 AD3 7 TYR F 199 PEG F 304 HOH F 426
SITE 1 AD4 4 ALA F 198 TYR F 199 GLU F 201 GOL F 303
CRYST1 70.615 96.341 129.617 90.00 98.22 90.00 P 1 21 1 12
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 0.014161 0.000000 0.002046 0.00000
SCALE2 0.000000 0.010380 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007795 0.00000
TER 1911 LEU A 294
TER 3838 LEU B 294
TER 5695 LEU C 294
TER 7594 LEU D 294
TER 9495 LEU E 294
TER 11388 LEU F 294
MASTER 656 0 37 54 48 0 24 612530 6 409 114
END |