HEADER HYDROLASE/HYDROLASE INHIBITOR 30-MAR-11 3RC5
TITLE MOLECULAR MECHANISMS OF VIRAL AND HOST-CELL SUBSTRATE RECOGNITION BY
TITLE 2 HCV NS3/4A PROTEASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NS3/4A PROTEASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 36-218;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: PRODUCT MAVS;
COMPND 9 CHAIN: B;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HEPATITIS C VIRUS SUBTYPE 1A;
SOURCE 3 ORGANISM_TAXID: 31646;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET28A;
SOURCE 9 MOL_ID: 2;
SOURCE 10 SYNTHETIC: YES;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606
KEYWDS DRUG RESISTANCE, DRUG DESIGN, PROTEASE INHIBITORS, SERINE PROTEASE,
KEYWDS 2 HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR C.A.SCHIFFER,K.P.ROMANO
REVDAT 5 13-SEP-23 3RC5 1 REMARK
REVDAT 4 26-JUL-23 3RC5 1 JRNL REMARK LINK
REVDAT 3 08-NOV-17 3RC5 1 REMARK
REVDAT 2 28-JUN-17 3RC5 1 DBREF
REVDAT 1 04-MAY-11 3RC5 0
JRNL AUTH K.P.ROMANO,J.M.LAINE,L.M.DEVEAU,H.CAO,F.MASSI,C.A.SCHIFFER
JRNL TITL MOLECULAR MECHANISMS OF VIRAL AND HOST CELL SUBSTRATE
JRNL TITL 2 RECOGNITION BY HEPATITIS C VIRUS NS3/4A PROTEASE.
JRNL REF J.VIROL. V. 85 6106 2011
JRNL REFN ESSN 1098-5514
JRNL PMID 21507982
JRNL DOI 10.1128/JVI.00377-11
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.05
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 25918
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) : 0.173
REMARK 3 R VALUE (WORKING SET) : 0.171
REMARK 3 FREE R VALUE : 0.193
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1310
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) : 1.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.64
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1784
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.06
REMARK 3 BIN R VALUE (WORKING SET) : 0.1870
REMARK 3 BIN FREE R VALUE SET COUNT : 88
REMARK 3 BIN FREE R VALUE : 0.2410
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1502
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 11
REMARK 3 SOLVENT ATOMS : 182
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.19
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.49000
REMARK 3 B22 (A**2) : -1.27000
REMARK 3 B33 (A**2) : 0.78000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.083
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.052
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.949
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.964
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.955
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1541 ; 0.009 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 1021 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2097 ; 1.260 ; 1.972
REMARK 3 BOND ANGLES OTHERS (DEGREES): 2499 ; 0.820 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 205 ; 6.187 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 56 ;34.002 ;23.393
