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HEADER TRANSFERASE 05-DEC-13 4NVR
TITLE 2.22 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF A PUTATIVE
TITLE 2 ACYLTRANSFERASE FROM SALMONELLA ENTERICA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE ACYLTRANSFERASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SALMONELLA ENTERICA;
SOURCE 3 ORGANISM_TAXID: 99287;
SOURCE 4 STRAIN: LT2 / SGSC1412 / ATCC 700720;
SOURCE 5 GENE: MHPC, STM0332;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21-CODONPLUS(DE3)-RIPL;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMCSG7
KEYWDS STRUCTURAL GENOMICS, CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS
KEYWDS 2 DISEASES, CSGID, ALPHA/BETA HYDROLASE FAMILY, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR G.MINASOV,Z.WAWRZAK,T.SKARINA,E.GORDON,J.STAM,K.KWON,A.SAVCHENKO,
AUTHOR 2 W.F.ANDERSON,CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES
AUTHOR 3 (CSGID)
REVDAT 1 18-DEC-13 4NVR 0
JRNL AUTH G.MINASOV,Z.WAWRZAK,T.SKARINA,E.GORDON,J.STAM,K.KWON,
JRNL AUTH 2 A.SAVCHENKO,W.F.ANDERSON
JRNL TITL 2.22 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF A PUTATIVE
JRNL TITL 2 ACYLTRANSFERASE FROM SALMONELLA ENTERICA.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.22 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0046
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) : 2.22
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.63
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 3 NUMBER OF REFLECTIONS : 50666
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) : 0.184
REMARK 3 R VALUE (WORKING SET) : 0.181
REMARK 3 FREE R VALUE : 0.241
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2697
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) : 2.22
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.28
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3600
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.50
REMARK 3 BIN R VALUE (WORKING SET) : 0.2320
REMARK 3 BIN FREE R VALUE SET COUNT : 198
REMARK 3 BIN FREE R VALUE : 0.3130
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9482
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 7
REMARK 3 SOLVENT ATOMS : 597
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 27.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.82
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.14000
REMARK 3 B22 (A**2) : -1.82000
REMARK 3 B33 (A**2) : 1.00000
REMARK 3 B12 (A**2) : -1.03000
REMARK 3 B13 (A**2) : 0.02000
REMARK 3 B23 (A**2) : 0.36000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.422
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.247
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.180
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.842
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.943
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.899
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9906 ; 0.011 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 9239 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 13481 ; 1.566 ; 1.958
REMARK 3 BOND ANGLES OTHERS (DEGREES): 21245 ; 0.792 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1232 ; 3.178 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 455 ;29.455 ;23.099
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1484 ;11.051 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 71 ;14.681 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1463 ; 0.093 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 11342 ; 0.020 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 2393 ; 0.017 ; 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): 4904 ; 1.312 ; 1.267
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 4903 ; 1.312 ; 1.267
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6140 ; 1.394 ; 1.894
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 6141 ; 1.394 ; 1.894
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 5002 ; 1.513 ; 1.431
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 5002 ; 1.513 ; 1.431
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 7341 ; 2.100 ; 2.085
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 11884 ; 5.106 ;11.317
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 11693 ; 5.002 ;11.049
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 : 19
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 3 A 22
REMARK 3 ORIGIN FOR THE GROUP (A): 45.5108 42.0117 99.5046
REMARK 3 T TENSOR
REMARK 3 T11: 0.4219 T22: 0.3884
REMARK 3 T33: 0.3460 T12: -0.0039
REMARK 3 T13: -0.1843 T23: 0.1100
REMARK 3 L TENSOR
REMARK 3 L11: 9.6720 L22: 1.8978
REMARK 3 L33: 3.3526 L12: -0.1420
REMARK 3 L13: -0.8157 L23: -0.5699
REMARK 3 S TENSOR
REMARK 3 S11: 0.3974 S12: -0.7031 S13: -0.9321
REMARK 3 S21: 0.4591 S22: -0.4269 S23: -0.5759
