HEADER LYASE 19-JAN-18 6C73
TITLE TRYPTOPHAN SYNTHASE Q114A MUTANT (INTERNAL ALDIMINE STATE) IN COMPLEX
TITLE 2 WITH N-(4'-TRIFLUOROMETHOXYBENZENESULFONYL)-2-AMINO-1-ETHYLPHOSPHATE
TITLE 3 (F9F) WITH CESIUM ION BOUND IN THE METAL COORDINATION 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;
COMPND 11 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SALMONELLA ENTERICA SUBSP. ENTERICA SEROVAR
SOURCE 3 TYPHIMURIUM;
SOURCE 4 ORGANISM_TAXID: 90371;
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_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PEBA-10;
SOURCE 12 MOL_ID: 2;
SOURCE 13 ORGANISM_SCIENTIFIC: SALMONELLA ENTERICA SUBSP. ENTERICA SEROVAR
SOURCE 14 TYPHIMURIUM;
SOURCE 15 ORGANISM_TAXID: 90371;
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_VECTOR_TYPE: PLASMID;
SOURCE 21 EXPRESSION_SYSTEM_PLASMID: PEBA-10
KEYWDS F9F LIGAND, CESIUM ION, MUTANT BETA-Q114A, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.HILARIO,M.F.DUNN,L.J.MUELLER,L.FAN
REVDAT 5 04-OCT-23 6C73 1 REMARK
REVDAT 4 29-SEP-21 6C73 1 REMARK LINK
REVDAT 3 27-NOV-19 6C73 1 REMARK
REVDAT 2 20-FEB-19 6C73 1 REMARK
REVDAT 1 23-JAN-19 6C73 0
JRNL AUTH E.HILARIO,M.F.DUNN,L.J.MUELLER,L.FAN
JRNL TITL TRYPTOPHAN SYNTHASE Q114A MUTANT (INTERNAL ALDIMINE STATE)
JRNL TITL 2 IN COMPLEX WITH
JRNL TITL 3 N-(4'-TRIFLUOROMETHOXYBENZENESULFONYL)
JRNL TITL 4 -2-AMINO-1-ETHYLPHOSPHATE (F9F) WITH CESIUM ION BOUND IN THE
JRNL TITL 5 METAL COORDINATION SITE.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.65 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0135
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.82
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 80889
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) : 0.141
REMARK 3 R VALUE (WORKING SET) : 0.138
REMARK 3 FREE R VALUE : 0.183
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 4306
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) : 1.65
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.69
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5862
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.53
REMARK 3 BIN R VALUE (WORKING SET) : 0.2250
REMARK 3 BIN FREE R VALUE SET COUNT : 320
REMARK 3 BIN FREE R VALUE : 0.2910
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5005
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 149
REMARK 3 SOLVENT ATOMS : 863
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 11.92
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.71
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.01000
REMARK 3 B22 (A**2) : 0.02000
REMARK 3 B33 (A**2) : 0.00000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.02000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.121
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.086
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.051
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.314
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.971
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.952
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5567 ; 0.013 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7552 ; 1.535 ; 1.989
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 734 ; 5.750 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 233 ;36.580 ;24.163