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 245 ;12.655 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 12 ;16.891 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 245 ; 0.073 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1726 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 292 ; 0.001 ; 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): 1019 ; 0.598 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 421 ; 0.159 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1639 ; 1.093 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 522 ; 1.665 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 457 ; 2.704 ; 4.500
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 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 20
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 983 A 988
REMARK 3 ORIGIN FOR THE GROUP (A): 6.9692 -20.8927 -2.7105
REMARK 3 T TENSOR
REMARK 3 T11: 0.4806 T22: 0.1023
REMARK 3 T33: 0.0691 T12: 0.0208
REMARK 3 T13: 0.1137 T23: 0.0436
REMARK 3 L TENSOR
REMARK 3 L11: 5.8636 L22: 26.7787
REMARK 3 L33: 26.0368 L12: -0.4753
REMARK 3 L13: 3.0810 L23: 25.2976
REMARK 3 S TENSOR
REMARK 3 S11: 0.8298 S12: -0.2533 S13: 0.0482
REMARK 3 S21: -0.4681 S22: -0.0208 S23: -0.8149
REMARK 3 S31: 0.1568 S32: -0.0797 S33: -0.8090
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 989 A 997
REMARK 3 ORIGIN FOR THE GROUP (A): 4.9493 -6.1237 14.8820
REMARK 3 T TENSOR
REMARK 3 T11: 0.0467 T22: 0.0978
REMARK 3 T33: 0.0856 T12: -0.0028
REMARK 3 T13: 0.0058 T23: 0.0136
REMARK 3 L TENSOR
REMARK 3 L11: 0.6251 L22: 4.2402
REMARK 3 L33: 0.4856 L12: 0.3869
REMARK 3 L13: -0.5294 L23: -0.5783
REMARK 3 S TENSOR
REMARK 3 S11: 0.0560 S12: 0.0440 S13: -0.0163
REMARK 3 S21: -0.1615 S22: -0.0944 S23: -0.1053
REMARK 3 S31: -0.0435 S32: 0.0124 S33: 0.0383
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 : A 998 A 1007
REMARK 3 ORIGIN FOR THE GROUP (A): -0.0202 7.1245 28.1764
REMARK 3 T TENSOR
REMARK 3 T11: 0.1696 T22: 0.0692
REMARK 3 T33: 0.0825 T12: -0.0192
REMARK 3 T13: 0.0101 T23: -0.0189
REMARK 3 L TENSOR
REMARK 3 L11: 5.0254 L22: 7.2584
REMARK 3 L33: 7.9334 L12: 0.6374
REMARK 3 L13: 0.5360 L23: -3.1727
REMARK 3 S TENSOR
REMARK 3 S11: 0.1793 S12: -0.2449 S13: 0.3241
REMARK 3 S21: 0.7052 S22: -0.1082 S23: -0.0727
REMARK 3 S31: -0.4637 S32: 0.0495 S33: -0.0711
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 : A 1008 A 1012
REMARK 3 ORIGIN FOR THE GROUP (A): 7.0122 3.2669 16.0661
REMARK 3 T TENSOR
REMARK 3 T11: 0.1041 T22: 0.0795
REMARK 3 T33: 0.0973 T12: -0.0014
REMARK 3 T13: -0.0008 T23: 0.0210
REMARK 3 L TENSOR
REMARK 3 L11: 2.2179 L22: 4.7614
REMARK 3 L33: 0.6780 L12: 1.3019
REMARK 3 L13: -1.2109 L23: -0.4524
REMARK 3 S TENSOR
REMARK 3 S11: 0.0451 S12: -0.2124 S13: -0.1175
REMARK 3 S21: -0.0728 S22: -0.0847 S23: -0.1264
REMARK 3 S31: -0.0464 S32: 0.1211 S33: 0.0396