REMARK 3 S31: 0.1123 S32: 0.1582 S33: 0.0295
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 23 A 185
REMARK 3 ORIGIN FOR THE GROUP (A): 36.7255 44.5018 83.5337
REMARK 3 T TENSOR
REMARK 3 T11: 0.0779 T22: 0.1397
REMARK 3 T33: 0.0202 T12: 0.0693
REMARK 3 T13: -0.0097 T23: -0.0071
REMARK 3 L TENSOR
REMARK 3 L11: 0.4618 L22: 1.0213
REMARK 3 L33: 1.7704 L12: 0.3193
REMARK 3 L13: 0.3967 L23: 0.2172
REMARK 3 S TENSOR
REMARK 3 S11: 0.0551 S12: -0.0838 S13: -0.0205
REMARK 3 S21: 0.0474 S22: 0.0431 S23: 0.0496
REMARK 3 S31: -0.1253 S32: -0.2731 S33: -0.0982
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 186 A 198
REMARK 3 ORIGIN FOR THE GROUP (A): 52.0839 47.9482 73.3330
REMARK 3 T TENSOR
REMARK 3 T11: 0.7586 T22: 0.8238
REMARK 3 T33: 1.0679 T12: -0.1832
REMARK 3 T13: -0.5360 T23: 0.3280
REMARK 3 L TENSOR
REMARK 3 L11: 1.6494 L22: 19.3131
REMARK 3 L33: 0.1006 L12: 5.6195
REMARK 3 L13: -0.3780 L23: -1.3339
REMARK 3 S TENSOR
REMARK 3 S11: -0.6793 S12: 0.2972 S13: 0.6910
REMARK 3 S21: -2.1196 S22: 0.7693 S23: 2.0362
REMARK 3 S31: 0.0916 S32: -0.0033 S33: -0.0900
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 199 A 304
REMARK 3 ORIGIN FOR THE GROUP (A): 37.8853 51.9366 79.5270
REMARK 3 T TENSOR
REMARK 3 T11: 0.1438 T22: 0.1515
REMARK 3 T33: 0.0199 T12: 0.1015
REMARK 3 T13: 0.0141 T23: -0.0171
REMARK 3 L TENSOR
REMARK 3 L11: 0.4055 L22: 0.8844
REMARK 3 L33: 1.4978 L12: -0.1052
REMARK 3 L13: 0.1442 L23: -0.1641
REMARK 3 S TENSOR
REMARK 3 S11: -0.0208 S12: -0.0000 S13: 0.0338
REMARK 3 S21: -0.0235 S22: 0.1141 S23: -0.0113
REMARK 3 S31: -0.3490 S32: -0.1897 S33: -0.0932
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 : B 3 B 15
REMARK 3 ORIGIN FOR THE GROUP (A): 24.0089 -1.2089 35.4957
REMARK 3 T TENSOR
REMARK 3 T11: 0.2475 T22: 0.2004
REMARK 3 T33: 0.0922 T12: 0.0460
REMARK 3 T13: 0.0873 T23: 0.0173
REMARK 3 L TENSOR
REMARK 3 L11: 13.6364 L22: 4.3516
REMARK 3 L33: 6.9267 L12: -5.0468
REMARK 3 L13: 4.1635 L23: -4.4935
REMARK 3 S TENSOR
REMARK 3 S11: 0.0113 S12: 0.5177 S13: 0.3940
REMARK 3 S21: -0.4097 S22: -0.1723 S23: -0.4084
REMARK 3 S31: -0.0338 S32: -0.1698 S33: 0.1611
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 : B 16 B 185
REMARK 3 ORIGIN FOR THE GROUP (A): 13.2809 -2.9221 50.7869
REMARK 3 T TENSOR
REMARK 3 T11: 0.0644 T22: 0.1163
REMARK 3 T33: 0.0257 T12: -0.0034
REMARK 3 T13: -0.0038 T23: -0.0184
REMARK 3 L TENSOR
REMARK 3 L11: 0.4155 L22: 1.0839
REMARK 3 L33: 1.8383 L12: -0.1496
REMARK 3 L13: -0.1825 L23: 0.3305
REMARK 3 S TENSOR
REMARK 3 S11: 0.0333 S12: 0.0660 S13: 0.0350
REMARK 3 S21: -0.0309 S22: -0.0056 S23: 0.0939
REMARK 3 S31: 0.1051 S32: -0.2115 S33: -0.0276
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 : B 186 B 198
REMARK 3 ORIGIN FOR THE GROUP (A): 28.1980 -6.5665 61.7177
REMARK 3 T TENSOR
REMARK 3 T11: 0.5227 T22: 0.5614
REMARK 3 T33: 0.4886 T12: -0.0055
REMARK 3 T13: 0.1351 T23: 0.0720
REMARK 3 L TENSOR
REMARK 3 L11: 17.5616 L22: 13.7270
REMARK 3 L33: 6.4112 L12: -15.2731
REMARK 3 L13: -10.5632 L23: 9.0270
REMARK 3 S TENSOR
REMARK 3 S11: -1.5313 S12: -0.6580 S13: -2.4402
REMARK 3 S21: 1.3644 S22: 0.0719 S23: 2.0842
REMARK 3 S31: 0.8814 S32: 0.5659 S33: 1.4594
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 : B 199 B 304
REMARK 3 ORIGIN FOR THE GROUP (A): 14.0616 -10.4804 55.5260
REMARK 3 T TENSOR
REMARK 3 T11: 0.1375 T22: 0.1294
REMARK 3 T33: 0.0161 T12: -0.0262
REMARK 3 T13: -0.0228 T23: -0.0299
REMARK 3 L TENSOR
REMARK 3 L11: 0.5980 L22: 1.2215
REMARK 3 L33: 1.4423 L12: 0.1477
REMARK 3 L13: -0.1250 L23: 0.1446
REMARK 3 S TENSOR
REMARK 3 S11: 0.0155 S12: -0.0213 S13: -0.0162
REMARK 3 S21: 0.0597 S22: 0.0200 S23: 0.0205
REMARK 3 S31: 0.3297 S32: -0.1668 S33: -0.0355
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 : C 4 C 29
REMARK 3 ORIGIN FOR THE GROUP (A): 49.5639 18.7839 35.3913
REMARK 3 T TENSOR
REMARK 3 T11: 0.2732 T22: 0.3654
REMARK 3 T33: 0.3177 T12: 0.0462
REMARK 3 T13: 0.0881 T23: -0.1237
REMARK 3 L TENSOR
REMARK 3 L11: 4.6288 L22: 2.7611
REMARK 3 L33: 5.5986 L12: -0.6556
REMARK 3 L13: -0.6064 L23: 1.1947
REMARK 3 S TENSOR
REMARK 3 S11: 0.0658 S12: 0.1297 S13: -0.4956
REMARK 3 S21: -0.5502 S22: 0.1425 S23: -0.7135
REMARK 3 S31: -0.0255 S32: 0.4885 S33: -0.2083
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 : C 30 C 72
REMARK 3 ORIGIN FOR THE GROUP (A): 38.7052 19.6915 38.0152
REMARK 3 T TENSOR
REMARK 3 T11: 0.1467 T22: 0.1421
REMARK 3 T33: 0.0519 T12: -0.0107
REMARK 3 T13: -0.0064 T23: -0.0586
REMARK 3 L TENSOR
REMARK 3 L11: 0.7609 L22: 3.2642
REMARK 3 L33: 4.7642 L12: 0.0486
REMARK 3 L13: -0.3616 L23: 0.7984
REMARK 3 S TENSOR
REMARK 3 S11: 0.0709 S12: 0.1445 S13: -0.1477
REMARK 3 S21: -0.4113 S22: 0.1300 S23: -0.1349
REMARK 3 S31: -0.0307 S32: 0.0054 S33: -0.2008
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 : C 73 C 242
