HEADER LYASE/LYASE INHIBITOR 20-JUN-18 6DUC
TITLE CRYSTAL STRUCTURE OF MUTANT BETA-K167T TRYPTOPHAN SYNTHASE IN COMPLEX
TITLE 2 WITH INHIBITOR N-(4'-TRIFLUOROMETHOXYBENZENESULFONYL)-2-AMINO-1-
TITLE 3 ETHYLPHOSPHATE (F9F) AT THE ALPHA-SITE, CESIUM ION AT THE METAL
TITLE 4 COORDINATION SITE, AND 2-AMINOPHENOL QUINONOID (1D0) AT 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;
COMPND 11 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SALMONELLA TYPHIMURIUM;
SOURCE 3 ORGANISM_COMMON: SALMONELLA ENTERICA SUBSP. ENTERICA SEROVAR
SOURCE 4 TYPHIMURIUM;
SOURCE 5 ORGANISM_TAXID: 90371;
SOURCE 6 GENE: TRPA, DD95_04145;
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 TYPHIMURIUM;
SOURCE 14 ORGANISM_COMMON: SALMONELLA ENTERICA SUBSP. ENTERICA SEROVAR
SOURCE 15 TYPHIMURIUM;
SOURCE 16 ORGANISM_TAXID: 90371;
SOURCE 17 GENE: TRPB, DD95_04150;
SOURCE 18 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 19 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 20 EXPRESSION_SYSTEM_STRAIN: CB149;
SOURCE 21 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 22 EXPRESSION_SYSTEM_PLASMID: PEBA-10
KEYWDS F9F, 1D0, CESIUM ION, MUTANT BETA-K167T, LYASE, LYASE INHIBITOR, 2-
KEYWDS 2 AMINOPHENOL QUINONOID, SALMONELLA TYPHIMURIUM, LYASE-LYASE INHIBITOR
KEYWDS 3 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR E.HILARIO,M.F.DUNN,L.J.MUELLER,L.FAN
REVDAT 3 11-OCT-23 6DUC 1 LINK
REVDAT 2 18-DEC-19 6DUC 1 REMARK
REVDAT 1 26-JUN-19 6DUC 0
JRNL AUTH E.HILARIO,M.F.DUNN,L.J.MUELLER,L.FAN
JRNL TITL TRYPTOPHAN SYNTHASE Q114A MUTANT IN COMPLEX WITH INHIBITOR
JRNL TITL 2 N-(4'-TRIFLUOROMETHOXYBENZENESULFONYL)
JRNL TITL 3 -2-AMINO-1-ETHYLPHOSPHATE (F9F) AT THE ALPHA-SITE,
JRNL TITL 4 AMINOACRYLATE (P1T) AT THE BETA SITE, AND CESIUM ION AT THE
JRNL TITL 5 METAL COORDINATION SITE.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.79 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.13-2998
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.79
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.70
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 3 NUMBER OF REFLECTIONS : 67592
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.188
REMARK 3 R VALUE (WORKING SET) : 0.185
REMARK 3 FREE R VALUE : 0.232
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 3515
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 19.7046 - 5.2057 0.99 2724 125 0.1905 0.2074
REMARK 3 2 5.2057 - 4.1445 1.00 2673 141 0.1540 0.1920
REMARK 3 3 4.1445 - 3.6243 1.00 2633 148 0.1597 0.2006
REMARK 3 4 3.6243 - 3.2946 0.99 2613 147 0.1735 0.2281
REMARK 3 5 3.2946 - 3.0594 1.00 2602 147 0.1719 0.2220
REMARK 3 6 3.0594 - 2.8796 1.00 2651 149 0.1749 0.2272
REMARK 3 7 2.8796 - 2.7358 1.00 2575 165 0.1795 0.2432
REMARK 3 8 2.7358 - 2.6170 1.00 2610 135 0.1834 0.2469