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 : A 1013 A 1027
REMARK 3 ORIGIN FOR THE GROUP (A): 11.4038 -5.3550 10.9702
REMARK 3 T TENSOR
REMARK 3 T11: 0.0650 T22: 0.0724
REMARK 3 T33: 0.0973 T12: 0.0078
REMARK 3 T13: 0.0465 T23: 0.0305
REMARK 3 L TENSOR
REMARK 3 L11: 3.0824 L22: 4.9418
REMARK 3 L33: 5.6797 L12: -0.8951
REMARK 3 L13: 0.0238 L23: 0.1354
REMARK 3 S TENSOR
REMARK 3 S11: -0.0692 S12: 0.1281 S13: 0.0156
REMARK 3 S21: -0.3108 S22: -0.1226 S23: -0.2835
REMARK 3 S31: -0.0676 S32: 0.3064 S33: 0.1918
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 : A 1028 A 1033
REMARK 3 ORIGIN FOR THE GROUP (A): 6.3250 -1.6528 26.3925
REMARK 3 T TENSOR
REMARK 3 T11: 0.0980 T22: 0.0645
REMARK 3 T33: 0.1276 T12: -0.0431
REMARK 3 T13: -0.0556 T23: -0.0080
REMARK 3 L TENSOR
REMARK 3 L11: 11.1171 L22: 3.8192
REMARK 3 L33: 4.8238 L12: 2.1670
REMARK 3 L13: -3.3888 L23: 0.6282
REMARK 3 S TENSOR
REMARK 3 S11: 0.0485 S12: -0.5988 S13: 0.4778
REMARK 3 S21: 0.2431 S22: -0.0890 S23: -0.3516
REMARK 3 S31: -0.2382 S32: 0.3308 S33: 0.0405
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 : A 1034 A 1041
REMARK 3 ORIGIN FOR THE GROUP (A): -0.0377 -5.2736 13.4052
REMARK 3 T TENSOR
REMARK 3 T11: 0.0732 T22: 0.0759
REMARK 3 T33: 0.0505 T12: 0.0146
REMARK 3 T13: -0.0081 T23: 0.0088
REMARK 3 L TENSOR
REMARK 3 L11: 0.8141 L22: 2.6125
REMARK 3 L33: 6.1216 L12: 0.7302
REMARK 3 L13: 0.8171 L23: 1.1617
REMARK 3 S TENSOR
REMARK 3 S11: 0.1178 S12: 0.0950 S13: -0.0335
REMARK 3 S21: -0.1934 S22: -0.0113 S23: -0.0573
REMARK 3 S31: -0.0562 S32: -0.1954 S33: -0.1066
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 : A 1042 A 1063
REMARK 3 ORIGIN FOR THE GROUP (A): -1.3317 -11.3464 20.2499
REMARK 3 T TENSOR
REMARK 3 T11: 0.0415 T22: 0.0392
REMARK 3 T33: 0.0534 T12: 0.0026
REMARK 3 T13: -0.0005 T23: 0.0117
REMARK 3 L TENSOR
REMARK 3 L11: 1.9165 L22: 1.6641
REMARK 3 L33: 0.9813 L12: -0.2090
REMARK 3 L13: -0.0062 L23: -0.0201
REMARK 3 S TENSOR
REMARK 3 S11: 0.0345 S12: 0.0061 S13: -0.0607
REMARK 3 S21: 0.0037 S22: -0.0469 S23: -0.0552
REMARK 3 S31: 0.0230 S32: -0.0383 S33: 0.0123
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 : A 1064 A 1075
REMARK 3 ORIGIN FOR THE GROUP (A): 8.8388 -15.3753 19.4152
REMARK 3 T TENSOR
REMARK 3 T11: 0.0462 T22: 0.0729
REMARK 3 T33: 0.1372 T12: 0.0243
REMARK 3 T13: 0.0112 T23: 0.0173
REMARK 3 L TENSOR
REMARK 3 L11: 4.2396 L22: 1.6122
REMARK 3 L33: 2.1335 L12: 2.2880
REMARK 3 L13: -0.9804 L23: -1.3756
REMARK 3 S TENSOR
REMARK 3 S11: -0.0019 S12: -0.1333 S13: -0.2531
REMARK 3 S21: -0.0611 S22: -0.1693 S23: -0.2040
REMARK 3 S31: 0.1406 S32: 0.2263 S33: 0.1712
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 : A 1076 A 1089
REMARK 3 ORIGIN FOR THE GROUP (A): -0.7902 -16.2970 22.1182
REMARK 3 T TENSOR
REMARK 3 T11: 0.0565 T22: 0.0357
REMARK 3 T33: 0.0786 T12: 0.0072
REMARK 3 T13: -0.0116 T23: 0.0168
REMARK 3 L TENSOR
REMARK 3 L11: 1.4721 L22: 1.4776
REMARK 3 L33: 1.7022 L12: 0.8035