REMARK 3 ORIGIN FOR THE GROUP (A): 40.3946 32.1824 47.3301
REMARK 3 T TENSOR
REMARK 3 T11: 0.1818 T22: 0.1042
REMARK 3 T33: 0.0229 T12: -0.0400
REMARK 3 T13: 0.0196 T23: -0.0460
REMARK 3 L TENSOR
REMARK 3 L11: 0.3955 L22: 1.0417
REMARK 3 L33: 1.7149 L12: -0.1294
REMARK 3 L13: 0.0988 L23: 0.9033
REMARK 3 S TENSOR
REMARK 3 S11: -0.0465 S12: 0.0895 S13: -0.0329
REMARK 3 S21: -0.3147 S22: 0.1082 S23: -0.0814
REMARK 3 S31: -0.4006 S32: 0.1292 S33: -0.0618
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 : C 243 C 289
REMARK 3 ORIGIN FOR THE GROUP (A): 24.4983 30.7558 43.6114
REMARK 3 T TENSOR
REMARK 3 T11: 0.2431 T22: 0.2294
REMARK 3 T33: 0.1014 T12: 0.0591
REMARK 3 T13: -0.0773 T23: -0.0376
REMARK 3 L TENSOR
REMARK 3 L11: 1.6233 L22: 1.5364
REMARK 3 L33: 3.1776 L12: -0.8395
REMARK 3 L13: 0.2121 L23: 0.2701
REMARK 3 S TENSOR
REMARK 3 S11: 0.0665 S12: 0.0273 S13: -0.1094
REMARK 3 S21: -0.1638 S22: -0.0724 S23: 0.3323
REMARK 3 S31: -0.4833 S32: -0.4143 S33: 0.0059
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 : C 290 C 304
REMARK 3 ORIGIN FOR THE GROUP (A): 24.0700 20.7205 34.6121
REMARK 3 T TENSOR
REMARK 3 T11: 0.1215 T22: 0.1140
REMARK 3 T33: 0.0864 T12: 0.0245
REMARK 3 T13: -0.0693 T23: -0.0667
REMARK 3 L TENSOR
REMARK 3 L11: 8.8823 L22: 8.1526
REMARK 3 L33: 21.3703 L12: -2.5953
REMARK 3 L13: 4.8863 L23: -6.3467
REMARK 3 S TENSOR
REMARK 3 S11: -0.0550 S12: 0.1050 S13: -0.2265
REMARK 3 S21: -0.4926 S22: 0.2550 S23: 0.3795
REMARK 3 S31: -0.2897 S32: -0.5405 S33: -0.2000
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 : D 4 D 14
REMARK 3 ORIGIN FOR THE GROUP (A): 23.3873 28.8001 97.7793
REMARK 3 T TENSOR
REMARK 3 T11: 0.5116 T22: 0.4544
REMARK 3 T33: 0.6342 T12: -0.1214
REMARK 3 T13: -0.1717 T23: 0.0545
REMARK 3 L TENSOR
REMARK 3 L11: 14.8227 L22: 6.7053
REMARK 3 L33: 9.9366 L12: -7.0097
REMARK 3 L13: 11.6844 L23: -4.3473
REMARK 3 S TENSOR
REMARK 3 S11: -0.0542 S12: 0.1745 S13: -0.7983
REMARK 3 S21: 0.1769 S22: 0.4942 S23: -0.2056
REMARK 3 S31: -0.3080 S32: 0.5204 S33: -0.4400
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 : D 15 D 79
REMARK 3 ORIGIN FOR THE GROUP (A): 18.3174 20.4932 97.1967
REMARK 3 T TENSOR
REMARK 3 T11: 0.1361 T22: 0.1416
REMARK 3 T33: 0.0520 T12: 0.0611
REMARK 3 T13: -0.0315 T23: -0.0510
REMARK 3 L TENSOR
REMARK 3 L11: 1.5643 L22: 1.3412
REMARK 3 L33: 3.7597 L12: -0.4171
REMARK 3 L13: 0.3203 L23: 0.0733
REMARK 3 S TENSOR
REMARK 3 S11: 0.0176 S12: -0.1167 S13: 0.2130
REMARK 3 S21: 0.2417 S22: 0.0522 S23: -0.1881
REMARK 3 S31: -0.0134 S32: 0.2398 S33: -0.0699
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 : D 80 D 182
REMARK 3 ORIGIN FOR THE GROUP (A): 15.7522 6.9418 89.7262
REMARK 3 T TENSOR
REMARK 3 T11: 0.3024 T22: 0.1194
REMARK 3 T33: 0.0284 T12: 0.1052
REMARK 3 T13: -0.0100 T23: -0.0403
REMARK 3 L TENSOR
REMARK 3 L11: 0.8227 L22: 0.8795
REMARK 3 L33: 1.9969 L12: 0.2738
REMARK 3 L13: -0.4325 L23: 0.9892
REMARK 3 S TENSOR
REMARK 3 S11: -0.0969 S12: -0.0863 S13: -0.0573
REMARK 3 S21: 0.3276 S22: 0.0631 S23: -0.0540
REMARK 3 S31: 0.6272 S32: 0.1033 S33: 0.0338
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 : D 183 D 243
REMARK 3 ORIGIN FOR THE GROUP (A): 16.3277 12.4359 84.4455
REMARK 3 T TENSOR
REMARK 3 T11: 0.1276 T22: 0.0915
REMARK 3 T33: 0.0396 T12: 0.0657
REMARK 3 T13: -0.0179 T23: -0.0415
REMARK 3 L TENSOR
REMARK 3 L11: 0.3628 L22: 1.1188
REMARK 3 L33: 2.8689 L12: -0.4879
REMARK 3 L13: -0.2298 L23: -0.0783
REMARK 3 S TENSOR
REMARK 3 S11: -0.0398 S12: -0.0454 S13: 0.0738
REMARK 3 S21: 0.0750 S22: 0.0802 S23: -0.0402
REMARK 3 S31: 0.4076 S32: 0.0850 S33: -0.0404
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 : D 244 D 289
REMARK 3 ORIGIN FOR THE GROUP (A): 0.2744 10.7185 90.7742
REMARK 3 T TENSOR
REMARK 3 T11: 0.3007 T22: 0.3143
REMARK 3 T33: 0.1571 T12: -0.0230
REMARK 3 T13: 0.0308 T23: -0.0319
REMARK 3 L TENSOR
REMARK 3 L11: 1.1336 L22: 1.4470
REMARK 3 L33: 3.4389 L12: 0.9814
REMARK 3 L13: 0.2562 L23: 0.6572
REMARK 3 S TENSOR
REMARK 3 S11: 0.0775 S12: 0.0164 S13: 0.2053
REMARK 3 S21: 0.1316 S22: -0.0442 S23: 0.3927
REMARK 3 S31: 0.6362 S32: -0.4765 S33: -0.0333
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 : D 290 D 304
REMARK 3 ORIGIN FOR THE GROUP (A): -0.2447 20.4873 100.1924
REMARK 3 T TENSOR
REMARK 3 T11: 0.0895 T22: 0.1629
REMARK 3 T33: 0.0802 T12: 0.0577
REMARK 3 T13: 0.0410 T23: -0.0408
REMARK 3 L TENSOR
REMARK 3 L11: 4.9694 L22: 7.6688
REMARK 3 L33: 20.2713 L12: 1.7518
REMARK 3 L13: -1.7145 L23: -4.8538
REMARK 3 S TENSOR
REMARK 3 S11: -0.0189 S12: -0.0413 S13: 0.1181
REMARK 3 S21: 0.6165 S22: 0.3460 S23: 0.5630
REMARK 3 S31: -0.4537 S32: -0.8889 S33: -0.3271
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : 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 4NVR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-DEC-13.
