LinkDB: 6DZ4
Original site: 6DZ4
Chemical substance (4) PDB-CCD (4) Chemical reaction (1) KEGG ENZYME (1) Gene (2) KEGG GENES (2) Protein sequence (6) UniProt (2) SWISS-PROT (2) PDBSTR (2) Protein domain (11) InterPro (9) PROSITE (2) All databases (24)
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HEADER LYASE/LYASE INHIBITOR 02-JUL-18 6DZ4
TITLE CRYSTAL STRUCTURE OF SALMONELLA TYPHIMURIUM TRYPTOPHAN SYNTHASE WITH
TITLE 2 SODIUM ION AT THE METAL COORDINATION SITE AND (E)-N-({3-HYDROXY-2-
TITLE 3 METHYL-5-[(PHOSPHONOOXY)METHYL]PYRIDIN-4-YL}METHYLIDENE)-L-SERINE AT
TITLE 4 THE BETA-SITE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRYPTOPHAN SYNTHASE ALPHA CHAIN;
COMPND 3 CHAIN: A;
COMPND 4 EC: 4.2.1.20;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: TRYPTOPHAN SYNTHASE BETA CHAIN;
COMPND 8 CHAIN: B;
COMPND 9 EC: 4.2.1.20;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SALMONELLA TYPHIMURIUM (STRAIN LT2 / SGSC1412 /
SOURCE 3 ATCC 700720);
SOURCE 4 ORGANISM_TAXID: 99287;
SOURCE 5 STRAIN: LT2 / SGSC1412 / ATCC 700720;
SOURCE 6 GENE: TRPA, STM1727;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: CB149;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PEBA-10;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: SALMONELLA TYPHIMURIUM (STRAIN LT2 / SGSC1412 /
SOURCE 13 ATCC 700720);
SOURCE 14 ORGANISM_TAXID: 99287;
SOURCE 15 STRAIN: LT2 / SGSC1412 / ATCC 700720;
SOURCE 16 GENE: TRPB, STM1726;
SOURCE 17 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 18 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 19 EXPRESSION_SYSTEM_STRAIN: CB149;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PEBA-10
KEYWDS F9F, LYASE-LYASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR E.HILARIO,M.F.DUNN,L.J.MUELLER,L.FAN
REVDAT 5 11-OCT-23 6DZ4 1 LINK
REVDAT 4 10-JUN-20 6DZ4 1 COMPND KEYWDS REMARK LINK
REVDAT 4 2 1 SITE ATOM
REVDAT 3 06-MAY-20 6DZ4 1 HEADER TITLE COMPND KEYWDS
REVDAT 3 2 1 JRNL REMARK HET HETNAM
REVDAT 3 3 1 HETSYN FORMUL ATOM
REVDAT 2 18-DEC-19 6DZ4 1 REMARK
REVDAT 1 10-JUL-19 6DZ4 0
JRNL AUTH E.HILARIO,M.F.DUNN,L.J.MUELLER,L.FAN
JRNL TITL CRYSTAL STRUCTURE OF SALMONELLA TYPHIMURIUM TRYPTOPHAN
JRNL TITL 2 SYNTHASE WITH SODIUM ION AT THE METAL COORDINATION SITE AND
JRNL TITL 3 (E)-N-({3-HYDROXY-2-METHYL-5-[(PHOSPHONOOXY)
JRNL TITL 4 METHYL]PYRIDIN-4-YL}METHYLIDENE)-L-SERINE AT THE BETA SITE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.45 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0230
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) : 1.45
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.94
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 120118
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) : 0.149
REMARK 3 R VALUE (WORKING SET) : 0.147
REMARK 3 FREE R VALUE : 0.186
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 6241
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) : 1.45
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.49
REMARK 3 REFLECTION IN BIN (WORKING SET) : 8577
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.58