REMARK 3 L13: -0.1609 L23: 0.3936
REMARK 3 S TENSOR
REMARK 3 S11: -0.0084 S12: 0.0432 S13: -0.1234
REMARK 3 S21: 0.0474 S22: -0.0544 S23: -0.1063
REMARK 3 S31: 0.1035 S32: 0.0556 S33: 0.0628
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 : A 1090 A 1104
REMARK 3 ORIGIN FOR THE GROUP (A): -6.3653 -6.7980 36.0868
REMARK 3 T TENSOR
REMARK 3 T11: 0.1069 T22: 0.2353
REMARK 3 T33: 0.1042 T12: -0.0245
REMARK 3 T13: 0.0011 T23: -0.1103
REMARK 3 L TENSOR
REMARK 3 L11: 1.5031 L22: 0.9242
REMARK 3 L33: 2.5042 L12: -0.6686
REMARK 3 L13: -1.5617 L23: 0.1820
REMARK 3 S TENSOR
REMARK 3 S11: -0.0706 S12: -0.3695 S13: 0.0881
REMARK 3 S21: 0.2425 S22: 0.0490 S23: 0.0295
REMARK 3 S31: -0.1196 S32: 0.2372 S33: 0.0216
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 : A 1105 A 1110
REMARK 3 ORIGIN FOR THE GROUP (A): -8.4931 1.7101 24.1857
REMARK 3 T TENSOR
REMARK 3 T11: 0.0755 T22: 0.0151
REMARK 3 T33: 0.1362 T12: 0.0206
REMARK 3 T13: 0.0012 T23: -0.0070
REMARK 3 L TENSOR
REMARK 3 L11: 3.4192 L22: 3.8541
REMARK 3 L33: 9.4269 L12: 2.4444
REMARK 3 L13: -3.2277 L23: -2.5610
REMARK 3 S TENSOR
REMARK 3 S11: -0.1569 S12: -0.0711 S13: 0.3012
REMARK 3 S21: -0.1058 S22: -0.0252 S23: 0.2488
REMARK 3 S31: -0.1743 S32: 0.0454 S33: 0.1821
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1111 A 1118
REMARK 3 ORIGIN FOR THE GROUP (A): -14.6579 0.3734 29.6267
REMARK 3 T TENSOR
REMARK 3 T11: 0.1307 T22: 0.0970
REMARK 3 T33: 0.1767 T12: 0.0583
REMARK 3 T13: 0.0772 T23: -0.0184
REMARK 3 L TENSOR
REMARK 3 L11: 3.5281 L22: 0.5327
REMARK 3 L33: 1.6737 L12: 1.3196
REMARK 3 L13: -1.1374 L23: -0.6114
REMARK 3 S TENSOR
REMARK 3 S11: 0.1733 S12: -0.1231 S13: 0.6092
REMARK 3 S21: 0.1118 S22: 0.0305 S23: 0.2461
REMARK 3 S31: -0.2009 S32: -0.1947 S33: -0.2038
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1119 A 1128
REMARK 3 ORIGIN FOR THE GROUP (A): -20.0987 -6.3873 28.3070
REMARK 3 T TENSOR
REMARK 3 T11: 0.0819 T22: 0.1112
REMARK 3 T33: 0.1055 T12: 0.0198
REMARK 3 T13: 0.0351 T23: 0.0099
REMARK 3 L TENSOR
REMARK 3 L11: 1.9329 L22: 2.3112
REMARK 3 L33: 2.9856 L12: 0.6362
REMARK 3 L13: -1.4856 L23: -1.1599
REMARK 3 S TENSOR
REMARK 3 S11: 0.0433 S12: 0.0225 S13: 0.0417
REMARK 3 S21: 0.0999 S22: 0.1092 S23: 0.4472
REMARK 3 S31: -0.1927 S32: -0.1717 S33: -0.1525
REMARK 3
REMARK 3 TLS GROUP : 15
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1129 A 1134
REMARK 3 ORIGIN FOR THE GROUP (A): -17.1935 3.3448 17.6916
REMARK 3 T TENSOR
REMARK 3 T11: 0.1217 T22: 0.1377
REMARK 3 T33: 0.1335 T12: -0.0089
REMARK 3 T13: 0.0145 T23: 0.0664
REMARK 3 L TENSOR
REMARK 3 L11: 12.0781 L22: 4.2057
REMARK 3 L33: 5.5495 L12: 3.7174
REMARK 3 L13: -0.1473 L23: -2.4155
REMARK 3 S TENSOR
REMARK 3 S11: 0.2763 S12: -0.1157 S13: 0.4291
REMARK 3 S21: 0.4523 S22: -0.3237 S23: -0.1152
REMARK 3 S31: -0.0904 S32: -0.2593 S33: 0.0474
REMARK 3
REMARK 3 TLS GROUP : 16
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1135 A 1142