REMARK 100 THE RCSB ID CODE IS RCSB083716.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-JUN-09
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-F
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97872
REMARK 200 MONOCHROMATOR : DIAMOND
REMARK 200 OPTICS : BERYLLIUM LENSES
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 53580
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.220
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 200 DATA REDUNDANCY : 5.800
REMARK 200 R MERGE (I) : 0.12000
REMARK 200 R SYM (I) : 0.12000
REMARK 200 FOR THE DATA SET : 19.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.22
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.26
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.3
REMARK 200 DATA REDUNDANCY IN SHELL : 4.90
REMARK 200 R MERGE FOR SHELL (I) : 0.45800
REMARK 200 R SYM FOR SHELL (I) : 0.45800
REMARK 200 FOR SHELL : 3.600
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 (%): 40.18
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.06
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN: 8.8MG/ML, 0.3M SODIUM
REMARK 280 CLORIDE, 0.1M HEPES, PH 7.5. SCREEN: 0.2M CALCIUM ACETATE, 0.1M
REMARK 280 NA CACODYLATE, PH 6.5, 9% (W/V) PEG 8000, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2400 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21780 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -64.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: 2
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: 2330 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21810 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -50.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 SER A -2
REMARK 465 ASN A -1
REMARK 465 ALA A 0
REMARK 465 MSE A 1
REMARK 465 SER A 2
REMARK 465 SER B -2
REMARK 465 ASN B -1
REMARK 465 ALA B 0
REMARK 465 MSE B 1
REMARK 465 SER B 2
REMARK 465 SER C -2
REMARK 465 ASN C -1
REMARK 465 ALA C 0
REMARK 465 MSE C 1
REMARK 465 SER C 2
REMARK 465 THR C 3
REMARK 465 SER D -2
REMARK 465 ASN D -1
REMARK 465 ALA D 0
REMARK 465 MSE D 1
REMARK 465 SER D 2
REMARK 465 THR D 3
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 GLU A 268 OE1 - CD - OE2 ANGL. DEV. = 9.1 DEGREES
REMARK 500 GLU B 268 OE1 - CD - OE2 ANGL. DEV. = 9.9 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 PRO A 47 31.63 -97.07
REMARK 500 SER A 82 -163.04 -105.50
REMARK 500 SER A 108 -75.44 -105.92
REMARK 500 ASP A 116 -125.31 58.76
REMARK 500 ASP A 179 82.11 -162.40
REMARK 500 LEU A 192 -73.57 -88.18
REMARK 500 ILE A 194 94.71 -170.82
REMARK 500 GLU A 195 98.42 12.83
REMARK 500 THR A 228 -86.86 -134.82
REMARK 500 PRO B 47 40.13 -98.40
REMARK 500 SER B 108 -84.66 -97.05
REMARK 500 ASP B 116 -124.57 59.10
REMARK 500 ASP B 179 84.56 -158.87
REMARK 500 LEU B 192 -65.59 -98.78
REMARK 500 LYS B 193 27.77 42.77
REMARK 500 GLU B 195 90.34 3.70
REMARK 500 THR B 228 -90.42 -137.76
REMARK 500 CYS B 280 -176.94 -172.25
REMARK 500 HIS C 44 -178.94 -65.21
REMARK 500 SER C 108 -100.45 -104.51
REMARK 500 ASP C 116 -125.32 57.75
REMARK 500 ASP C 179 85.30 -161.09
REMARK 500 THR C 228 -97.34 -128.26
REMARK 500 HIS D 44 -178.52 -69.31
REMARK 500 ASN D 49 -167.58 -124.02
REMARK 500 SER D 108 -87.84 -75.87
REMARK 500 ASP D 116 -131.36 52.26
REMARK 500 ASP D 179 89.73 -174.52
REMARK 500 THR D 228 -89.72 -131.07
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 401 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 268 OE2
REMARK 620 2 GLU B 268 OE1 60.6
REMARK 620 3 THR B 238 O 105.4 131.9
REMARK 620 4 THR B 238 OG1 139.0 144.8 77.6
REMARK 620 5 HOH B 654 O 71.1 128.4 76.3 70.1
REMARK 620 6 HOH B 586 O 141.2 81.7 92.4 77.8 147.5
REMARK 620 7 HOH B 644 O 80.4 71.5 60.6 130.7 118.7 79.0
REMARK 620 8 HOH B 652 O 93.0 80.5 147.5 71.0 85.0 89.4 150.8
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 401 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 268 OE1
REMARK 620 2 GLU A 268 OE2 60.2
REMARK 620 3 THR A 238 O 131.3 104.3
REMARK 620 4 THR A 238 OG1 150.2 141.6 71.2
REMARK 620 5 HOH A 633 O 81.6 138.6 88.5 79.8
REMARK 620 6 HOH A 631 O 122.0 65.6 80.0 76.1 155.5
REMARK 620 7 HOH A 632 O 80.0 89.9 148.7 80.3 99.2 80.8
REMARK 620 8 HOH A 598 O 70.9 81.0 60.8 123.5 71.2 119.7 150.2
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 402 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 205 OE2
REMARK 620 2 ASN C 49 OD1 83.5
REMARK 620 3 HOH C 554 O 116.5 77.0
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 401 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER D 189 O
REMARK 620 2 LEU D 192 O 86.9