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 921 ;12.475 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 36 ;17.409 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 838 ; 0.102 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4257 ; 0.008 ; 0.021
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): 5567 ; 2.373 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 227 ;27.937 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 6153 ; 9.064 ; 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 : 15
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 30 A 159
REMARK 3 ORIGIN FOR THE GROUP (A): 37.8604 10.0226 8.8869
REMARK 3 T TENSOR
REMARK 3 T11: 0.0408 T22: 0.0241
REMARK 3 T33: 0.0443 T12: -0.0052
REMARK 3 T13: 0.0160 T23: 0.0070
REMARK 3 L TENSOR
REMARK 3 L11: 0.1291 L22: 0.3387
REMARK 3 L33: 0.1736 L12: 0.0427
REMARK 3 L13: 0.0770 L23: 0.0349
REMARK 3 S TENSOR
REMARK 3 S11: 0.0187 S12: 0.0117 S13: 0.0091
REMARK 3 S21: -0.0080 S22: -0.0149 S23: 0.0156
REMARK 3 S31: -0.0051 S32: 0.0018 S33: -0.0037
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 160 A 202
REMARK 3 ORIGIN FOR THE GROUP (A): 47.1109 -1.5979 21.7771
REMARK 3 T TENSOR
REMARK 3 T11: 0.0595 T22: 0.0233
REMARK 3 T33: 0.0705 T12: -0.0025
REMARK 3 T13: -0.0493 T23: 0.0131
REMARK 3 L TENSOR
REMARK 3 L11: 0.5457 L22: 0.6001
REMARK 3 L33: 0.3009 L12: -0.1996
REMARK 3 L13: 0.0380 L23: 0.3507
REMARK 3 S TENSOR
REMARK 3 S11: 0.0228 S12: -0.1119 S13: -0.0829
REMARK 3 S21: 0.0364 S22: 0.0464 S23: 0.0166
REMARK 3 S31: 0.0767 S32: 0.0010 S33: -0.0691
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 203 A 234
REMARK 3 ORIGIN FOR THE GROUP (A): 51.3520 6.6993 22.9123
REMARK 3 T TENSOR
REMARK 3 T11: 0.0400 T22: 0.0400
REMARK 3 T33: 0.0430 T12: -0.0144
REMARK 3 T13: -0.0114 T23: -0.0077
REMARK 3 L TENSOR
REMARK 3 L11: 0.1731 L22: 0.7117
REMARK 3 L33: 0.6615 L12: -0.0184
REMARK 3 L13: 0.2426 L23: 0.4375
REMARK 3 S TENSOR
REMARK 3 S11: 0.0436 S12: -0.0256 S13: 0.0175
REMARK 3 S21: 0.0404 S22: -0.0030 S23: -0.0847
REMARK 3 S31: 0.0757 S32: -0.0250 S33: -0.0406
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 235 A 247
REMARK 3 ORIGIN FOR THE GROUP (A): 37.4179 24.4795 23.1137
REMARK 3 T TENSOR
REMARK 3 T11: 0.0661 T22: 0.0236
REMARK 3 T33: 0.0374 T12: 0.0049
REMARK 3 T13: 0.0030 T23: -0.0125
REMARK 3 L TENSOR
REMARK 3 L11: 1.8920 L22: 6.9934
REMARK 3 L33: 0.0783 L12: -1.4117
REMARK 3 L13: 0.2629 L23: -0.6915
REMARK 3 S TENSOR
REMARK 3 S11: 0.0633 S12: -0.1281 S13: 0.0496
REMARK 3 S21: 0.1986 S22: -0.0814 S23: -0.1069
REMARK 3 S31: -0.0139 S32: -0.0049 S33: 0.0181
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 248 A 268
REMARK 3 ORIGIN FOR THE GROUP (A): 49.2846 24.4003 21.1961
REMARK 3 T TENSOR
REMARK 3 T11: 0.0690 T22: 0.0115
REMARK 3 T33: 0.0570 T12: -0.0249
REMARK 3 T13: 0.0004 T23: -0.0065
REMARK 3 L TENSOR
REMARK 3 L11: 3.0183 L22: 2.9359
REMARK 3 L33: 0.4022 L12: -2.4977
REMARK 3 L13: 0.7037 L23: -0.1356
REMARK 3 S TENSOR
REMARK 3 S11: -0.0906 S12: -0.0445 S13: 0.2033
REMARK 3 S21: 0.0653 S22: 0.0601 S23: -0.1786
REMARK 3 S31: -0.0465 S32: 0.0105 S33: 0.0305
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 2 B 37
REMARK 3 ORIGIN FOR THE GROUP (A): 27.8360 -13.1506 19.3565
REMARK 3 T TENSOR