REMARK 3 BIN R VALUE (WORKING SET) : 0.2820
REMARK 3 BIN FREE R VALUE SET COUNT : 509
REMARK 3 BIN FREE R VALUE : 0.3030
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4922
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 80
REMARK 3 SOLVENT ATOMS : 738
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.82
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.41000
REMARK 3 B22 (A**2) : 0.11000
REMARK 3 B33 (A**2) : 0.29000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.05000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.065
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.061
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.045
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.779
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.976
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.963
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5244 ; 0.007 ; 0.012
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7106 ; 1.376 ; 1.644
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 681 ; 6.052 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 259 ;33.401 ;22.124
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 873 ;11.997 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 35 ;18.262 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 691 ; 0.091 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3965 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 5244 ; 1.788 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 463 ;27.023 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 5457 ;13.018 ; 5.000
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 : 13
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 1 A 13
REMARK 3 ORIGIN FOR THE GROUP (A): -59.667 -21.554 25.797
REMARK 3 T TENSOR
REMARK 3 T11: 0.0188 T22: 0.1173
REMARK 3 T33: 0.0993 T12: -0.0100
REMARK 3 T13: -0.0002 T23: -0.0116
REMARK 3 L TENSOR
REMARK 3 L11: 5.3576 L22: 0.3380
REMARK 3 L33: 4.8884 L12: 1.0752
REMARK 3 L13: 1.9769 L23: -0.3153
REMARK 3 S TENSOR
REMARK 3 S11: 0.2396 S12: -0.1172 S13: -0.1456
REMARK 3 S21: 0.0314 S22: 0.0171 S23: 0.0010
REMARK 3 S31: 0.2103 S32: -0.4172 S33: -0.2567
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 14 A 77
REMARK 3 ORIGIN FOR THE GROUP (A): -41.559 -12.160 19.076
REMARK 3 T TENSOR
REMARK 3 T11: 0.0965 T22: 0.0767
REMARK 3 T33: 0.1196 T12: 0.0746
REMARK 3 T13: 0.0666 T23: 0.0163
REMARK 3 L TENSOR
REMARK 3 L11: 0.0564 L22: 0.3270
REMARK 3 L33: 0.9321 L12: -0.0883
REMARK 3 L13: 0.0550 L23: -0.4904
REMARK 3 S TENSOR
REMARK 3 S11: 0.0704 S12: 0.0510 S13: 0.0587
REMARK 3 S21: -0.0630 S22: -0.0683 S23: -0.0514
REMARK 3 S31: -0.0343 S32: 0.0103 S33: -0.0021
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 78 A 159
REMARK 3 ORIGIN FOR THE GROUP (A): -41.664 -24.098 27.570
REMARK 3 T TENSOR
REMARK 3 T11: 0.0539 T22: 0.0809
REMARK 3 T33: 0.0646 T12: -0.0065
REMARK 3 T13: 0.0232 T23: -0.0108
REMARK 3 L TENSOR
REMARK 3 L11: 0.7057 L22: 0.9462
REMARK 3 L33: 0.1983 L12: -0.7184
REMARK 3 L13: -0.2456 L23: 0.3677
REMARK 3 S TENSOR
REMARK 3 S11: 0.0919 S12: 0.0020 S13: 0.0216