REMARK 620 3 HOH D 610 O 77.0 85.2
REMARK 620 4 HOH D 573 O 86.9 86.3 162.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 401 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LEU C 192 O
REMARK 620 2 SER C 189 O 85.7
REMARK 620 3 HOH C 516 O 92.0 79.7
REMARK 620 4 HOH C 632 O 84.0 76.2 155.8
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 CA A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: CSGID-IDP01787 RELATED DB: TARGETTRACK
DBREF 4NVR A 1 304 UNP Q8ZRI7 Q8ZRI7_SALTY 1 304
DBREF 4NVR B 1 304 UNP Q8ZRI7 Q8ZRI7_SALTY 1 304
DBREF 4NVR C 1 304 UNP Q8ZRI7 Q8ZRI7_SALTY 1 304
DBREF 4NVR D 1 304 UNP Q8ZRI7 Q8ZRI7_SALTY 1 304
SEQADV 4NVR SER A -2 UNP Q8ZRI7 EXPRESSION TAG
SEQADV 4NVR ASN A -1 UNP Q8ZRI7 EXPRESSION TAG
SEQADV 4NVR ALA A 0 UNP Q8ZRI7 EXPRESSION TAG
SEQADV 4NVR SER B -2 UNP Q8ZRI7 EXPRESSION TAG
SEQADV 4NVR ASN B -1 UNP Q8ZRI7 EXPRESSION TAG
SEQADV 4NVR ALA B 0 UNP Q8ZRI7 EXPRESSION TAG
SEQADV 4NVR SER C -2 UNP Q8ZRI7 EXPRESSION TAG
SEQADV 4NVR ASN C -1 UNP Q8ZRI7 EXPRESSION TAG
SEQADV 4NVR ALA C 0 UNP Q8ZRI7 EXPRESSION TAG
SEQADV 4NVR SER D -2 UNP Q8ZRI7 EXPRESSION TAG
SEQADV 4NVR ASN D -1 UNP Q8ZRI7 EXPRESSION TAG
SEQADV 4NVR ALA D 0 UNP Q8ZRI7 EXPRESSION TAG
SEQRES 1 A 307 SER ASN ALA MSE SER THR LEU ILE GLU CYS GLY ALA SER
SEQRES 2 A 307 PRO PHE ILE PRO GLY PHE ALA LEU LYS ASP VAL ARG LEU
SEQRES 3 A 307 GLU ASN GLY LEU THR VAL ARG VAL ALA ILE GLY GLY SER
SEQRES 4 A 307 GLY SER PRO LEU VAL LEU LEU HIS GLY HIS PRO GLN ASN
SEQRES 5 A 307 HIS THR THR TRP ARG LYS VAL ALA PRO THR LEU ALA GLN
SEQRES 6 A 307 ASN HIS THR VAL ILE LEU PRO ASP LEU ARG GLY TYR GLY
SEQRES 7 A 307 ASP SER ASP LYS PRO THR SER ASP PRO ALA HIS ARG THR
SEQRES 8 A 307 TYR SER LYS ARG THR MSE ALA GLN ASP ILE VAL MSE LEU
SEQRES 9 A 307 MSE ASP ALA LEU GLY PHE SER ARG PHE ALA PHE VAL GLY
SEQRES 10 A 307 HIS ASP ARG GLY GLY ARG VAL GLY HIS ARG LEU ALA LEU
SEQRES 11 A 307 ASP TYR PRO ASP ARG VAL THR CYS CYS THR PHE ILE ASP
SEQRES 12 A 307 ILE ALA PRO THR ALA THR MSE TYR ALA LEU THR ASP LYS
SEQRES 13 A 307 SER PHE ALA THR ARG TYR PHE TRP TRP PHE PHE LEU ILE
SEQRES 14 A 307 GLN PRO PHE PRO LEU PRO GLU THR MSE ILE ALA HIS ASP
SEQRES 15 A 307 PRO ALA PHE PHE LEU ARG LYS HIS ILE SER GLY GLN LEU
SEQRES 16 A 307 LYS ILE GLU GLY ALA THR SER GLN GLU ALA PHE ASN GLU
SEQRES 17 A 307 TYR LEU ARG CYS TYR GLN ASN PRO GLU MSE ILE HIS ALA
SEQRES 18 A 307 ILE CYS GLU ASP TYR ARG ALA ALA ALA THR ILE ASP LEU
SEQRES 19 A 307 ASP ASP ASP ALA ALA ASP THR SER ALA ARG ILE ARG CYS
SEQRES 20 A 307 PRO LEU GLN LEU LEU TRP GLY GLY LEU GLY THR VAL GLY
SEQRES 21 A 307 GLN LEU TYR ASN VAL VAL GLY THR TRP LYS GLU LYS ALA
SEQRES 22 A 307 LEU ASN VAL GLN GLY GLU ALA LEU PRO CYS GLY HIS SER
SEQRES 23 A 307 PRO GLN GLU GLU CYS PRO GLU TYR PHE ILE GLN LYS LEU
SEQRES 24 A 307 GLN SER PHE LEU HIS SER VAL LEU
SEQRES 1 B 307 SER ASN ALA MSE SER THR LEU ILE GLU CYS GLY ALA SER
SEQRES 2 B 307 PRO PHE ILE PRO GLY PHE ALA LEU LYS ASP VAL ARG LEU
SEQRES 3 B 307 GLU ASN GLY LEU THR VAL ARG VAL ALA ILE GLY GLY SER
SEQRES 4 B 307 GLY SER PRO LEU VAL LEU LEU HIS GLY HIS PRO GLN ASN
SEQRES 5 B 307 HIS THR THR TRP ARG LYS VAL ALA PRO THR LEU ALA GLN
SEQRES 6 B 307 ASN HIS THR VAL ILE LEU PRO ASP LEU ARG GLY TYR GLY
SEQRES 7 B 307 ASP SER ASP LYS PRO THR SER ASP PRO ALA HIS ARG THR
SEQRES 8 B 307 TYR SER LYS ARG THR MSE ALA GLN ASP ILE VAL MSE LEU
SEQRES 9 B 307 MSE ASP ALA LEU GLY PHE SER ARG PHE ALA PHE VAL GLY
SEQRES 10 B 307 HIS ASP ARG GLY GLY ARG VAL GLY HIS ARG LEU ALA LEU
SEQRES 11 B 307 ASP TYR PRO ASP ARG VAL THR CYS CYS THR PHE ILE ASP
SEQRES 12 B 307 ILE ALA PRO THR ALA THR MSE TYR ALA LEU THR ASP LYS
SEQRES 13 B 307 SER PHE ALA THR ARG TYR PHE TRP TRP PHE PHE LEU ILE
SEQRES 14 B 307 GLN PRO PHE PRO LEU PRO GLU THR MSE ILE ALA HIS ASP
SEQRES 15 B 307 PRO ALA PHE PHE LEU ARG LYS HIS ILE SER GLY GLN LEU
SEQRES 16 B 307 LYS ILE GLU GLY ALA THR SER GLN GLU ALA PHE ASN GLU
SEQRES 17 B 307 TYR LEU ARG CYS TYR GLN ASN PRO GLU MSE ILE HIS ALA
SEQRES 18 B 307 ILE CYS GLU ASP TYR ARG ALA ALA ALA THR ILE ASP LEU
SEQRES 19 B 307 ASP ASP ASP ALA ALA ASP THR SER ALA ARG ILE ARG CYS
SEQRES 20 B 307 PRO LEU GLN LEU LEU TRP GLY GLY LEU GLY THR VAL GLY
SEQRES 21 B 307 GLN LEU TYR ASN VAL VAL GLY THR TRP LYS GLU LYS ALA
SEQRES 22 B 307 LEU ASN VAL GLN GLY GLU ALA LEU PRO CYS GLY HIS SER
SEQRES 23 B 307 PRO GLN GLU GLU CYS PRO GLU TYR PHE ILE GLN LYS LEU
SEQRES 24 B 307 GLN SER PHE LEU HIS SER VAL LEU
SEQRES 1 C 307 SER ASN ALA MSE SER THR LEU ILE GLU CYS GLY ALA SER
SEQRES 2 C 307 PRO PHE ILE PRO GLY PHE ALA LEU LYS ASP VAL ARG LEU