REMARK 3 ORIGIN FOR THE GROUP (A): -8.9380 -3.2754 19.4609
REMARK 3 T TENSOR
REMARK 3 T11: 0.0513 T22: 0.0489
REMARK 3 T33: 0.1106 T12: 0.0049
REMARK 3 T13: -0.0016 T23: 0.0053
REMARK 3 L TENSOR
REMARK 3 L11: 1.7088 L22: 1.1346
REMARK 3 L33: 2.9765 L12: -0.2010
REMARK 3 L13: -2.2110 L23: -0.0966
REMARK 3 S TENSOR
REMARK 3 S11: 0.0966 S12: 0.0817 S13: 0.0704
REMARK 3 S21: 0.0066 S22: -0.0022 S23: 0.0402
REMARK 3 S31: -0.1318 S32: -0.1082 S33: -0.0944
REMARK 3
REMARK 3 TLS GROUP : 17
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1143 A 1153
REMARK 3 ORIGIN FOR THE GROUP (A): -8.2686 -5.1201 34.0539
REMARK 3 T TENSOR
REMARK 3 T11: 0.0776 T22: 0.1094
REMARK 3 T33: 0.0903 T12: -0.0122
REMARK 3 T13: 0.0200 T23: -0.0683
REMARK 3 L TENSOR
REMARK 3 L11: 2.7104 L22: 1.2818
REMARK 3 L33: 3.1729 L12: -0.2601
REMARK 3 L13: -1.2037 L23: 0.7020
REMARK 3 S TENSOR
REMARK 3 S11: 0.0868 S12: -0.4014 S13: 0.4451
REMARK 3 S21: 0.0597 S22: -0.0509 S23: -0.0194
REMARK 3 S31: -0.0600 S32: -0.0724 S33: -0.0359
REMARK 3
REMARK 3 TLS GROUP : 18
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1154 A 1159
REMARK 3 ORIGIN FOR THE GROUP (A): -15.9321 -7.5003 20.0591
REMARK 3 T TENSOR
REMARK 3 T11: 0.0612 T22: 0.1354
REMARK 3 T33: 0.1405 T12: -0.0014
REMARK 3 T13: -0.0020 T23: 0.0588
REMARK 3 L TENSOR
REMARK 3 L11: 7.5145 L22: 1.2281
REMARK 3 L33: 0.0605 L12: -0.4142
REMARK 3 L13: -0.2596 L23: -0.0097
REMARK 3 S TENSOR
REMARK 3 S11: 0.2246 S12: 0.1557 S13: 0.2140
REMARK 3 S21: -0.0608 S22: -0.1355 S23: 0.2431
REMARK 3 S31: 0.0023 S32: -0.0797 S33: -0.0891
REMARK 3
REMARK 3 TLS GROUP : 19
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1160 A 1172
REMARK 3 ORIGIN FOR THE GROUP (A): -17.7332 -6.7313 22.7200
REMARK 3 T TENSOR
REMARK 3 T11: 0.0719 T22: 0.1001
REMARK 3 T33: 0.0906 T12: 0.0078
REMARK 3 T13: 0.0190 T23: 0.0309
REMARK 3 L TENSOR
REMARK 3 L11: 2.1672 L22: 1.8904
REMARK 3 L33: 2.5436 L12: -0.5535
REMARK 3 L13: 0.4636 L23: -1.5368
REMARK 3 S TENSOR
REMARK 3 S11: -0.0390 S12: 0.1236 S13: -0.0202
REMARK 3 S21: 0.1404 S22: 0.1918 S23: 0.3507
REMARK 3 S31: -0.1819 S32: -0.2447 S33: -0.1528
REMARK 3
REMARK 3 TLS GROUP : 20
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1173 A 1179
REMARK 3 ORIGIN FOR THE GROUP (A): -5.6266 -18.5834 31.7254
REMARK 3 T TENSOR
REMARK 3 T11: 0.1964 T22: 0.0838
REMARK 3 T33: 0.0677 T12: -0.0482
REMARK 3 T13: 0.0267 T23: -0.0037
REMARK 3 L TENSOR
REMARK 3 L11: 10.1192 L22: 4.4339
REMARK 3 L33: 2.7065 L12: -2.7629
REMARK 3 L13: -4.1136 L23: -0.6332
REMARK 3 S TENSOR
REMARK 3 S11: -0.3535 S12: -0.3216 S13: -0.4111
REMARK 3 S21: 0.1183 S22: 0.0931 S23: 0.0758
REMARK 3 S31: 0.2962 S32: 0.0407 S33: 0.2604
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 : 1.40
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 U VALUES: RESIDUAL ONLY
REMARK 4
REMARK 4 3RC5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-APR-11.