REMARK 3 S21: -0.0143 S22: -0.0801 S23: 0.0008
REMARK 3 S31: -0.0016 S32: -0.0406 S33: -0.0118
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 160 A 216
REMARK 3 ORIGIN FOR THE GROUP (A): -52.122 -32.295 13.462
REMARK 3 T TENSOR
REMARK 3 T11: 0.0461 T22: 0.1546
REMARK 3 T33: 0.0781 T12: 0.0656
REMARK 3 T13: -0.0493 T23: -0.0380
REMARK 3 L TENSOR
REMARK 3 L11: 0.5082 L22: 1.6122
REMARK 3 L33: 0.8120 L12: -0.1779
REMARK 3 L13: 0.5052 L23: -0.7742
REMARK 3 S TENSOR
REMARK 3 S11: 0.0980 S12: 0.0765 S13: -0.1225
REMARK 3 S21: -0.0996 S22: 0.0276 S23: 0.1133
REMARK 3 S31: 0.0774 S32: -0.0491 S33: -0.1256
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 217 A 247
REMARK 3 ORIGIN FOR THE GROUP (A): -48.787 -13.250 9.411
REMARK 3 T TENSOR
REMARK 3 T11: 0.1034 T22: 0.1402
REMARK 3 T33: 0.0584 T12: 0.1182
REMARK 3 T13: 0.0393 T23: 0.0404
REMARK 3 L TENSOR
REMARK 3 L11: 3.0835 L22: 2.0357
REMARK 3 L33: 0.6804 L12: 2.0420
REMARK 3 L13: 1.1489 L23: 0.3711
REMARK 3 S TENSOR
REMARK 3 S11: 0.1030 S12: 0.0507 S13: 0.0262
REMARK 3 S21: -0.0402 S22: -0.0590 S23: 0.0650
REMARK 3 S31: 0.0471 S32: 0.0145 S33: -0.0440
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 248 A 267
REMARK 3 ORIGIN FOR THE GROUP (A): -51.809 -4.895 12.807
REMARK 3 T TENSOR
REMARK 3 T11: 0.1071 T22: 0.1431
REMARK 3 T33: 0.1004 T12: 0.1119
REMARK 3 T13: 0.0234 T23: 0.0648
REMARK 3 L TENSOR
REMARK 3 L11: 4.5891 L22: 4.3138
REMARK 3 L33: 0.9061 L12: 3.6001
REMARK 3 L13: 1.9053 L23: 1.4186
REMARK 3 S TENSOR
REMARK 3 S11: 0.0046 S12: 0.1377 S13: 0.3377
REMARK 3 S21: -0.0623 S22: -0.0881 S23: 0.2349
REMARK 3 S31: -0.0923 S32: -0.0454 S33: 0.0836
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 2 B 37
REMARK 3 ORIGIN FOR THE GROUP (A): -30.482 -42.634 13.985
REMARK 3 T TENSOR
REMARK 3 T11: 0.0474 T22: 0.1645
REMARK 3 T33: 0.0363 T12: -0.0260
REMARK 3 T13: -0.0116 T23: -0.0199
REMARK 3 L TENSOR
REMARK 3 L11: 0.8522 L22: 0.0297
REMARK 3 L33: 0.4080 L12: 0.0345
REMARK 3 L13: -0.5238 L23: 0.0246
REMARK 3 S TENSOR
REMARK 3 S11: -0.0046 S12: 0.0793 S13: -0.0789
REMARK 3 S21: 0.0290 S22: -0.0492 S23: -0.0023
REMARK 3 S31: 0.0378 S32: -0.1607 S33: 0.0538
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 38 B 70
REMARK 3 ORIGIN FOR THE GROUP (A): -3.965 -47.110 5.706
REMARK 3 T TENSOR
REMARK 3 T11: 0.0598 T22: 0.0901
REMARK 3 T33: 0.0461 T12: -0.0039
REMARK 3 T13: -0.0152 T23: -0.0070
REMARK 3 L TENSOR
REMARK 3 L11: 0.1834 L22: 0.1212
REMARK 3 L33: 0.4594 L12: 0.0041
REMARK 3 L13: -0.2104 L23: 0.1547
REMARK 3 S TENSOR
REMARK 3 S11: -0.0517 S12: 0.0309 S13: -0.0165
REMARK 3 S21: 0.0174 S22: 0.0339 S23: 0.0143
REMARK 3 S31: 0.0726 S32: 0.0458 S33: 0.0178
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 : B 71 B 100
REMARK 3 ORIGIN FOR THE GROUP (A): -8.765 -41.503 5.789
REMARK 3 T TENSOR
REMARK 3 T11: 0.0573 T22: 0.0893
REMARK 3 T33: 0.0444 T12: -0.0026
REMARK 3 T13: -0.0112 T23: -0.0075
REMARK 3 L TENSOR
REMARK 3 L11: 0.0985 L22: 0.0173
REMARK 3 L33: 0.4213 L12: -0.0371
REMARK 3 L13: 0.0755 L23: 0.0030
REMARK 3 S TENSOR
REMARK 3 S11: 0.0169 S12: 0.0467 S13: 0.0024
REMARK 3 S21: -0.0075 S22: -0.0179 S23: -0.0054