SEQRES 3 C 307 GLU ASN GLY LEU THR VAL ARG VAL ALA ILE GLY GLY SER
SEQRES 4 C 307 GLY SER PRO LEU VAL LEU LEU HIS GLY HIS PRO GLN ASN
SEQRES 5 C 307 HIS THR THR TRP ARG LYS VAL ALA PRO THR LEU ALA GLN
SEQRES 6 C 307 ASN HIS THR VAL ILE LEU PRO ASP LEU ARG GLY TYR GLY
SEQRES 7 C 307 ASP SER ASP LYS PRO THR SER ASP PRO ALA HIS ARG THR
SEQRES 8 C 307 TYR SER LYS ARG THR MSE ALA GLN ASP ILE VAL MSE LEU
SEQRES 9 C 307 MSE ASP ALA LEU GLY PHE SER ARG PHE ALA PHE VAL GLY
SEQRES 10 C 307 HIS ASP ARG GLY GLY ARG VAL GLY HIS ARG LEU ALA LEU
SEQRES 11 C 307 ASP TYR PRO ASP ARG VAL THR CYS CYS THR PHE ILE ASP
SEQRES 12 C 307 ILE ALA PRO THR ALA THR MSE TYR ALA LEU THR ASP LYS
SEQRES 13 C 307 SER PHE ALA THR ARG TYR PHE TRP TRP PHE PHE LEU ILE
SEQRES 14 C 307 GLN PRO PHE PRO LEU PRO GLU THR MSE ILE ALA HIS ASP
SEQRES 15 C 307 PRO ALA PHE PHE LEU ARG LYS HIS ILE SER GLY GLN LEU
SEQRES 16 C 307 LYS ILE GLU GLY ALA THR SER GLN GLU ALA PHE ASN GLU
SEQRES 17 C 307 TYR LEU ARG CYS TYR GLN ASN PRO GLU MSE ILE HIS ALA
SEQRES 18 C 307 ILE CYS GLU ASP TYR ARG ALA ALA ALA THR ILE ASP LEU
SEQRES 19 C 307 ASP ASP ASP ALA ALA ASP THR SER ALA ARG ILE ARG CYS
SEQRES 20 C 307 PRO LEU GLN LEU LEU TRP GLY GLY LEU GLY THR VAL GLY
SEQRES 21 C 307 GLN LEU TYR ASN VAL VAL GLY THR TRP LYS GLU LYS ALA
SEQRES 22 C 307 LEU ASN VAL GLN GLY GLU ALA LEU PRO CYS GLY HIS SER
SEQRES 23 C 307 PRO GLN GLU GLU CYS PRO GLU TYR PHE ILE GLN LYS LEU
SEQRES 24 C 307 GLN SER PHE LEU HIS SER VAL LEU
SEQRES 1 D 307 SER ASN ALA MSE SER THR LEU ILE GLU CYS GLY ALA SER
SEQRES 2 D 307 PRO PHE ILE PRO GLY PHE ALA LEU LYS ASP VAL ARG LEU
SEQRES 3 D 307 GLU ASN GLY LEU THR VAL ARG VAL ALA ILE GLY GLY SER
SEQRES 4 D 307 GLY SER PRO LEU VAL LEU LEU HIS GLY HIS PRO GLN ASN
SEQRES 5 D 307 HIS THR THR TRP ARG LYS VAL ALA PRO THR LEU ALA GLN
SEQRES 6 D 307 ASN HIS THR VAL ILE LEU PRO ASP LEU ARG GLY TYR GLY
SEQRES 7 D 307 ASP SER ASP LYS PRO THR SER ASP PRO ALA HIS ARG THR
SEQRES 8 D 307 TYR SER LYS ARG THR MSE ALA GLN ASP ILE VAL MSE LEU
SEQRES 9 D 307 MSE ASP ALA LEU GLY PHE SER ARG PHE ALA PHE VAL GLY
SEQRES 10 D 307 HIS ASP ARG GLY GLY ARG VAL GLY HIS ARG LEU ALA LEU
SEQRES 11 D 307 ASP TYR PRO ASP ARG VAL THR CYS CYS THR PHE ILE ASP
SEQRES 12 D 307 ILE ALA PRO THR ALA THR MSE TYR ALA LEU THR ASP LYS
SEQRES 13 D 307 SER PHE ALA THR ARG TYR PHE TRP TRP PHE PHE LEU ILE
SEQRES 14 D 307 GLN PRO PHE PRO LEU PRO GLU THR MSE ILE ALA HIS ASP
SEQRES 15 D 307 PRO ALA PHE PHE LEU ARG LYS HIS ILE SER GLY GLN LEU
SEQRES 16 D 307 LYS ILE GLU GLY ALA THR SER GLN GLU ALA PHE ASN GLU
SEQRES 17 D 307 TYR LEU ARG CYS TYR GLN ASN PRO GLU MSE ILE HIS ALA
SEQRES 18 D 307 ILE CYS GLU ASP TYR ARG ALA ALA ALA THR ILE ASP LEU
SEQRES 19 D 307 ASP ASP ASP ALA ALA ASP THR SER ALA ARG ILE ARG CYS
SEQRES 20 D 307 PRO LEU GLN LEU LEU TRP GLY GLY LEU GLY THR VAL GLY
SEQRES 21 D 307 GLN LEU TYR ASN VAL VAL GLY THR TRP LYS GLU LYS ALA
SEQRES 22 D 307 LEU ASN VAL GLN GLY GLU ALA LEU PRO CYS GLY HIS SER
SEQRES 23 D 307 PRO GLN GLU GLU CYS PRO GLU TYR PHE ILE GLN LYS LEU
SEQRES 24 D 307 GLN SER PHE LEU HIS SER VAL LEU
MODRES 4NVR MSE A 94 MET SELENOMETHIONINE
MODRES 4NVR MSE A 100 MET SELENOMETHIONINE
MODRES 4NVR MSE A 102 MET SELENOMETHIONINE
MODRES 4NVR MSE A 147 MET SELENOMETHIONINE
MODRES 4NVR MSE A 175 MET SELENOMETHIONINE
MODRES 4NVR MSE A 215 MET SELENOMETHIONINE
MODRES 4NVR MSE B 94 MET SELENOMETHIONINE
MODRES 4NVR MSE B 100 MET SELENOMETHIONINE
MODRES 4NVR MSE B 102 MET SELENOMETHIONINE
MODRES 4NVR MSE B 147 MET SELENOMETHIONINE
MODRES 4NVR MSE B 175 MET SELENOMETHIONINE
MODRES 4NVR MSE B 215 MET SELENOMETHIONINE
MODRES 4NVR MSE C 94 MET SELENOMETHIONINE
MODRES 4NVR MSE C 100 MET SELENOMETHIONINE
MODRES 4NVR MSE C 102 MET SELENOMETHIONINE
MODRES 4NVR MSE C 147 MET SELENOMETHIONINE
MODRES 4NVR MSE C 175 MET SELENOMETHIONINE
MODRES 4NVR MSE C 215 MET SELENOMETHIONINE
MODRES 4NVR MSE D 94 MET SELENOMETHIONINE
MODRES 4NVR MSE D 100 MET SELENOMETHIONINE
MODRES 4NVR MSE D 102 MET SELENOMETHIONINE
MODRES 4NVR MSE D 147 MET SELENOMETHIONINE
MODRES 4NVR MSE D 175 MET SELENOMETHIONINE
MODRES 4NVR MSE D 215 MET SELENOMETHIONINE
HET MSE A 94 8
HET MSE A 100 8
HET MSE A 102 8
HET MSE A 147 8
HET MSE A 175 8
HET MSE A 215 8
HET MSE B 94 8
HET MSE B 100 8
HET MSE B 102 8
HET MSE B 147 8
HET MSE B 175 8
HET MSE B 215 8
HET MSE C 94 8
HET MSE C 100 8
HET MSE C 102 8
HET MSE C 147 8
HET MSE C 175 8
HET MSE C 215 8
HET MSE D 94 8
HET MSE D 100 8
HET MSE D 102 8
HET MSE D 147 8
HET MSE D 175 8
HET MSE D 215 8
HET CA A 401 1
HET CL A 402 1
HET CA B 401 1
HET CL B 402 1
HET CA C 401 1