REMARK 3 9 2.6170 - 2.5164 1.00 2621 157 0.1801 0.2194
REMARK 3 10 2.5164 - 2.4298 1.00 2616 132 0.1852 0.2571
REMARK 3 11 2.4298 - 2.3539 1.00 2628 139 0.1748 0.2355
REMARK 3 12 2.3539 - 2.2867 1.00 2585 153 0.1704 0.2035
REMARK 3 13 2.2867 - 2.2266 0.99 2571 145 0.1745 0.2187
REMARK 3 14 2.2266 - 2.1724 1.00 2604 157 0.1764 0.2294
REMARK 3 15 2.1724 - 2.1230 1.00 2627 151 0.1800 0.2219
REMARK 3 16 2.1230 - 2.0779 1.00 2571 143 0.1882 0.2479
REMARK 3 17 2.0779 - 2.0364 1.00 2601 151 0.1960 0.2481
REMARK 3 18 2.0364 - 1.9980 1.00 2571 153 0.2024 0.2501
REMARK 3 19 1.9980 - 1.9623 1.00 2629 130 0.2081 0.2746
REMARK 3 20 1.9623 - 1.9291 1.00 2593 136 0.2294 0.2845
REMARK 3 21 1.9291 - 1.8980 0.99 2637 119 0.2520 0.3251
REMARK 3 22 1.8980 - 1.8688 0.93 2366 156 0.2742 0.3076
REMARK 3 23 1.8688 - 1.8414 0.93 2442 115 0.2729 0.2943
REMARK 3 24 1.8414 - 1.8155 0.94 2462 120 0.2751 0.3195
REMARK 3 25 1.8155 - 1.7909 0.71 1872 101 0.3228 0.3481
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.200
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.920
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 16.76
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.55
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 8
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 159 )
REMARK 3 ORIGIN FOR THE GROUP (A): 40.1475 10.3184 8.8371
REMARK 3 T TENSOR
REMARK 3 T11: -0.1118 T22: 0.1111
REMARK 3 T33: 0.1327 T12: -0.1140
REMARK 3 T13: 0.0877 T23: 0.0819
REMARK 3 L TENSOR
REMARK 3 L11: 0.0044 L22: 0.0110
REMARK 3 L33: 0.0007 L12: 0.0109
REMARK 3 L13: 0.0016 L23: -0.0048
REMARK 3 S TENSOR
REMARK 3 S11: 0.1029 S12: 0.0330 S13: 0.0149
REMARK 3 S21: 0.0483 S22: -0.0437 S23: 0.0186
REMARK 3 S31: 0.0222 S32: 0.0345 S33: 0.0000
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 160 THROUGH 202 )
REMARK 3 ORIGIN FOR THE GROUP (A): 46.3313 -1.3741 21.1162
REMARK 3 T TENSOR
REMARK 3 T11: 0.1726 T22: 0.2281
REMARK 3 T33: 0.2559 T12: -0.0210
REMARK 3 T13: -0.0778 T23: 0.0460
REMARK 3 L TENSOR
REMARK 3 L11: 0.0016 L22: 0.0010
REMARK 3 L33: 0.0004 L12: 0.0000
REMARK 3 L13: 0.0006 L23: -0.0010
REMARK 3 S TENSOR
REMARK 3 S11: 0.0120 S12: -0.0039 S13: -0.0139
REMARK 3 S21: 0.0157 S22: -0.0033 S23: -0.0008
REMARK 3 S31: -0.0101 S32: 0.0067 S33: 0.0000
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 203 THROUGH 268 )
REMARK 3 ORIGIN FOR THE GROUP (A): 46.7028 17.4806 21.5062
REMARK 3 T TENSOR
REMARK 3 T11: 0.2587 T22: 0.2742
REMARK 3 T33: 0.2888 T12: -0.1059
REMARK 3 T13: -0.0365 T23: 0.0576
REMARK 3 L TENSOR
REMARK 3 L11: 0.0051 L22: 0.0022
REMARK 3 L33: 0.0000 L12: 0.0051
REMARK 3 L13: 0.0006 L23: 0.0003
REMARK 3 S TENSOR
REMARK 3 S11: 0.0153 S12: -0.0138 S13: -0.0089
REMARK 3 S21: 0.0107 S22: -0.0002 S23: -0.0003
REMARK 3 S31: -0.0175 S32: 0.0002 S33: 0.0000