REMARK 3 S31: 0.0216 S32: -0.0003 S33: 0.0009
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 : B 101 B 165
REMARK 3 ORIGIN FOR THE GROUP (A): -17.435 -26.633 0.820
REMARK 3 T TENSOR
REMARK 3 T11: 0.1334 T22: 0.1025
REMARK 3 T33: 0.0276 T12: 0.0480
REMARK 3 T13: 0.0220 T23: 0.0095
REMARK 3 L TENSOR
REMARK 3 L11: 0.1225 L22: 0.5087
REMARK 3 L33: 0.9006 L12: 0.0764
REMARK 3 L13: 0.1372 L23: 0.1768
REMARK 3 S TENSOR
REMARK 3 S11: 0.0775 S12: 0.0229 S13: -0.0320
REMARK 3 S21: -0.0474 S22: 0.0405 S23: -0.0898
REMARK 3 S31: -0.1793 S32: -0.1390 S33: -0.1180
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 : B 166 B 196
REMARK 3 ORIGIN FOR THE GROUP (A): -27.006 -31.543 7.907
REMARK 3 T TENSOR
REMARK 3 T11: 0.0688 T22: 0.1794
REMARK 3 T33: 0.0350 T12: 0.0431
REMARK 3 T13: -0.0089 T23: 0.0204
REMARK 3 L TENSOR
REMARK 3 L11: 0.0728 L22: 0.1519
REMARK 3 L33: 0.8261 L12: 0.0994
REMARK 3 L13: -0.2019 L23: -0.3332
REMARK 3 S TENSOR
REMARK 3 S11: 0.0430 S12: 0.0786 S13: 0.0185
REMARK 3 S21: 0.0506 S22: 0.0730 S23: 0.0353
REMARK 3 S31: -0.0420 S32: -0.1515 S33: -0.1160
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 : B 197 B 364
REMARK 3 ORIGIN FOR THE GROUP (A): -8.115 -36.287 20.313
REMARK 3 T TENSOR
REMARK 3 T11: 0.0562 T22: 0.0756
REMARK 3 T33: 0.0528 T12: -0.0005
REMARK 3 T13: -0.0037 T23: -0.0006
REMARK 3 L TENSOR
REMARK 3 L11: 0.2229 L22: 0.0280
REMARK 3 L33: 0.2509 L12: 0.0051
REMARK 3 L13: -0.0322 L23: 0.0799
REMARK 3 S TENSOR
REMARK 3 S11: 0.0069 S12: -0.0204 S13: 0.0214
REMARK 3 S21: -0.0006 S22: -0.0035 S23: 0.0083
REMARK 3 S31: 0.0104 S32: 0.0019 S33: -0.0034
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 : B 365 B 396
REMARK 3 ORIGIN FOR THE GROUP (A): 4.350 -30.333 15.503
REMARK 3 T TENSOR
REMARK 3 T11: 0.0717 T22: 0.1039
REMARK 3 T33: 0.0383 T12: -0.0147
REMARK 3 T13: 0.0233 T23: -0.0290
REMARK 3 L TENSOR
REMARK 3 L11: 0.2869 L22: 0.2885
REMARK 3 L33: 0.5912 L12: -0.2423
REMARK 3 L13: -0.1908 L23: -0.0050
REMARK 3 S TENSOR
REMARK 3 S11: 0.1006 S12: -0.0097 S13: 0.0324
REMARK 3 S21: -0.0697 S22: 0.0333 S23: 0.0067
REMARK 3 S31: -0.0882 S32: 0.0686 S33: -0.1339
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: U VALUES : WITH TLS ADDED
REMARK 4
REMARK 4 6DZ4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-JUL-18.
REMARK 100 THE DEPOSITION ID IS D_1000235460.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-APR-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.6-8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 12.3.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97930
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM 7.2.2
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.2.22
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 126505
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.450
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 5.600
REMARK 200 R MERGE (I) : 0.08500
REMARK 200 R SYM (I) : 0.08500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.45
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.53
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.1