HET CA C 402 1
HET CA D 401 1
HETNAM MSE SELENOMETHIONINE
HETNAM CA CALCIUM ION
HETNAM CL CHLORIDE ION
FORMUL 1 MSE 24(C5 H11 N O2 SE)
FORMUL 5 CA 5(CA 2+)
FORMUL 6 CL 2(CL 1-)
FORMUL 12 HOH *597(H2 O)
HELIX 1 1 ASN A 49 ARG A 54 5 6
HELIX 2 2 VAL A 56 ALA A 61 1 6
HELIX 3 3 HIS A 86 TYR A 89 5 4
HELIX 4 4 SER A 90 LEU A 105 1 16
HELIX 5 5 ASP A 116 TYR A 129 1 14
HELIX 6 6 PRO A 143 LEU A 150 1 8
HELIX 7 7 ASP A 152 TYR A 159 1 8
HELIX 8 8 PHE A 160 LEU A 165 1 6
HELIX 9 9 PRO A 170 HIS A 178 1 9
HELIX 10 10 ASP A 179 LYS A 193 1 15
HELIX 11 11 SER A 199 GLN A 211 1 13
HELIX 12 12 ASN A 212 ALA A 227 1 16
HELIX 13 13 THR A 228 ASP A 237 1 10
HELIX 14 14 GLY A 254 TYR A 260 1 7
HELIX 15 15 ASN A 261 LYS A 267 1 7
HELIX 16 16 SER A 283 CYS A 288 1 6
HELIX 17 17 CYS A 288 VAL A 303 1 16
HELIX 18 18 ASN B 49 ARG B 54 5 6
HELIX 19 19 VAL B 56 ALA B 61 1 6
HELIX 20 20 HIS B 86 TYR B 89 5 4
HELIX 21 21 SER B 90 LEU B 105 1 16
HELIX 22 22 ASP B 116 TYR B 129 1 14
HELIX 23 23 PRO B 143 LEU B 150 1 8
HELIX 24 24 ASP B 152 TYR B 159 1 8
HELIX 25 25 PHE B 160 LEU B 165 1 6
HELIX 26 26 PRO B 170 ASP B 179 1 10
HELIX 27 27 ASP B 179 LYS B 193 1 15
HELIX 28 28 SER B 199 GLN B 211 1 13
HELIX 29 29 ASN B 212 ALA B 227 1 16
HELIX 30 30 THR B 228 ASP B 237 1 10
HELIX 31 31 GLY B 254 TYR B 260 1 7
HELIX 32 32 VAL B 263 LYS B 267 5 5
HELIX 33 33 SER B 283 CYS B 288 1 6
HELIX 34 34 CYS B 288 VAL B 303 1 16
HELIX 35 35 ASN C 49 ARG C 54 5 6
HELIX 36 36 VAL C 56 ALA C 61 1 6
HELIX 37 37 HIS C 86 TYR C 89 5 4
HELIX 38 38 SER C 90 GLY C 106 1 17
HELIX 39 39 ASP C 116 TYR C 129 1 14
HELIX 40 40 PRO C 143 LEU C 150 1 8
HELIX 41 41 ASP C 152 TYR C 159 1 8
HELIX 42 42 PHE C 160 LEU C 165 1 6
HELIX 43 43 PRO C 170 ASP C 179 1 10
HELIX 44 44 ASP C 179 LEU C 192 1 14
HELIX 45 45 SER C 199 GLN C 211 1 13
HELIX 46 46 ASN C 212 THR C 228 1 17
HELIX 47 47 THR C 228 ASP C 237 1 10
HELIX 48 48 GLY C 254 TYR C 260 1 7
HELIX 49 49 ASN C 261 GLU C 268 1 8
HELIX 50 50 SER C 283 CYS C 288 1 6
HELIX 51 51 CYS C 288 LEU C 304 1 17
HELIX 52 52 ASN D 49 ARG D 54 5 6
HELIX 53 53 VAL D 56 ALA D 61 1 6
HELIX 54 54 HIS D 86 TYR D 89 5 4
HELIX 55 55 SER D 90 LEU D 105 1 16
HELIX 56 56 ASP D 116 TYR D 129 1 14
HELIX 57 57 PRO D 143 LEU D 150 1 8
HELIX 58 58 ASP D 152 TYR D 159 1 8
HELIX 59 59 PHE D 160 LEU D 165 1 6
HELIX 60 60 PRO D 170 HIS D 178 1 9
HELIX 61 61 ASP D 179 LEU D 192 1 14
HELIX 62 62 SER D 199 GLN D 211 1 13
HELIX 63 63 ASN D 212 THR D 228 1 17
HELIX 64 64 THR D 228 ASP D 237 1 10
HELIX 65 65 GLY D 254 TYR D 260 1 7
HELIX 66 66 ASN D 261 GLU D 268 1 8
HELIX 67 67 SER D 283 CYS D 288 1 6
HELIX 68 68 CYS D 288 LEU D 304 1 17
SHEET 1 A 9 LEU A 4 ALA A 9 0
SHEET 2 A 9 ALA A 17 ARG A 22 -1 O LEU A 18 N GLY A 8
SHEET 3 A 9 THR A 28 GLY A 35 -1 O VAL A 31 N LYS A 19
SHEET 4 A 9 THR A 65 PRO A 69 -1 O LEU A 68 N ALA A 32
SHEET 5 A 9 PRO A 39 LEU A 43 1 N LEU A 40 O ILE A 67
SHEET 6 A 9 PHE A 110 HIS A 115 1 O VAL A 113 N VAL A 41
SHEET 7 A 9 VAL A 133 ILE A 139 1 O THR A 137 N GLY A 114
SHEET 8 A 9 LEU A 246 GLY A 251 1 O GLN A 247 N CYS A 136
SHEET 9 A 9 VAL A 273 LEU A 278 1 O LEU A 278 N TRP A 250
SHEET 1 B 9 LEU B 4 ALA B 9 0
SHEET 2 B 9 ALA B 17 ARG B 22 -1 O LEU B 18 N GLY B 8
SHEET 3 B 9 THR B 28 GLY B 35 -1 O VAL B 29 N VAL B 21
SHEET 4 B 9 THR B 65 PRO B 69 -1 O VAL B 66 N GLY B 34
SHEET 5 B 9 PRO B 39 LEU B 43 1 N LEU B 40 O ILE B 67
SHEET 6 B 9 PHE B 110 HIS B 115 1 O VAL B 113 N LEU B 43
SHEET 7 B 9 VAL B 133 ILE B 139 1 O ILE B 139 N GLY B 114
SHEET 8 B 9 LEU B 246 GLY B 251 1 O GLN B 247 N CYS B 136
SHEET 9 B 9 VAL B 273 LEU B 278 1 O LEU B 278 N TRP B 250
SHEET 1 C 9 ILE C 5 ALA C 9 0
SHEET 2 C 9 ALA C 17 ARG C 22 -1 O LEU C 18 N GLY C 8
SHEET 3 C 9 THR C 28 GLY C 35 -1 O VAL C 31 N LYS C 19
SHEET 4 C 9 HIS C 64 PRO C 69 -1 O LEU C 68 N ALA C 32
SHEET 5 C 9 SER C 38 LEU C 43 1 N LEU C 40 O THR C 65
SHEET 6 C 9 PHE C 110 HIS C 115 1 O VAL C 113 N LEU C 43
SHEET 7 C 9 VAL C 133 ILE C 139 1 O ILE C 139 N GLY C 114
SHEET 8 C 9 LEU C 246 GLY C 251 1 O GLN C 247 N PHE C 138
SHEET 9 C 9 VAL C 273 LEU C 278 1 O LEU C 278 N TRP C 250
SHEET 1 D 9 ILE D 5 ALA D 9 0
SHEET 2 D 9 ALA D 17 ARG D 22 -1 O LEU D 18 N GLY D 8
SHEET 3 D 9 THR D 28 GLY D 35 -1 O VAL D 29 N VAL D 21
SHEET 4 D 9 HIS D 64 PRO D 69 -1 O VAL D 66 N GLY D 34
SHEET 5 D 9 SER D 38 LEU D 43 1 N LEU D 42 O ILE D 67
SHEET 6 D 9 PHE D 110 HIS D 115 1 O VAL D 113 N LEU D 43
SHEET 7 D 9 VAL D 133 ILE D 139 1 O ILE D 139 N GLY D 114
SHEET 8 D 9 LEU D 246 GLY D 251 1 O GLN D 247 N PHE D 138
SHEET 9 D 9 VAL D 273 LEU D 278 1 O LEU D 278 N TRP D 250