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 2 THROUGH 37 )
REMARK 3 ORIGIN FOR THE GROUP (A): 27.7800 -12.9423 19.7619
REMARK 3 T TENSOR
REMARK 3 T11: 0.0499 T22: 0.1181
REMARK 3 T33: 0.0557 T12: 0.0388
REMARK 3 T13: -0.0184 T23: 0.0283
REMARK 3 L TENSOR
REMARK 3 L11: 0.0016 L22: -0.0012
REMARK 3 L33: 0.0006 L12: -0.0019
REMARK 3 L13: -0.0014 L23: -0.0012
REMARK 3 S TENSOR
REMARK 3 S11: 0.0277 S12: -0.0023 S13: -0.0238
REMARK 3 S21: 0.0059 S22: 0.0042 S23: -0.0128
REMARK 3 S31: -0.0033 S32: 0.0126 S33: 0.0000
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 38 THROUGH 70 )
REMARK 3 ORIGIN FOR THE GROUP (A): 1.6640 -17.6189 28.2837
REMARK 3 T TENSOR
REMARK 3 T11: 0.0390 T22: 0.0655
REMARK 3 T33: 0.0015 T12: 0.0106
REMARK 3 T13: -0.0296 T23: 0.0277
REMARK 3 L TENSOR
REMARK 3 L11: 0.0032 L22: 0.0018
REMARK 3 L33: 0.0031 L12: 0.0004
REMARK 3 L13: -0.0069 L23: -0.0037
REMARK 3 S TENSOR
REMARK 3 S11: -0.0234 S12: 0.0062 S13: -0.0102
REMARK 3 S21: 0.0352 S22: -0.0289 S23: -0.0038
REMARK 3 S31: 0.0312 S32: -0.0177 S33: 0.0000
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 71 THROUGH 196 )
REMARK 3 ORIGIN FOR THE GROUP (A): 14.0387 -1.7019 29.3460
REMARK 3 T TENSOR
REMARK 3 T11: -0.0338 T22: 0.0520
REMARK 3 T33: -0.2905 T12: -0.0137
REMARK 3 T13: 0.1594 T23: -0.0332
REMARK 3 L TENSOR
REMARK 3 L11: -0.0053 L22: -0.0029
REMARK 3 L33: 0.0081 L12: 0.0034
REMARK 3 L13: 0.0013 L23: -0.0063
REMARK 3 S TENSOR
REMARK 3 S11: 0.1513 S12: -0.0050 S13: 0.0058
REMARK 3 S21: -0.0569 S22: 0.0816 S23: 0.0176
REMARK 3 S31: -0.0363 S32: 0.0154 S33: -0.0000
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 197 THROUGH 365 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.2557 -6.9368 12.9337
REMARK 3 T TENSOR
REMARK 3 T11: 0.0343 T22: -0.0016
REMARK 3 T33: -0.0039 T12: 0.0224
REMARK 3 T13: -0.0096 T23: 0.0355
REMARK 3 L TENSOR
REMARK 3 L11: 0.0005 L22: 0.0074
REMARK 3 L33: 0.0184 L12: 0.0045
REMARK 3 L13: 0.0088 L23: 0.0008
REMARK 3 S TENSOR
REMARK 3 S11: 0.0343 S12: 0.0118 S13: 0.1562
REMARK 3 S21: 0.0262 S22: -0.0304 S23: 0.0004
REMARK 3 S31: 0.0771 S32: -0.0156 S33: 0.0000
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 366 THROUGH 395 )
REMARK 3 ORIGIN FOR THE GROUP (A): -6.4509 -1.9735 18.4669
REMARK 3 T TENSOR
REMARK 3 T11: 0.0644 T22: 0.0374
REMARK 3 T33: 0.0207 T12: 0.0074
REMARK 3 T13: 0.0094 T23: 0.0137
REMARK 3 L TENSOR
REMARK 3 L11: -0.0003 L22: -0.0002
REMARK 3 L33: 0.0031 L12: 0.0023
REMARK 3 L13: -0.0014 L23: -0.0014
REMARK 3 S TENSOR
REMARK 3 S11: 0.0233 S12: -0.0016 S13: -0.0064
REMARK 3 S21: 0.0012 S22: 0.0148 S23: 0.0005
REMARK 3 S31: -0.0006 S32: -0.0086 S33: 0.0000
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6DUC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-JUN-18.