REMARK 200 DATA REDUNDANCY IN SHELL : 5.30
REMARK 200 R MERGE FOR SHELL (I) : 0.63200
REMARK 200 R SYM FOR SHELL (I) : 0.04100
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: MOLREP 11.6.03
REMARK 200 STARTING MODEL: 4HN4
REMARK 200
REMARK 200 REMARK: LARGE PLATE-LIKE CRYSTAL.
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.48
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50MM BICINE-NAOH, PH 7.8, CONTAINING
REMARK 280 9% PEG3350, 50MM NACL, 2MM SPERMINE, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 297K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 91.25450
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 29.65000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 91.25450
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 29.65000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 14350 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 44610 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -158.0 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 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 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 ARG A 179
REMARK 465 SER A 180
REMARK 465 GLY A 181
REMARK 465 VAL A 182
REMARK 465 THR A 183
REMARK 465 GLY A 184
REMARK 465 ALA A 185
REMARK 465 GLU A 186
REMARK 465 ASN A 187
REMARK 465 ARG A 188
REMARK 465 GLY A 189
REMARK 465 ALA A 190
REMARK 465 ALA A 268
REMARK 465 MET B 1
REMARK 465 ILE B 397
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 551 O HOH A 573 1.98
REMARK 500 O HOH B 908 O HOH B 927 1.98
REMARK 500 O HOH B 783 O HOH B 856 2.11
REMARK 500 O DMS B 417 O HOH B 501 2.13
REMARK 500 NH2 ARG B 222 O HOH B 502 2.15
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 SER A 235 -12.22 -144.84
REMARK 500 ALA B 269 63.71 -119.43
REMARK 500 SER B 308 -153.49 -137.35
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 654 DISTANCE = 6.03 ANGSTROMS
REMARK 525 HOH A 655 DISTANCE = 6.27 ANGSTROMS
REMARK 525 HOH B 976 DISTANCE = 5.81 ANGSTROMS
REMARK 525 HOH B 977 DISTANCE = 6.18 ANGSTROMS
REMARK 525 HOH B 978 DISTANCE = 6.30 ANGSTROMS
REMARK 525 HOH B 979 DISTANCE = 6.60 ANGSTROMS
REMARK 525 HOH B 980 DISTANCE = 6.62 ANGSTROMS
REMARK 525 HOH B 981 DISTANCE = 6.72 ANGSTROMS
REMARK 525 HOH B 982 DISTANCE = 6.96 ANGSTROMS
REMARK 525 HOH B 983 DISTANCE = 7.21 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 402 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR B 69 O
REMARK 620 2 THR B 71 O 93.7
REMARK 620 3 HOH B 693 O 129.4 116.0
REMARK 620 4 HOH B 824 O 83.1 80.5 138.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 403 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY B 232 O
REMARK 620 2 PHE B 306 O 103.5
REMARK 620 3 SER B 308 O 93.4 85.4
REMARK 620 4 HOH B 584 O 115.6 76.5 148.6
REMARK 620 5 HOH B 690 O 89.2 164.3 103.2 89.8
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue KOU B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS B 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS B 411
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS B 412