REMARK 3 T11: 0.0386 T22: 0.0619
REMARK 3 T33: 0.0408 T12: 0.0046
REMARK 3 T13: -0.0155 T23: 0.0012
REMARK 3 L TENSOR
REMARK 3 L11: 0.3923 L22: 0.0015
REMARK 3 L33: 0.5001 L12: -0.0194
REMARK 3 L13: -0.4277 L23: 0.0202
REMARK 3 S TENSOR
REMARK 3 S11: -0.0239 S12: -0.0409 S13: -0.0397
REMARK 3 S21: -0.0033 S22: 0.0011 S23: 0.0029
REMARK 3 S31: 0.0378 S32: 0.0824 S33: 0.0228
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 38 B 70
REMARK 3 ORIGIN FOR THE GROUP (A): 1.3540 -17.6381 27.8067
REMARK 3 T TENSOR
REMARK 3 T11: 0.0388 T22: 0.0627
REMARK 3 T33: 0.0248 T12: -0.0055
REMARK 3 T13: -0.0042 T23: 0.0098
REMARK 3 L TENSOR
REMARK 3 L11: 0.0309 L22: 0.2036
REMARK 3 L33: 0.1847 L12: -0.0416
REMARK 3 L13: -0.0141 L23: -0.1359
REMARK 3 S TENSOR
REMARK 3 S11: -0.0241 S12: -0.0069 S13: -0.0019
REMARK 3 S21: 0.0047 S22: 0.0222 S23: -0.0093
REMARK 3 S31: 0.0420 S32: -0.0416 S33: 0.0019
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 71 B 126
REMARK 3 ORIGIN FOR THE GROUP (A): 10.5580 -8.7006 30.2135
REMARK 3 T TENSOR
REMARK 3 T11: 0.0454 T22: 0.0612
REMARK 3 T33: 0.0226 T12: 0.0055
REMARK 3 T13: -0.0086 T23: 0.0119
REMARK 3 L TENSOR
REMARK 3 L11: 0.0126 L22: 0.1655
REMARK 3 L33: 0.0272 L12: 0.0431
REMARK 3 L13: 0.0165 L23: 0.0654
REMARK 3 S TENSOR
REMARK 3 S11: 0.0116 S12: 0.0051 S13: -0.0007
REMARK 3 S21: 0.0251 S22: -0.0069 S23: -0.0116
REMARK 3 S31: 0.0119 S32: -0.0112 S33: -0.0046
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 127 B 165
REMARK 3 ORIGIN FOR THE GROUP (A): 14.3087 7.1632 32.2552
REMARK 3 T TENSOR
REMARK 3 T11: 0.0564 T22: 0.0279
REMARK 3 T33: 0.0459 T12: 0.0087
REMARK 3 T13: 0.0382 T23: 0.0205
REMARK 3 L TENSOR
REMARK 3 L11: 0.1209 L22: 0.4622
REMARK 3 L33: 0.8772 L12: 0.2233
REMARK 3 L13: 0.2026 L23: 0.2119
REMARK 3 S TENSOR
REMARK 3 S11: 0.0165 S12: 0.0225 S13: 0.0019
REMARK 3 S21: 0.0669 S22: 0.0568 S23: 0.0276
REMARK 3 S31: -0.1351 S32: 0.0139 S33: -0.0732
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 166 B 244
REMARK 3 ORIGIN FOR THE GROUP (A): 12.8717 -11.4304 21.1607
REMARK 3 T TENSOR
REMARK 3 T11: 0.0429 T22: 0.0493
REMARK 3 T33: 0.0327 T12: -0.0009
REMARK 3 T13: -0.0089 T23: 0.0074
REMARK 3 L TENSOR
REMARK 3 L11: 0.0728 L22: 0.1154
REMARK 3 L33: 0.1960 L12: 0.0431
REMARK 3 L13: -0.0252 L23: 0.1130
REMARK 3 S TENSOR
REMARK 3 S11: -0.0098 S12: -0.0128 S13: -0.0177
REMARK 3 S21: -0.0068 S22: -0.0006 S23: -0.0077
REMARK 3 S31: 0.0143 S32: 0.0204 S33: 0.0104
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 245 B 273
REMARK 3 ORIGIN FOR THE GROUP (A): 5.9126 -4.2109 7.5083
REMARK 3 T TENSOR
REMARK 3 T11: 0.0457 T22: 0.0462
REMARK 3 T33: 0.0345 T12: 0.0012
REMARK 3 T13: 0.0015 T23: 0.0049
REMARK 3 L TENSOR
REMARK 3 L11: 0.0507 L22: 0.6693
REMARK 3 L33: 0.2194 L12: 0.0255
REMARK 3 L13: 0.0785 L23: -0.1926
REMARK 3 S TENSOR
REMARK 3 S11: -0.0113 S12: 0.0325 S13: 0.0128
REMARK 3 S21: -0.0232 S22: -0.0129 S23: 0.0117
REMARK 3 S31: 0.0007 S32: 0.0455 S33: 0.0242
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 274 B 295
REMARK 3 ORIGIN FOR THE GROUP (A): 20.8248 3.0409 8.9535
REMARK 3 T TENSOR
REMARK 3 T11: 0.0382 T22: 0.0327
REMARK 3 T33: 0.0738 T12: -0.0045
REMARK 3 T13: 0.0101 T23: 0.0182
REMARK 3 L TENSOR
REMARK 3 L11: 0.7542 L22: 0.8729
REMARK 3 L33: 0.3525 L12: 0.0603
REMARK 3 L13: -0.1793 L23: -0.5279