REMARK 100 THE DEPOSITION ID IS D_1000235255.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-MAR-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.8-8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : BENT CYLINDERS, STRIPES OF PT,
REMARK 200 RH, AND CLEAR
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM 7.2.1
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.22
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 67697
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.791
REMARK 200 RESOLUTION RANGE LOW (A) : 91.827
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : 8.000
REMARK 200 R MERGE (I) : 0.21500
REMARK 200 R SYM (I) : 0.21500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.3
REMARK 200 DATA REDUNDANCY IN SHELL : 4.40
REMARK 200 R MERGE FOR SHELL (I) : 0.52200
REMARK 200 R SYM FOR SHELL (I) : 0.52200
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.8.2, DM 7.0.058
REMARK 200 STARTING MODEL: PDB ENTRY 4HPJ
REMARK 200
REMARK 200 REMARK: LARGE PLATE-LIKE CRYSTAL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM BICINE-CS, 10-12% PEG3350, 50 MM
REMARK 280 CESIUM CHLORIDE, 4-8 MM SPERMINE, PH 7.9, VAPOR DIFFUSION,
REMARK 280 SITTING 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 92.13050
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 30.02200
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 92.13050
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 30.02200
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: 17160 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 42600 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -348.0 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 -5.45576
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 67.07649
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 CS CS B 412 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 678 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A 189
REMARK 465 ALA A 190
REMARK 465 LEU A 191
REMARK 465 MET B 1
REMARK 465 ILE B 397
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLU A 2 CG CD OE1 OE2
REMARK 470 ARG A 14 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 15 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 32 CG CD OE1 NE2
REMARK 470 GLU A 186 CG CD OE1 OE2
REMARK 470 ASN A 187 CG OD1 ND2
REMARK 470 ARG A 188 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 193 CG CD1 CD2
REMARK 470 HIS A 194 CG ND1 CD2 CE1 NE2
REMARK 470 GLU A 218 CG CD OE1 OE2
REMARK 470 GLU A 242 CG CD OE1 OE2
REMARK 470 LYS A 243 CG CD CE NZ
REMARK 470 LEU B 391 CG CD1 CD2
REMARK 470 LYS B 392 CG CD CE NZ
REMARK 470 GLU B 396 CG CD OE1 OE2
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 OE2 GLU B 30 O HOH B 501 1.75
REMARK 500 O HOH A 409 O HOH A 461 1.99
REMARK 500 OE2 GLU B 367 O HOH B 502 2.04
REMARK 500 NH1 ARG B 379 O HOH B 503 2.08
REMARK 500 O ARG A 225 O HOH A 401 2.08
REMARK 500 OE2 GLU B 367 O HOH B 502 2.11
REMARK 500 OE2 GLU B 172 O HOH B 504 2.14
REMARK 500 OG1 THR A 63 O HOH A 402 2.16
REMARK 500 OE1 GLU B 140 O HOH B 505 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 NH2 ARG A 225 O ARG B 100 4556 2.06
REMARK 500
REMARK 500 REMARK: NULL
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 LEU A 58 CB - CG - CD2 ANGL. DEV. = -10.2 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 ASN A 157 76.93 -101.04
REMARK 500 PHE A 212 84.15 74.97
REMARK 500 THR B 165 -164.77 -129.59
REMARK 500 ALA B 191 57.40 -92.26
REMARK 500 ALA B 269 66.44 -119.20
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 557 DISTANCE = 6.31 ANGSTROMS