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS B 413
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS B 414
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS B 415
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS B 416
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS B 417
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4HN4 RELATED DB: PDB
REMARK 900 RELATED ID: 4HPX RELATED DB: PDB
DBREF 6DZ4 A 1 268 UNP P00929 TRPA_SALTY 1 268
DBREF 6DZ4 B 1 397 UNP P0A2K1 TRPB_SALTY 1 397
SEQRES 1 A 268 MET GLU ARG TYR GLU ASN LEU PHE ALA GLN LEU ASN ASP
SEQRES 2 A 268 ARG ARG GLU GLY ALA PHE VAL PRO PHE VAL THR LEU GLY
SEQRES 3 A 268 ASP PRO GLY ILE GLU GLN SER LEU LYS ILE ILE ASP THR
SEQRES 4 A 268 LEU ILE ASP ALA GLY ALA ASP ALA LEU GLU LEU GLY VAL
SEQRES 5 A 268 PRO PHE SER ASP PRO LEU ALA ASP GLY PRO THR ILE GLN
SEQRES 6 A 268 ASN ALA ASN LEU ARG ALA PHE ALA ALA GLY VAL THR PRO
SEQRES 7 A 268 ALA GLN CYS PHE GLU MET LEU ALA LEU ILE ARG GLU LYS
SEQRES 8 A 268 HIS PRO THR ILE PRO ILE GLY LEU LEU MET TYR ALA ASN
SEQRES 9 A 268 LEU VAL PHE ASN ASN GLY ILE ASP ALA PHE TYR ALA ARG
SEQRES 10 A 268 CYS GLU GLN VAL GLY VAL ASP SER VAL LEU VAL ALA ASP
SEQRES 11 A 268 VAL PRO VAL GLU GLU SER ALA PRO PHE ARG GLN ALA ALA
SEQRES 12 A 268 LEU ARG HIS ASN ILE ALA PRO ILE PHE ILE CYS PRO PRO
SEQRES 13 A 268 ASN ALA ASP ASP ASP LEU LEU ARG GLN VAL ALA SER TYR
SEQRES 14 A 268 GLY ARG GLY TYR THR TYR LEU LEU SER ARG SER GLY VAL
SEQRES 15 A 268 THR GLY ALA GLU ASN ARG GLY ALA LEU PRO LEU HIS HIS
SEQRES 16 A 268 LEU ILE GLU LYS LEU LYS GLU TYR HIS ALA ALA PRO ALA
SEQRES 17 A 268 LEU GLN GLY PHE GLY ILE SER SER PRO GLU GLN VAL SER
SEQRES 18 A 268 ALA ALA VAL ARG ALA GLY ALA ALA GLY ALA ILE SER GLY
SEQRES 19 A 268 SER ALA ILE VAL LYS ILE ILE GLU LYS ASN LEU ALA SER
SEQRES 20 A 268 PRO LYS GLN MET LEU ALA GLU LEU ARG SER PHE VAL SER
SEQRES 21 A 268 ALA MET LYS ALA ALA SER ARG ALA
SEQRES 1 B 397 MET THR THR LEU LEU ASN PRO TYR PHE GLY GLU PHE GLY
SEQRES 2 B 397 GLY MET TYR VAL PRO GLN ILE LEU MET PRO ALA LEU ASN
SEQRES 3 B 397 GLN LEU GLU GLU ALA PHE VAL SER ALA GLN LYS ASP PRO
SEQRES 4 B 397 GLU PHE GLN ALA GLN PHE ALA ASP LEU LEU LYS ASN TYR
SEQRES 5 B 397 ALA GLY ARG PRO THR ALA LEU THR LYS CYS GLN ASN ILE
SEQRES 6 B 397 THR ALA GLY THR ARG THR THR LEU TYR LEU LYS ARG GLU
SEQRES 7 B 397 ASP LEU LEU HIS GLY GLY ALA HIS LYS THR ASN GLN VAL
SEQRES 8 B 397 LEU GLY GLN ALA LEU LEU ALA LYS ARG MET GLY LYS SER
SEQRES 9 B 397 GLU ILE ILE ALA GLU THR GLY ALA GLY GLN HIS GLY VAL
SEQRES 10 B 397 ALA SER ALA LEU ALA SER ALA LEU LEU GLY LEU LYS CYS
SEQRES 11 B 397 ARG ILE TYR MET GLY ALA LYS ASP VAL GLU ARG GLN SER
SEQRES 12 B 397 PRO ASN VAL PHE ARG MET ARG LEU MET GLY ALA GLU VAL
SEQRES 13 B 397 ILE PRO VAL HIS SER GLY SER ALA THR LEU LYS ASP ALA
SEQRES 14 B 397 CYS ASN GLU ALA LEU ARG ASP TRP SER GLY SER TYR GLU
SEQRES 15 B 397 THR ALA HIS TYR MET LEU GLY THR ALA ALA GLY PRO HIS
SEQRES 16 B 397 PRO TYR PRO THR ILE VAL ARG GLU PHE GLN ARG MET ILE
SEQRES 17 B 397 GLY GLU GLU THR LYS ALA GLN ILE LEU ASP LYS GLU GLY
SEQRES 18 B 397 ARG LEU PRO ASP ALA VAL ILE ALA CYS VAL GLY GLY GLY