REMARK 3 S TENSOR
REMARK 3 S11: 0.0523 S12: -0.0106 S13: 0.1418
REMARK 3 S21: -0.0287 S22: -0.0226 S23: 0.0300
REMARK 3 S31: 0.0184 S32: 0.0231 S33: -0.0298
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 296 B 322
REMARK 3 ORIGIN FOR THE GROUP (A): 11.2068 -4.2767 11.6063
REMARK 3 T TENSOR
REMARK 3 T11: 0.0360 T22: 0.0569
REMARK 3 T33: 0.0276 T12: -0.0086
REMARK 3 T13: 0.0021 T23: 0.0034
REMARK 3 L TENSOR
REMARK 3 L11: 0.5483 L22: 0.2625
REMARK 3 L33: 0.2785 L12: -0.3421
REMARK 3 L13: -0.1536 L23: 0.2020
REMARK 3 S TENSOR
REMARK 3 S11: 0.0150 S12: -0.0191 S13: 0.0504
REMARK 3 S21: -0.0065 S22: 0.0283 S23: -0.0463
REMARK 3 S31: 0.0089 S32: 0.0240 S33: -0.0433
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 : B 323 B 365
REMARK 3 ORIGIN FOR THE GROUP (A): -6.3870 -2.9776 13.8906
REMARK 3 T TENSOR
REMARK 3 T11: 0.0472 T22: 0.0488
REMARK 3 T33: 0.0279 T12: 0.0020
REMARK 3 T13: -0.0008 T23: 0.0044
REMARK 3 L TENSOR
REMARK 3 L11: 0.2726 L22: 0.0426
REMARK 3 L33: 0.2465 L12: 0.0571
REMARK 3 L13: -0.0039 L23: -0.0865
REMARK 3 S TENSOR
REMARK 3 S11: -0.0080 S12: 0.0080 S13: 0.0140
REMARK 3 S21: 0.0049 S22: 0.0143 S23: 0.0030
REMARK 3 S31: -0.0329 S32: -0.0309 S33: -0.0063
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 : B 366 B 396
REMARK 3 ORIGIN FOR THE GROUP (A): -6.9634 -0.3840 18.4720
REMARK 3 T TENSOR
REMARK 3 T11: 0.0473 T22: 0.0616
REMARK 3 T33: 0.0269 T12: 0.0148
REMARK 3 T13: 0.0139 T23: 0.0077
REMARK 3 L TENSOR
REMARK 3 L11: 0.1342 L22: 0.2949
REMARK 3 L33: 0.5364 L12: 0.1928
REMARK 3 L13: 0.1366 L23: 0.1862
REMARK 3 S TENSOR
REMARK 3 S11: 0.0140 S12: -0.0092 S13: 0.0255
REMARK 3 S21: 0.0297 S22: 0.0114 S23: 0.0501
REMARK 3 S31: -0.0533 S32: -0.0567 S33: -0.0255
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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 6C73 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-JAN-18.
REMARK 100 THE DEPOSITION ID IS D_1000232156.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-NOV-17
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) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : VARIMAX
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM 7.2.1
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.22
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 85206
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.650
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.04100
REMARK 200 R SYM (I) : 0.04100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.74
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : 0.18000
REMARK 200 R SYM FOR SHELL (I) : 0.18000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP 11.6.02
REMARK 200 STARTING MODEL: PDB ENTRY 4HT3
REMARK 200
REMARK 200 REMARK: LARGE PLATE-LIKE CRYSTAL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.07
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.51
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM BICINE-CSOH, PH 7.8, 5-10%
REMARK 280 PEG8000, 1 MM DTT, 1 MM EDTA, 2 MM F9F, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 298K
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 90.80450
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 29.49000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 90.80450