REMARK 525 HOH B 860 DISTANCE = 6.09 ANGSTROMS
REMARK 525 HOH B 861 DISTANCE = 6.09 ANGSTROMS
REMARK 525 HOH B 862 DISTANCE = 7.50 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 B 412 CS
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY B 54 O
REMARK 620 2 GLY B 54 O 0.0
REMARK 620 3 PRO B 56 O 63.5 63.5
REMARK 620 4 PRO B 56 O 63.5 63.5 0.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CS B 411 CS
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR B 66 O
REMARK 620 2 THR B 66 OG1 58.1
REMARK 620 3 THR B 69 O 73.8 125.2
REMARK 620 4 THR B 71 O 87.9 63.8 91.5
REMARK 620 5 HOH B 702 O 78.8 59.5 137.1 120.0
REMARK 620 6 HOH B 779 O 125.7 69.7 158.8 82.0 61.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CS B 410 CS
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL B 231 O
REMARK 620 2 GLY B 232 O 70.7
REMARK 620 3 GLY B 268 O 97.4 120.5
REMARK 620 4 SER B 308 O 137.6 68.0 111.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CS B 410 CS
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY B 232 O
REMARK 620 2 GLY B 268 O 167.9
REMARK 620 3 LEU B 304 O 92.9 87.4
REMARK 620 4 PHE B 306 O 105.2 86.8 79.2
REMARK 620 5 SER B 308 O 69.0 117.9 138.6 70.9
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 F9F 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 EDO A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 1D0 B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 2AP B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS B 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS B 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS B 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CS B 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CS B 411
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CS B 412
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 415
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 416
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 418
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 420
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 421
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4HPJ RELATED DB: PDB
REMARK 900 TRYPTOPHAN SYNTHASE AT 1.45 A RESOLUTION IN COMPLEX WITH 2-
REMARK 900 AMINOPHENOL QUINONOID IN THE BETA SITE AND THE F9 INHIBITOR IN THE
REMARK 900 ALPHA SITE
DBREF1 6DUC A 1 268 UNP A0A0D6FWC1_SALTM
DBREF2 6DUC A A0A0D6FWC1 1 268
DBREF1 6DUC B 1 397 UNP A0A0J0ZFZ1_SALTM
DBREF2 6DUC B A0A0J0ZFZ1 1 397
SEQADV 6DUC THR B 167 UNP A0A0J0ZFZ LYS 167 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 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 THR 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 F9F A 301 22
HET DMS A 302 4
HET EDO A 303 4
HET CL A 304 1
HET CL A 305 1
HET 1D0 B 401 29
HET DMS B 402 4
HET 2AP B 403 7
HET DMS B 404 4
HET DMS B 405 4
HET DMS B 406 4
HET EDO B 407 4
HET EDO B 408 4
HET DMS B 409 4
HET CS B 410 2
HET CS B 411 1
HET CS B 412 1
HET CL B 413 1
HET CL B 414 1
HET CL B 415 1
HET CL B 416 1
HET CL B 417 1
HET CL B 418 1
HET CL B 419 1
HET CL B 420 1
HET CL B 421 1
HETNAM F9F 2-({[4-(TRIFLUOROMETHOXY)PHENYL]SULFONYL}AMINO)ETHYL
HETNAM 2 F9F DIHYDROGEN PHOSPHATE
HETNAM DMS DIMETHYL SULFOXIDE
HETNAM EDO 1,2-ETHANEDIOL
HETNAM CL CHLORIDE ION
HETNAM 1D0 (2E)-2-[({3-HYDROXY-2-METHYL-5-[(PHOSPHONOOXY)
HETNAM 2 1D0 METHYL]PYRIDIN-4-YL}METHYL)IMINO]-3-[(2-
HETNAM 3 1D0 HYDROXYPHENYL)AMINO]PROPANOIC ACID
HETNAM 2AP 2-AMINOPYRIDINE
HETNAM CS CESIUM ION
HETSYN F9F N-(4'-TRIFLUOROMETHOXYBENZENESULFONYL)-2-AMINO-1-
HETSYN 2 F9F ETHYLPHOSPHATE, F9