SEQRES 19 B 397 SER ASN ALA ILE GLY MET PHE ALA ASP PHE ILE ASN ASP
SEQRES 20 B 397 THR SER VAL GLY LEU ILE GLY VAL GLU PRO GLY GLY HIS
SEQRES 21 B 397 GLY ILE GLU THR GLY GLU HIS GLY ALA PRO LEU LYS HIS
SEQRES 22 B 397 GLY ARG VAL GLY ILE TYR PHE GLY MET LYS ALA PRO MET
SEQRES 23 B 397 MET GLN THR ALA ASP GLY GLN ILE GLU GLU SER TYR SER
SEQRES 24 B 397 ILE SER ALA GLY LEU ASP PHE PRO SER VAL GLY PRO GLN
SEQRES 25 B 397 HIS ALA TYR LEU ASN SER ILE GLY ARG ALA ASP TYR VAL
SEQRES 26 B 397 SER ILE THR ASP ASP GLU ALA LEU GLU ALA PHE LYS THR
SEQRES 27 B 397 LEU CYS ARG HIS GLU GLY ILE ILE PRO ALA LEU GLU SER
SEQRES 28 B 397 SER HIS ALA LEU ALA HIS ALA LEU LYS MET MET ARG GLU
SEQRES 29 B 397 GLN PRO GLU LYS GLU GLN LEU LEU VAL VAL ASN LEU SER
SEQRES 30 B 397 GLY ARG GLY ASP LYS ASP ILE PHE THR VAL HIS ASP ILE
SEQRES 31 B 397 LEU LYS ALA ARG GLY GLU ILE
HET CL A 301 1
HET CL A 302 1
HET DMS A 303 4
HET DMS A 304 4
HET DMS A 305 4
HET DMS A 306 4
HET KOU B 401 22
HET NA B 402 1
HET NA B 403 1
HET CL B 404 1
HET CL B 405 1
HET CL B 406 1
HET CL B 407 1
HET CL B 408 1
HET CL B 409 1
HET DMS B 410 4
HET DMS B 411 4
HET DMS B 412 4
HET DMS B 413 4
HET DMS B 414 4
HET DMS B 415 4
HET DMS B 416 4
HET DMS B 417 4
HETNAM CL CHLORIDE ION
HETNAM DMS DIMETHYL SULFOXIDE
HETNAM KOU (E)-N-({3-HYDROXY-2-METHYL-5-[(PHOSPHONOOXY)
HETNAM 2 KOU METHYL]PYRIDIN-4-YL}METHYLIDENE)-L-SERINE
HETNAM NA SODIUM ION
FORMUL 3 CL 8(CL 1-)
FORMUL 5 DMS 12(C2 H6 O S)
FORMUL 9 KOU C11 H15 N2 O8 P
FORMUL 10 NA 2(NA 1+)
FORMUL 26 HOH *738(H2 O)
HELIX 1 AA1 GLU A 2 ARG A 14 1 13
HELIX 2 AA2 GLY A 29 ALA A 43 1 15
HELIX 3 AA3 GLY A 61 ALA A 74 1 14
HELIX 4 AA4 THR A 77 HIS A 92 1 16
HELIX 5 AA5 TYR A 102 ASN A 108 1 7
HELIX 6 AA6 GLY A 110 GLY A 122 1 13
HELIX 7 AA7 PRO A 132 GLU A 135 5 4
HELIX 8 AA8 SER A 136 HIS A 146 1 11
HELIX 9 AA9 ASP A 159 GLY A 170 1 12
HELIX 10 AB1 PRO A 192 TYR A 203 1 12
HELIX 11 AB2 SER A 216 ALA A 226 1 11
HELIX 12 AB3 SER A 235 ASN A 244 1 10
HELIX 13 AB4 SER A 247 ALA A 265 1 19
HELIX 14 AB5 PRO B 18 ILE B 20 5 3
HELIX 15 AB6 LEU B 21 LYS B 37 1 17
HELIX 16 AB7 ASP B 38 TYR B 52 1 15
HELIX 17 AB8 GLN B 63 ALA B 67 5 5
HELIX 18 AB9 ASP B 79 LEU B 81 5 3
HELIX 19 AC1 LYS B 87 MET B 101 1 15
HELIX 20 AC2 GLY B 113 GLY B 127 1 15
HELIX 21 AC3 ALA B 136 GLN B 142 1 7
HELIX 22 AC4 GLN B 142 MET B 152 1 11
HELIX 23 AC5 THR B 165 TYR B 181 1 17
HELIX 24 AC6 PRO B 196 PHE B 204 1 9
HELIX 25 AC7 ARG B 206 GLY B 221 1 16
HELIX 26 AC8 GLY B 234 ALA B 242 1 9
HELIX 27 AC9 ASP B 243 ILE B 245 5 3
HELIX 28 AD1 GLY B 261 GLY B 265 5 5
HELIX 29 AD2 ALA B 269 GLY B 274 1 6
HELIX 30 AD3 SER B 301 ASP B 305 5 5
HELIX 31 AD4 GLY B 310 ILE B 319 1 10
HELIX 32 AD5 ASP B 329 GLY B 344 1 16
HELIX 33 AD6 ALA B 348 GLN B 365 1 18
HELIX 34 AD7 GLY B 380 LYS B 382 5 3
HELIX 35 AD8 ASP B 383 GLY B 395 1 13
SHEET 1 AA1 9 ALA A 149 ILE A 151 0
SHEET 2 AA1 9 SER A 125 VAL A 128 1 N VAL A 126 O ALA A 149
SHEET 3 AA1 9 ILE A 97 MET A 101 1 N MET A 101 O LEU A 127
SHEET 4 AA1 9 LEU A 48 GLY A 51 1 N LEU A 48 O GLY A 98
SHEET 5 AA1 9 ALA A 18 THR A 24 1 N VAL A 23 O GLY A 51