LINK C THR A 93 N MSE A 94 1555 1555 1.33
LINK C MSE A 94 N ALA A 95 1555 1555 1.34
LINK C VAL A 99 N MSE A 100 1555 1555 1.33
LINK C MSE A 100 N LEU A 101 1555 1555 1.34
LINK C LEU A 101 N MSE A 102 1555 1555 1.33
LINK C MSE A 102 N ASP A 103 1555 1555 1.34
LINK C THR A 146 N MSE A 147 1555 1555 1.32
LINK C MSE A 147 N TYR A 148 1555 1555 1.33
LINK C THR A 174 N MSE A 175 1555 1555 1.32
LINK C MSE A 175 N ILE A 176 1555 1555 1.34
LINK C GLU A 214 N MSE A 215 1555 1555 1.34
LINK C MSE A 215 N AILE A 216 1555 1555 1.33
LINK C MSE A 215 N BILE A 216 1555 1555 1.33
LINK C THR B 93 N MSE B 94 1555 1555 1.33
LINK C MSE B 94 N ALA B 95 1555 1555 1.33
LINK C VAL B 99 N MSE B 100 1555 1555 1.34
LINK C MSE B 100 N LEU B 101 1555 1555 1.34
LINK C LEU B 101 N MSE B 102 1555 1555 1.34
LINK C MSE B 102 N ASP B 103 1555 1555 1.33
LINK C THR B 146 N MSE B 147 1555 1555 1.33
LINK C MSE B 147 N TYR B 148 1555 1555 1.34
LINK C THR B 174 N MSE B 175 1555 1555 1.32
LINK C MSE B 175 N ILE B 176 1555 1555 1.33
LINK C GLU B 214 N MSE B 215 1555 1555 1.34
LINK C MSE B 215 N ILE B 216 1555 1555 1.32
LINK C THR C 93 N MSE C 94 1555 1555 1.32
LINK C MSE C 94 N ALA C 95 1555 1555 1.33
LINK C VAL C 99 N MSE C 100 1555 1555 1.33
LINK C MSE C 100 N LEU C 101 1555 1555 1.32
LINK C LEU C 101 N MSE C 102 1555 1555 1.34
LINK C MSE C 102 N ASP C 103 1555 1555 1.33
LINK C THR C 146 N MSE C 147 1555 1555 1.34
LINK C MSE C 147 N TYR C 148 1555 1555 1.33
LINK C THR C 174 N MSE C 175 1555 1555 1.32
LINK C MSE C 175 N ILE C 176 1555 1555 1.33
LINK C GLU C 214 N MSE C 215 1555 1555 1.34
LINK C MSE C 215 N AILE C 216 1555 1555 1.32
LINK C MSE C 215 N BILE C 216 1555 1555 1.33
LINK C THR D 93 N MSE D 94 1555 1555 1.33
LINK C MSE D 94 N ALA D 95 1555 1555 1.33
LINK C VAL D 99 N MSE D 100 1555 1555 1.33
LINK C MSE D 100 N LEU D 101 1555 1555 1.32
LINK C LEU D 101 N MSE D 102 1555 1555 1.33
LINK C MSE D 102 N ASP D 103 1555 1555 1.34
LINK C THR D 146 N MSE D 147 1555 1555 1.33
LINK C MSE D 147 N TYR D 148 1555 1555 1.34
LINK C THR D 174 N MSE D 175 1555 1555 1.32
LINK C MSE D 175 N ILE D 176 1555 1555 1.34
LINK C GLU D 214 N MSE D 215 1555 1555 1.33
LINK C MSE D 215 N ILE D 216 1555 1555 1.32
LINK OE2 GLU B 268 CA CA B 401 1555 1555 2.26
LINK OE1 GLU B 268 CA CA B 401 1555 1555 2.27
LINK OE1 GLU A 268 CA CA A 401 1555 1555 2.27
LINK OE2 GLU A 268 CA CA A 401 1555 1555 2.27
LINK OE2 GLU C 205 CA CA C 402 1555 1555 2.30
LINK OD1 ASN C 49 CA CA C 402 1555 1555 2.32
LINK O SER D 189 CA CA D 401 1555 1555 2.32
LINK O THR A 238 CA CA A 401 1555 1555 2.32
LINK O THR B 238 CA CA B 401 1555 1555 2.33
LINK O LEU D 192 CA CA D 401 1555 1555 2.33
LINK OG1 THR B 238 CA CA B 401 1555 1555 2.33
LINK O LEU C 192 CA CA C 401 1555 1555 2.33
LINK OG1 THR A 238 CA CA A 401 1555 1555 2.34
LINK O SER C 189 CA CA C 401 1555 1555 2.34
LINK CA CA D 401 O HOH D 610 1555 1555 2.12
LINK CA CA C 401 O HOH C 516 1555 1555 2.24
LINK CA CA A 401 O HOH A 633 1555 1555 2.39
LINK CA CA A 401 O AHOH A 631 1555 1555 2.39
LINK CA CA B 401 O HOH B 654 1555 1555 2.43
LINK CA CA C 401 O HOH C 632 1555 1555 2.44
LINK CA CA A 401 O HOH A 632 1555 1555 2.46
LINK CA CA B 401 O HOH B 586 1555 1555 2.50
LINK CA CA D 401 O HOH D 573 1555 1555 2.50
LINK CA CA A 401 O HOH A 598 1555 1555 2.51
LINK CA CA B 401 O HOH B 644 1555 1555 2.56
LINK CA CA B 401 O HOH B 652 1555 1555 2.59
LINK CA CA C 402 O HOH C 554 1555 1555 2.71
LINK CA CA A 401 O BHOH A 631 1555 1555 3.13
CISPEP 1 HIS A 46 PRO A 47 0 -0.22
CISPEP 2 PHE A 169 PRO A 170 0 2.20
CISPEP 3 HIS B 46 PRO B 47 0 -1.99
CISPEP 4 PHE B 169 PRO B 170 0 2.50
CISPEP 5 HIS C 46 PRO C 47 0 -0.26
CISPEP 6 PHE C 169 PRO C 170 0 0.87
CISPEP 7 HIS D 46 PRO D 47 0 -0.08
CISPEP 8 PHE D 169 PRO D 170 0 -0.05
SITE 1 AC1 6 THR A 238 GLU A 268 HOH A 598 HOH A 631
SITE 2 AC1 6 HOH A 632 HOH A 633
SITE 1 AC2 3 ASP A 116 ARG A 117 ARG A 120
SITE 1 AC3 6 THR B 238 GLU B 268 HOH B 586 HOH B 644
SITE 2 AC3 6 HOH B 652 HOH B 654
SITE 1 AC4 3 ASP B 116 ARG B 117 ARG B 120
SITE 1 AC5 5 SER C 189 LEU C 192 GLU C 195 HOH C 516
SITE 2 AC5 5 HOH C 632
SITE 1 AC6 5 ASN C 49 HIS C 50 THR C 51 GLU C 205
SITE 2 AC6 5 HOH C 554
SITE 1 AC7 4 SER D 189 LEU D 192 HOH D 573 HOH D 610
CRYST1 47.931 71.380 90.327 113.03 92.41 90.09 P 1 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 0.020863 0.000034 0.000968 0.00000
SCALE2 0.000000 0.014010 0.005963 0.00000
SCALE3 0.000000 0.000000 0.012043 0.00000
TER 2459 LEU A 304
TER 4846 LEU B 304
TER 7248 LEU C 304
TER 9616 LEU D 304
MASTER 765 0 31 68 36 0 11 610086 4 278 96
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