REMARK 100 THE DEPOSITION ID IS D_1000064749.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-AUG-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26041
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.03900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.66
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.1
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : 0.23000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ID 3M5M
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.24
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20-25% PEG 3350, 0.1M MES (PH 6.5), 4%
REMARK 280 AMMONIUM SULFATE, HANGING DROP, VAPOR DIFFUSION, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 27.04800
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 30.66250
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 29.10500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 30.66250
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.04800
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 29.10500
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1570 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9890 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -37.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A 980
REMARK 465 SER A 981
REMARK 465 HIS A 982
REMARK 465 SER A 1181
REMARK 465 PRO A 1182
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLU A1014 CG CD OE1 OE2
REMARK 470 LYS A1026 CG CD CE NZ
REMARK 470 GLN A1028 CG CD OE1 NE2
REMARK 470 ARG A1092 CG CD NE CZ NH1 NH2
REMARK 470 ARG A1161 CG CD NE CZ NH1 NH2
REMARK 470 ARG A1180 CG CD NE CZ NH1 NH2
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 ZN A1183 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A1097 SG
REMARK 620 2 CYS A1099 SG 109.0
REMARK 620 3 CYS A1145 SG 108.5 118.9
REMARK 620 4 HIS A1149 ND1 124.6 102.9 93.0
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 SO4 A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1183
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3RC6 RELATED DB: PDB
REMARK 900 RELATED ID: 3RC4 RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE COFACTOR 4A RESIDUES 990-1000 (GLY SER VAL VAL ILE VAL GLY ARG
REMARK 999 ILE ASN LEU) IN THIS ENTRY CORRESPOND TO RESIDUES NUMBERING 1678-
REMARK 999 1688 OF DATABASE SEQUENCE REFERENCE (UNP A8DG50). THIS PEPTIDE IS
REMARK 999 COVALENTLY LINKED TO THE N-TERMINUS OF NS3. C1679S MUTATION WAS
REMARK 999 ENGINEERED TO PREVENT DISULFIDE FORMATION. THE V1686I AND I1687N
REMARK 999 WERE ENGINEERED TO OPTIMIZE THE LINKER BETWEEN THE COFACTOR 4A AND