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 29.49000
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: 8570 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 44630 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.0 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 -5.15168
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 66.95209
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 NH2 ARG B 222 O HOH B 501 2.14
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 PHE A 212 120.62 102.83
REMARK 500 THR B 165 -158.43 -129.41
REMARK 500 GLU B 266 78.14 -100.58
REMARK 500 LEU B 304 30.50 -97.47
REMARK 500 SER B 308 -151.85 -145.51
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 746 DISTANCE = 6.84 ANGSTROMS
REMARK 525 HOH B1009 DISTANCE = 5.84 ANGSTROMS
REMARK 525 HOH B1010 DISTANCE = 5.85 ANGSTROMS
REMARK 525 HOH B1011 DISTANCE = 6.21 ANGSTROMS
REMARK 525 HOH B1012 DISTANCE = 6.28 ANGSTROMS
REMARK 525 HOH B1013 DISTANCE = 6.51 ANGSTROMS
REMARK 525 HOH B1014 DISTANCE = 6.65 ANGSTROMS
REMARK 525 HOH B1015 DISTANCE = 6.81 ANGSTROMS
REMARK 525 HOH B1016 DISTANCE = 7.18 ANGSTROMS
REMARK 525 HOH B1017 DISTANCE = 8.17 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 CS A 313 CS
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA A 167 O
REMARK 620 2 GLY A 170 O 86.8
REMARK 620 3 HOH A 671 O 146.9 90.8
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CS B 418 CS
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR B 66 O
REMARK 620 2 THR B 66 OG1 60.8
REMARK 620 3 THR B 69 O 74.0 128.0
REMARK 620 4 THR B 71 O 88.1 65.2 90.4
REMARK 620 5 HOH B 619 O 77.9 57.0 137.5 120.0
REMARK 620 6 HOH B 694 O 77.6 115.5 75.1 161.8 68.2
REMARK 620 7 HOH B 759 O 142.3 133.1 72.9 74.6 139.7 110.3
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CS B 417 CS
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL B 231 O
REMARK 620 2 GLY B 232 O 68.7
REMARK 620 3 GLU B 256 OE1 105.4 147.1
REMARK 620 4 GLY B 268 O 95.4 136.2 75.5
REMARK 620 5 SER B 308 O 135.1 66.5 110.8 118.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CS B 417 CS
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY B 232 O
REMARK 620 2 GLY B 268 O 145.6
REMARK 620 3 PHE B 306 O 88.3 124.1
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS 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 DMS A 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 308
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 309
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue F9F A 310
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 311
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 312
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CS A 313
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PLP B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS B 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS B 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS B 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS B 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS B 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS B 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS B 411
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS B 412
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 413