SHEET 6 AA1 9 GLY A 230 SER A 233 1 O ALA A 231 N ALA A 18
SHEET 7 AA1 9 ALA A 208 GLN A 210 1 N GLN A 210 O ILE A 232
SHEET 8 AA1 9 THR A 174 LEU A 176 1 N THR A 174 O LEU A 209
SHEET 9 AA1 9 ILE A 153 CYS A 154 1 N CYS A 154 O TYR A 175
SHEET 1 AA2 4 TYR B 8 PHE B 9 0
SHEET 2 AA2 4 PHE B 12 TYR B 16 -1 O PHE B 12 N PHE B 9
SHEET 3 AA2 4 GLY B 281 MET B 286 -1 O LYS B 283 N GLY B 13
SHEET 4 AA2 4 ARG B 275 TYR B 279 -1 N GLY B 277 O ALA B 284
SHEET 1 AA3 6 LEU B 59 LYS B 61 0
SHEET 2 AA3 6 THR B 71 ARG B 77 -1 O LEU B 75 N THR B 60
SHEET 3 AA3 6 GLN B 370 LEU B 376 1 O LEU B 372 N THR B 72
SHEET 4 AA3 6 ALA B 226 CYS B 230 1 N ILE B 228 O ASN B 375
SHEET 5 AA3 6 GLY B 251 GLY B 259 1 O ILE B 253 N VAL B 227
SHEET 6 AA3 6 ASP B 323 THR B 328 1 O ILE B 327 N GLY B 258
SHEET 1 AA4 4 GLU B 155 VAL B 159 0
SHEET 2 AA4 4 LYS B 129 GLY B 135 1 N ILE B 132 O ILE B 157
SHEET 3 AA4 4 GLU B 105 GLU B 109 1 N ALA B 108 O TYR B 133
SHEET 4 AA4 4 ALA B 184 TYR B 186 1 O HIS B 185 N ILE B 107
LINK O THR B 69 NA NA B 402 1555 1555 3.00
LINK O THR B 71 NA NA B 402 1555 1555 2.96
LINK O GLY B 232 NA NA B 403 1555 1555 2.21
LINK O PHE B 306 NA NA B 403 1555 1555 2.47
LINK O SER B 308 NA NA B 403 1555 1555 2.29
LINK NA NA B 402 O HOH B 693 1555 1555 3.04
LINK NA NA B 402 O HOH B 824 1555 1555 2.14
LINK NA NA B 403 O HOH B 584 1555 1555 2.37
LINK NA NA B 403 O HOH B 690 1555 1555 2.35
CISPEP 1 ASP A 27 PRO A 28 0 7.74
CISPEP 2 ARG B 55 PRO B 56 0 -0.34
CISPEP 3 HIS B 195 PRO B 196 0 10.32
SITE 1 AC1 5 HIS A 92 PRO A 93 THR A 94 ILE A 95
SITE 2 AC1 5 HOH A 592
SITE 1 AC2 3 ARG A 225 CL B 407 HOH B 758
SITE 1 AC3 3 PHE A 82 HOH A 499 HOH A 549
SITE 1 AC4 4 GLU A 5 ILE A 148 ALA A 149 HOH A 555
SITE 1 AC5 2 ASP A 60 TYR A 175
SITE 1 AC6 2 ASN A 12 GLU A 16
SITE 1 AC7 22 HIS B 86 LYS B 87 THR B 110 GLY B 111
SITE 2 AC7 22 ALA B 112 GLY B 113 GLN B 114 HIS B 115
SITE 3 AC7 22 THR B 190 GLY B 232 GLY B 233 GLY B 234
SITE 4 AC7 22 SER B 235 ASN B 236 ALA B 302 GLY B 303
SITE 5 AC7 22 ASP B 305 GLU B 350 SER B 377 HOH B 646
SITE 6 AC7 22 HOH B 677 HOH B 681
SITE 1 AC8 5 THR B 66 THR B 69 THR B 71 HOH B 693
SITE 2 AC8 5 HOH B 824
SITE 1 AC9 5 GLY B 232 PHE B 306 SER B 308 HOH B 584
SITE 2 AC9 5 HOH B 690
SITE 1 AD1 2 LYS B 219 GLU B 220
SITE 1 AD2 2 GLY B 274 DMS B 411
SITE 1 AD3 4 VAL A 224 ARG A 225 CL A 302 HOH B 755
SITE 1 AD4 2 PRO A 138 LYS B 283
SITE 1 AD5 4 GLN B 42 ALA B 46 HOH B 902 HOH B 939
SITE 1 AD6 7 LEU B 271 ASN B 317 ARG B 363 GLU B 364
SITE 2 AD6 7 CL B 406 HOH B 527 HOH B 559
SITE 1 AD7 5 SER B 143 PRO B 144 PHE B 385 HIS B 388
SITE 2 AD7 5 HOH B 596
SITE 1 AD8 4 ILE B 262 HIS B 267 HIS B 273 HOH B 615
SITE 1 AD9 2 GLN B 36 LYS B 37
SITE 1 AE1 3 TYR B 8 GLY B 10 HOH B 899
SITE 1 AE2 4 THR B 3 LEU B 4 LEU B 5 ASN B 6
SITE 1 AE3 6 HIS B 357 GLU B 364 HOH B 501 HOH B 621
SITE 2 AE3 6 HOH B 879 HOH B 954
CRYST1 182.509 59.300 67.325 90.00 94.69 90.00 C 1 2 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 0.005479 0.000000 0.000449 0.00000
SCALE2 0.000000 0.016863 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014903 0.00000
(ATOM LINES ARE NOT SHOWN.)
END