REMARK 999 NS3.
DBREF 3RC5 A 1000 1182 UNP D6MZ98 D6MZ98_9HEPC 36 218
DBREF 3RC5 B 0 7 PDB 3RC5 3RC5 0 7
SEQADV 3RC5 GLY A 980 UNP D6MZ98 EXPRESSION TAG
SEQADV 3RC5 SER A 981 UNP D6MZ98 EXPRESSION TAG
SEQADV 3RC5 HIS A 982 UNP D6MZ98 EXPRESSION TAG
SEQADV 3RC5 MET A 983 UNP D6MZ98 EXPRESSION TAG
SEQADV 3RC5 ALA A 984 UNP D6MZ98 EXPRESSION TAG
SEQADV 3RC5 SER A 985 UNP D6MZ98 EXPRESSION TAG
SEQADV 3RC5 MET A 986 UNP D6MZ98 EXPRESSION TAG
SEQADV 3RC5 LYS A 987 UNP D6MZ98 EXPRESSION TAG
SEQADV 3RC5 LYS A 988 UNP D6MZ98 EXPRESSION TAG
SEQADV 3RC5 LYS A 989 UNP D6MZ98 EXPRESSION TAG
SEQADV 3RC5 GLY A 990 UNP D6MZ98 EXPRESSION TAG
SEQADV 3RC5 SER A 991 UNP D6MZ98 EXPRESSION TAG
SEQADV 3RC5 VAL A 992 UNP D6MZ98 EXPRESSION TAG
SEQADV 3RC5 VAL A 993 UNP D6MZ98 EXPRESSION TAG
SEQADV 3RC5 ILE A 994 UNP D6MZ98 EXPRESSION TAG
SEQADV 3RC5 VAL A 995 UNP D6MZ98 EXPRESSION TAG
SEQADV 3RC5 GLY A 996 UNP D6MZ98 EXPRESSION TAG
SEQADV 3RC5 ARG A 997 UNP D6MZ98 EXPRESSION TAG
SEQADV 3RC5 ILE A 998 UNP D6MZ98 EXPRESSION TAG
SEQADV 3RC5 ASN A 999 UNP D6MZ98 EXPRESSION TAG
SEQADV 3RC5 SER A 1001 UNP D6MZ98 ALA 37 ENGINEERED MUTATION
SEQADV 3RC5 GLY A 1002 UNP D6MZ98 PRO 38 ENGINEERED MUTATION
SEQADV 3RC5 ASP A 1003 UNP D6MZ98 ILE 39 ENGINEERED MUTATION
SEQADV 3RC5 GLU A 1013 UNP D6MZ98 LEU 49 ENGINEERED MUTATION
SEQADV 3RC5 GLU A 1014 UNP D6MZ98 LEU 50 ENGINEERED MUTATION
SEQADV 3RC5 GLN A 1017 UNP D6MZ98 ILE 53 ENGINEERED MUTATION
SEQADV 3RC5 GLU A 1018 UNP D6MZ98 VAL 54 ENGINEERED MUTATION
SEQADV 3RC5 GLN A 1021 UNP D6MZ98 LEU 57 ENGINEERED MUTATION
SEQADV 3RC5 SER A 1047 UNP D6MZ98 CYS 83 ENGINEERED MUTATION
SEQADV 3RC5 LEU A 1052 UNP D6MZ98 CYS 88 ENGINEERED MUTATION
SEQADV 3RC5 THR A 1072 UNP D6MZ98 ILE 108 ENGINEERED MUTATION
SEQADV 3RC5 LYS A 1080 UNP D6MZ98 GLN 116 ENGINEERED MUTATION
SEQADV 3RC5 GLN A 1086 UNP D6MZ98 PRO 122 ENGINEERED MUTATION
SEQADV 3RC5 SER A 1091 UNP D6MZ98 ALA 127 ENGINEERED MUTATION
SEQADV 3RC5 ALA A 1139 UNP D6MZ98 SER 175 ENGINEERED MUTATION
SEQADV 3RC5 SER A 1159 UNP D6MZ98 CYS 195 ENGINEERED MUTATION
SEQRES 1 A 203 GLY SER HIS MET ALA SER MET LYS LYS LYS GLY SER VAL
SEQRES 2 A 203 VAL ILE VAL GLY ARG ILE ASN LEU SER GLY ASP THR ALA
SEQRES 3 A 203 TYR ALA GLN GLN THR ARG GLY GLU GLU GLY CYS GLN GLU
SEQRES 4 A 203 THR SER GLN THR GLY ARG ASP LYS ASN GLN VAL GLU GLY
SEQRES 5 A 203 GLU VAL GLN ILE VAL SER THR ALA THR GLN THR PHE LEU
SEQRES 6 A 203 ALA THR SER ILE ASN GLY VAL LEU TRP THR VAL TYR HIS
SEQRES 7 A 203 GLY ALA GLY THR ARG THR ILE ALA SER PRO LYS GLY PRO