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 414
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 415
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 416
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CS B 417
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CS B 418
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4XUG RELATED DB: PDB
REMARK 900 TRYPTOPHAN SYNTHASE, INTERNAL ALDIMINE FORM WITH F9F INHIBITOR IN
REMARK 900 THE ALPHA-SUBUNIT
REMARK 900 RELATED ID: 4HN4 RELATED DB: PDB
REMARK 900 TRYPTOPHAN SYNTHASE, ALPHA AMINOACRYLATE E(A-A) FORM WITH F9F
REMARK 900 INHIBITOR IN THE ALPHA-SUBUNIT
REMARK 900 RELATED ID: 4HPJ RELATED DB: PDB
REMARK 900 TRYPTOPHAN SYNTHASE, COMPLEX WITH 2-AMINOPHENOL QUINONOID IN THE
REMARK 900 BETA SITE AND F9F INHIBITOR IN THE ALPHA-SUBUNIT
REMARK 900 RELATED ID: 4HPX RELATED DB: PDB
REMARK 900 TRYPTOPHAN SYNTHASE, COMPLEX WITH BENZIMIDAZOLE IN THE BETA-SUBUNIT
REMARK 900 AND F9F INHIBITOR IN THE ALPHA-SUBUNIT
REMARK 900 RELATED ID: 4HT3 RELATED DB: PDB
REMARK 900 TRYPTOPHAN SYNTHASE, INTERNAL ALDIMINE FORM WITH F9F INHIBITOR IN
REMARK 900 THE ALPHA-SUBUNIT
REMARK 900 RELATED ID: 5CGQ RELATED DB: PDB
REMARK 900 TRYPTOPHAN SYNTHASE, COMPLEX WITH F9F INHIBTOR IN THE ALPHA-SUBUNIT
REMARK 900 AND L-TRYPTOPHAN IN THE BETA-SUBUNIT
DBREF 6C73 A 1 268 UNP P00929 TRPA_SALTY 1 268
DBREF 6C73 B 2 396 UNP P0A2K1 TRPB_SALTY 2 396
SEQADV 6C73 ALA B 114 UNP P0A2K1 GLN 114 ENGINEERED MUTATION
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 395 THR THR LEU LEU ASN PRO TYR PHE GLY GLU PHE GLY GLY
SEQRES 2 B 395 MET TYR VAL PRO GLN ILE LEU MET PRO ALA LEU ASN GLN
SEQRES 3 B 395 LEU GLU GLU ALA PHE VAL SER ALA GLN LYS ASP PRO GLU
SEQRES 4 B 395 PHE GLN ALA GLN PHE ALA ASP LEU LEU LYS ASN TYR ALA
SEQRES 5 B 395 GLY ARG PRO THR ALA LEU THR LYS CYS GLN ASN ILE THR
SEQRES 6 B 395 ALA GLY THR ARG THR THR LEU TYR LEU LYS ARG GLU ASP
SEQRES 7 B 395 LEU LEU HIS GLY GLY ALA HIS LYS THR ASN GLN VAL LEU
SEQRES 8 B 395 GLY GLN ALA LEU LEU ALA LYS ARG MET GLY LYS SER GLU
SEQRES 9 B 395 ILE ILE ALA GLU THR GLY ALA GLY ALA HIS GLY VAL ALA
SEQRES 10 B 395 SER ALA LEU ALA SER ALA LEU LEU GLY LEU LYS CYS ARG
SEQRES 11 B 395 ILE TYR MET GLY ALA LYS ASP VAL GLU ARG GLN SER PRO
SEQRES 12 B 395 ASN VAL PHE ARG MET ARG LEU MET GLY ALA GLU VAL ILE
SEQRES 13 B 395 PRO VAL HIS SER GLY SER ALA THR LEU LYS ASP ALA CYS
SEQRES 14 B 395 ASN GLU ALA LEU ARG ASP TRP SER GLY SER TYR GLU THR
SEQRES 15 B 395 ALA HIS TYR MET LEU GLY THR ALA ALA GLY PRO HIS PRO
SEQRES 16 B 395 TYR PRO THR ILE VAL ARG GLU PHE GLN ARG MET ILE GLY
SEQRES 17 B 395 GLU GLU THR LYS ALA GLN ILE LEU ASP LYS GLU GLY ARG
SEQRES 18 B 395 LEU PRO ASP ALA VAL ILE ALA CYS VAL GLY GLY GLY SER
SEQRES 19 B 395 ASN ALA ILE GLY MET PHE ALA ASP PHE ILE ASN ASP THR
SEQRES 20 B 395 SER VAL GLY LEU ILE GLY VAL GLU PRO GLY GLY HIS GLY
SEQRES 21 B 395 ILE GLU THR GLY GLU HIS GLY ALA PRO LEU LYS HIS GLY
SEQRES 22 B 395 ARG VAL GLY ILE TYR PHE GLY MET LYS ALA PRO MET MET
SEQRES 23 B 395 GLN THR ALA ASP GLY GLN ILE GLU GLU SER TYR SER ILE
SEQRES 24 B 395 SER ALA GLY LEU ASP PHE PRO SER VAL GLY PRO GLN HIS
SEQRES 25 B 395 ALA TYR LEU ASN SER ILE GLY ARG ALA ASP TYR VAL SER
SEQRES 26 B 395 ILE THR ASP ASP GLU ALA LEU GLU ALA PHE LYS THR LEU
SEQRES 27 B 395 CYS ARG HIS GLU GLY ILE ILE PRO ALA LEU GLU SER SER