SEQRES 8 A 203 VAL THR GLN MET TYR THR ASN VAL ASP LYS ASP LEU VAL
SEQRES 9 A 203 GLY TRP GLN ALA PRO GLN GLY SER ARG SER LEU THR PRO
SEQRES 10 A 203 CYS THR CYS GLY SER SER ASP LEU TYR LEU VAL THR ARG
SEQRES 11 A 203 HIS ALA ASP VAL ILE PRO VAL ARG ARG ARG GLY ASP SER
SEQRES 12 A 203 ARG GLY SER LEU LEU SER PRO ARG PRO ILE SER TYR LEU
SEQRES 13 A 203 LYS GLY SER ALA GLY GLY PRO LEU LEU CYS PRO ALA GLY
SEQRES 14 A 203 HIS ALA VAL GLY ILE PHE ARG ALA ALA VAL SER THR ARG
SEQRES 15 A 203 GLY VAL ALA LYS ALA VAL ASP PHE ILE PRO VAL GLU SER
SEQRES 16 A 203 LEU GLU THR THR MET ARG SER PRO
SEQRES 1 B 8 ACE GLN GLU ARG GLU VAL PRO CYS
HET ACE B 0 3
HET SO4 A 1 5
HET SO4 A 2 5
HET ZN A1183 1
HETNAM ACE ACETYL GROUP
HETNAM SO4 SULFATE ION
HETNAM ZN ZINC ION
FORMUL 2 ACE C2 H4 O
FORMUL 3 SO4 2(O4 S 2-)
FORMUL 5 ZN ZN 2+
FORMUL 6 HOH *182(H2 O)
HELIX 1 1 GLY A 1012 GLY A 1023 1 12
HELIX 2 2 VAL A 1055 GLY A 1060 1 6
HELIX 3 3 ILE A 1132 LYS A 1136 1 5
HELIX 4 4 VAL A 1172 ARG A 1180 1 9
SHEET 1 A 7 TYR A1006 GLN A1009 0
SHEET 2 A 7 VAL A 993 ASN A 999 -1 N ASN A 999 O TYR A1006
SHEET 3 A 7 VAL A1033 SER A1037 -1 O ILE A1035 N VAL A 995
SHEET 4 A 7 THR A1042 ILE A1048 -1 O ALA A1045 N GLN A1034
SHEET 5 A 7 VAL A1051 THR A1054 -1 O TRP A1053 N THR A1046
SHEET 6 A 7 LEU A1082 GLN A1086 -1 O TRP A1085 N LEU A1052
SHEET 7 A 7 TYR A1075 ASN A1077 -1 N ASN A1077 O LEU A1082
SHEET 1 B 8 ARG B 3 PRO B 6 0
SHEET 2 B 8 ALA A1150 THR A1160 -1 N SER A1159 O ARG B 3
SHEET 3 B 8 VAL A1163 PRO A1171 -1 O ASP A1168 N ALA A1156
SHEET 4 B 8 ARG A1123 PRO A1131 -1 N ARG A1130 O ALA A1164
SHEET 5 B 8 VAL A1113 ARG A1118 -1 N ARG A1117 O SER A1125
SHEET 6 B 8 ASP A1103 VAL A1107 -1 N LEU A1106 O ILE A1114
SHEET 7 B 8 PRO A1142 LEU A1144 -1 O LEU A1144 N TYR A1105
SHEET 8 B 8 ALA A1150 THR A1160 -1 O VAL A1151 N LEU A1143
LINK C ACE B 0 N GLN B 1 1555 1555 1.33
LINK SG CYS A1097 ZN ZN A1183 1555 1555 2.38
LINK SG CYS A1099 ZN ZN A1183 1555 1555 2.30
LINK SG CYS A1145 ZN ZN A1183 1555 1555 2.14
LINK ND1 HIS A1149 ZN ZN A1183 1555 1555 2.27
SITE 1 AC1 7 HOH A 9 HOH A 17 HOH A 20 HOH A 47
SITE 2 AC1 7 TYR A1006 GLN A1008 TYR A1056
SITE 1 AC2 7 HOH A 151 LYS A 989 GLY A 990 SER A1020
SITE 2 AC2 7 THR A1038 ALA A1039 ARG A1062
SITE 1 AC3 4 CYS A1097 CYS A1099 CYS A1145 HIS A1149
CRYST1 54.096 58.210 61.325 90.00 90.00 90.00 P 21 21 21 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.018486 0.000000 0.000000 0.00000
SCALE2 0.000000 0.017179 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016307 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