SEQRES 28 B 395 HIS ALA LEU ALA HIS ALA LEU LYS MET MET ARG GLU GLN
SEQRES 29 B 395 PRO GLU LYS GLU GLN LEU LEU VAL VAL ASN LEU SER GLY
SEQRES 30 B 395 ARG GLY ASP LYS ASP ILE PHE THR VAL HIS ASP ILE LEU
SEQRES 31 B 395 LYS ALA ARG GLY GLU
HET DMS A 301 4
HET DMS A 302 4
HET DMS A 303 4
HET DMS A 304 4
HET DMS A 305 4
HET DMS A 306 4
HET DMS A 307 4
HET DMS A 308 4
HET DMS A 309 4
HET F9F A 310 22
HET PEG A 311 7
HET EDO A 312 4
HET CS A 313 1
HET PLP B 401 15
HET DMS B 402 4
HET DMS B 403 4
HET DMS B 404 4
HET DMS B 405 4
HET DMS B 406 4
HET DMS B 407 4
HET DMS B 408 4
HET DMS B 409 4
HET DMS B 410 4
HET DMS B 411 4
HET DMS B 412 4
HET EDO B 413 4
HET EDO B 414 4
HET EDO B 415 4
HET EDO B 416 4
HET CS B 417 2
HET CS B 418 1
HET CS B 419 1
HET CL B 420 1
HETNAM DMS DIMETHYL SULFOXIDE
HETNAM F9F 2-({[4-(TRIFLUOROMETHOXY)PHENYL]SULFONYL}AMINO)ETHYL
HETNAM 2 F9F DIHYDROGEN PHOSPHATE
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM EDO 1,2-ETHANEDIOL
HETNAM CS CESIUM ION
HETNAM PLP PYRIDOXAL-5'-PHOSPHATE
HETNAM CL CHLORIDE ION
HETSYN F9F N-(4'-TRIFLUOROMETHOXYBENZENESULFONYL)-2-AMINO-1-
HETSYN 2 F9F ETHYLPHOSPHATE, F9
HETSYN EDO ETHYLENE GLYCOL
HETSYN PLP VITAMIN B6 PHOSPHATE
FORMUL 3 DMS 20(C2 H6 O S)
FORMUL 12 F9F C9 H11 F3 N O7 P S
FORMUL 13 PEG C4 H10 O3
FORMUL 14 EDO 5(C2 H6 O2)
FORMUL 15 CS 4(CS 1+)
FORMUL 16 PLP C8 H10 N O6 P
FORMUL 35 CL CL 1-
FORMUL 36 HOH *863(H2 O)
HELIX 1 AA1 MET A 1 ARG A 14 1 14
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 LEU A 193 TYR A 203 1 11
HELIX 11 AB2 SER A 216 ALA A 226 1 11
HELIX 12 AB3 GLY A 234 ASN A 244 1 11
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 ASP B 79 LEU B 81 5 3
HELIX 18 AB9 LYS B 87 MET B 101 1 15
HELIX 19 AC1 GLY B 113 GLY B 127 1 15
HELIX 20 AC2 ALA B 136 GLN B 142 1 7
HELIX 21 AC3 GLN B 142 MET B 152 1 11
HELIX 22 AC4 THR B 165 TYR B 181 1 17
HELIX 23 AC5 PRO B 196 PHE B 204 1 9
HELIX 24 AC6 ARG B 206 GLY B 221 1 16
HELIX 25 AC7 GLY B 234 ALA B 242 1 9
HELIX 26 AC8 ASP B 243 ILE B 245 5 3
HELIX 27 AC9 GLY B 261 GLY B 265 5 5
HELIX 28 AD1 ALA B 269 GLY B 274 1 6
HELIX 29 AD2 SER B 301 ASP B 305 5 5
HELIX 30 AD3 GLY B 310 ILE B 319 1 10
HELIX 31 AD4 ASP B 329 GLY B 344 1 16
HELIX 32 AD5 ALA B 348 GLN B 365 1 18
HELIX 33 AD6 GLY B 380 LYS B 382 5 3
HELIX 34 AD7 ASP B 383 GLY B 395 1 13
SHEET 1 AA1 9 ALA A 149 PRO A 150 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 50 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 VAL A 20
SHEET 7 AA1 9 ALA A 208 GLY A 211 1 N GLN A 210 O ILE A 232
SHEET 8 AA1 9 THR A 174 LEU A 177 1 N LEU A 176 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 TYR B 279 O MET B 282
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 VAL B 373
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 GLU B 155
SHEET 3 AA4 4 GLU B 105 THR B 110 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 GLU B 105
LINK NZ LYS B 87 C4A PLP B 401 1555 1555 1.27
LINK O ALA A 167 CS CS A 313 1555 1555 3.10
LINK O GLY A 170 CS CS A 313 1555 1555 3.17
LINK CS CS A 313 O HOH A 671 1555 1555 3.00
LINK O THR B 66 CS CS B 418 1555 1555 3.18
LINK OG1 THR B 66 CS CS B 418 1555 1555 3.29
LINK O THR B 69 CS CS B 418 1555 1555 3.15
LINK O THR B 71 CS CS B 418 1555 1555 3.04
LINK O VAL B 231 CS C CS B 417 1555 1555 3.29
LINK O GLY B 232 CS C CS B 417 1555 1555 2.92
LINK O GLY B 232 CS B CS B 417 1555 1555 3.15
LINK OE1 GLU B 256 CS C CS B 417 1555 1555 3.32
LINK O GLY B 268 CS C CS B 417 1555 1555 3.35
LINK O GLY B 268 CS B CS B 417 1555 1555 2.95
LINK O PHE B 306 CS B CS B 417 1555 1555 3.10
LINK O SER B 308 CS C CS B 417 1555 1555 3.40
LINK CS CS B 418 O HOH B 619 1555 1555 3.11
LINK CS CS B 418 O HOH B 694 1555 1555 3.35
LINK CS CS B 418 O HOH B 759 1555 1555 2.87
CISPEP 1 ASP A 27 PRO A 28 0 7.61
CISPEP 2 ARG B 55 PRO B 56 0 2.24
CISPEP 3 HIS B 195 PRO B 196 0 17.09
SITE 1 AC1 5 ILE A 41 HIS A 92 PRO A 93 THR A 94
SITE 2 AC1 5 ILE A 95
SITE 1 AC2 7 PHE A 139 ARG A 140 PRO A 150 ILE A 151
SITE 2 AC2 7 PHE A 152 HOH A 411 HOH A 444
SITE 1 AC3 5 LEU A 69 PHE A 72 HOH A 489 HOH A 493
SITE 2 AC3 5 GLY B 162
SITE 1 AC4 8 MET A 1 ARG A 3 VAL A 123 ASP A 124
SITE 2 AC4 8 HIS A 146 ASN A 147 ILE A 148 HOH A 497
SITE 1 AC5 3 LEU A 191 LEU A 193 HOH A 428
SITE 1 AC6 4 PHE A 82 ARG A 117 HOH A 405 HOH A 415
SITE 1 AC7 6 ASP A 38 LYS A 91 LEU A 144 ARG A 145
SITE 2 AC7 6 ASN A 147 HOH A 606
SITE 1 AC8 2 ARG A 15 GLU A 16
SITE 1 AC9 6 ARG A 267 ALA A 268 LYS B 99 LEU B 126
SITE 2 AC9 6 GLY B 127 HOH B 705
SITE 1 AD1 21 PHE A 22 GLU A 49 ALA A 59 ILE A 64
SITE 2 AD1 21 LEU A 100 LEU A 127 ALA A 129 ILE A 153
SITE 3 AD1 21 TYR A 175 THR A 183 GLY A 184 PHE A 212
SITE 4 AD1 21 GLY A 213 ILE A 232 GLY A 234 SER A 235
SITE 5 AD1 21 HOH A 414 HOH A 469 HOH A 528 HOH A 666
SITE 6 AD1 21 PRO B 18
SITE 1 AD2 10 ILE A 111 GLU A 135 PRO A 138 PHE A 139
SITE 2 AD2 10 HOH A 401 HOH A 403 HOH A 435 TYR B 16
SITE 3 AD2 10 LYS B 283 HOH B 539
SITE 1 AD3 5 PRO A 217 PHE A 258 HOH A 406 HOH A 611
SITE 2 AD3 5 GLU B 182
SITE 1 AD4 4 ALA A 167 GLY A 170 HIS A 204 HOH A 671
SITE 1 AD5 16 ALA B 85 HIS B 86 LYS B 87 THR B 190
SITE 2 AD5 16 CYS B 230 GLY B 232 GLY B 233 GLY B 234
SITE 3 AD5 16 SER B 235 ASN B 236 GLU B 350 SER B 377
SITE 4 AD5 16 GLY B 378 HOH B 544 HOH B 611 HOH B 634
SITE 1 AD6 5 TYR B 133 GLU B 172 ARG B 175 HOH B 567
SITE 2 AD6 5 HOH B 787
SITE 1 AD7 6 LYS B 50 GLY B 54 ARG B 55 PRO B 56
SITE 2 AD7 6 THR B 57 GLN B 215
SITE 1 AD8 4 GLN B 42 ALA B 46 HOH B 559 HOH B 816
SITE 1 AD9 5 LEU B 271 ASN B 317 ARG B 363 GLU B 364
SITE 2 AD9 5 HOH B 531
SITE 1 AE1 7 SER A 221 ARG A 225 ALA A 268 HOH A 702
SITE 2 AE1 7 LYS B 99 ARG B 100 HOH B 745
SITE 1 AE2 3 ILE B 262 HIS B 267 HIS B 273
SITE 1 AE3 4 THR B 3 LEU B 4 LEU B 5 ASN B 6
SITE 1 AE4 5 HIS B 273 MET B 287 GLN B 288 GLU B 295
SITE 2 AE4 5 HOH B 853
SITE 1 AE5 3 LYS B 37 PRO B 39 EDO B 416
SITE 1 AE6 2 ARG B 150 LEU B 391
SITE 1 AE7 4 SER B 143 ILE B 384 PHE B 385 HIS B 388
SITE 1 AE8 4 GLU B 11 PHE B 12 LYS B 283 HOH B 801
SITE 1 AE9 5 ILE B 65 HIS B 342 ARG B 363 HOH B 649
SITE 2 AE9 5 HOH B 650
SITE 1 AF1 4 ARG B 70 ILE B 319 GLU B 367 GLU B 369
SITE 1 AF2 4 GLN B 36 GLN B 42 DMS B 410 HOH B 557
SITE 1 AF3 7 VAL B 231 GLY B 232 GLU B 256 GLY B 268
SITE 2 AF3 7 PRO B 270 PHE B 306 SER B 308
SITE 1 AF4 4 THR B 66 THR B 69 THR B 71 HOH B 759
CRYST1 181.609 58.980 67.150 90.00 94.40 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 0.005506 0.000000 0.000424 0.00000
SCALE2 0.000000 0.016955 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014936 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