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 F9F C9 H11 F3 N O7 P S
FORMUL 4 DMS 6(C2 H6 O S)
FORMUL 5 EDO 3(C2 H6 O2)
FORMUL 6 CL 11(CL 1-)
FORMUL 8 1D0 C17 H20 N3 O8 P
FORMUL 10 2AP C5 H7 N2 1+
FORMUL 17 CS 3(CS 1+)
FORMUL 29 HOH *519(H2 O)
HELIX 1 AA1 MET A 1 ASP A 13 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 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 SER A 266 1 20
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 GLY B 179 1 15
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 ARG B 394 1 12
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 LEU A 99 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 ARG B 275 O MET B 286
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 VAL B 374 N TYR B 74
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 ILE B 157
SHEET 3 AA4 4 GLU B 105 THR B 110 1 N ILE B 106 O LYS B 129
SHEET 4 AA4 4 ALA B 184 TYR B 186 1 O HIS B 185 N GLU B 105
LINK O GLY B 54 CS CS B 412 1555 1555 3.18
LINK O GLY B 54 CS CS B 412 1555 2556 3.18
LINK O PRO B 56 CS CS B 412 1555 1555 2.93
LINK O PRO B 56 CS CS B 412 1555 2556 2.93
LINK O THR B 66 CS CS B 411 1555 1555 3.20
LINK OG1 THR B 66 CS CS B 411 1555 1555 3.23
LINK O THR B 69 CS CS B 411 1555 1555 3.22
LINK O THR B 71 CS CS B 411 1555 1555 2.96
LINK O VAL B 231 CS B CS B 410 1555 1555 3.22
LINK O GLY B 232 CS A CS B 410 1555 1555 2.85
LINK O GLY B 232 CS B CS B 410 1555 1555 3.21
LINK O GLY B 268 CS A CS B 410 1555 1555 2.92
LINK O GLY B 268 CS B CS B 410 1555 1555 3.40
LINK O LEU B 304 CS A CS B 410 1555 1555 3.45
LINK O PHE B 306 CS A CS B 410 1555 1555 3.00
LINK O SER B 308 CS A CS B 410 1555 1555 3.36
LINK O SER B 308 CS B CS B 410 1555 1555 3.12
LINK CS CS B 411 O HOH B 702 1555 1555 3.04
LINK CS CS B 411 O HOH B 779 1555 1555 3.37
CISPEP 1 ASP A 27 PRO A 28 0 6.15
CISPEP 2 ARG B 55 PRO B 56 0 -2.57
CISPEP 3 HIS B 195 PRO B 196 0 16.19
SITE 1 AC1 19 PHE A 22 GLU A 49 ALA A 59 ILE A 64
SITE 2 AC1 19 LEU A 100 LEU A 127 ALA A 129 ILE A 153
SITE 3 AC1 19 TYR A 175 THR A 183 GLY A 184 PHE A 212
SITE 4 AC1 19 GLY A 213 ILE A 232 GLY A 234 SER A 235
SITE 5 AC1 19 HOH A 405 HOH A 424 PRO B 18
SITE 1 AC2 8 MET A 1 ARG A 3 GLU A 119 VAL A 123
SITE 2 AC2 8 ASP A 124 HIS A 146 ASN A 147 ILE A 148
SITE 1 AC3 3 ALA A 113 ALA A 116 HOH A 498
SITE 1 AC4 3 ILE A 41 ALA A 45 HOH A 430
SITE 1 AC5 3 ALA A 167 GLY A 170 HIS A 204
SITE 1 AC6 22 HIS B 86 LYS B 87 GLU B 109 THR B 110
SITE 2 AC6 22 GLY B 111 ALA B 112 GLY B 113 GLN B 114
SITE 3 AC6 22 HIS B 115 LEU B 166 THR B 190 CYS B 230
SITE 4 AC6 22 GLY B 232 GLY B 233 GLY B 234 SER B 235
SITE 5 AC6 22 ASN B 236 GLY B 303 GLU B 350 SER B 377
SITE 6 AC6 22 GLY B 378 HOH B 589
SITE 1 AC7 2 GLU B 331 HOH B 563
SITE 1 AC8 3 THR B 3 LEU B 4 ASN B 6
SITE 1 AC9 1 GLN B 42
SITE 1 AD1 8 LYS B 50 GLY B 54 ARG B 55 PRO B 56
SITE 2 AD1 8 THR B 57 ALA B 58 GLN B 215 CS B 412
SITE 1 AD2 6 SER A 180 GLY B 179 SER B 180 TYR B 181
SITE 2 AD2 6 GLU B 182 HOH B 716
SITE 1 AD3 3 MET B 287 GLN B 288 HOH B 601
SITE 1 AD4 7 LEU B 48 TYR B 52 THR B 60 LYS B 61
SITE 2 AD4 7 GLN B 63 LEU B 125 GLU B 343
SITE 1 AD5 4 LEU B 271 ASN B 317 ARG B 363 GLU B 364
SITE 1 AD6 7 VAL B 231 GLY B 232 GLU B 256 GLY B 268
SITE 2 AD6 7 LEU B 304 PHE B 306 SER B 308
SITE 1 AD7 4 THR B 66 THR B 69 THR B 71 HOH B 702
SITE 1 AD8 3 GLY B 54 PRO B 56 DMS B 405
SITE 1 AD9 2 GLU B 369 HOH B 729
SITE 1 AE1 2 LYS B 219 HOH B 738
SITE 1 AE2 2 ARG B 275 ALA B 290
SITE 1 AE3 1 GLN B 36
SITE 1 AE4 4 VAL B 325 SER B 326 HOH B 726 HOH B 856
CRYST1 184.261 60.044 67.298 90.00 94.65 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 0.005427 0.000000 0.000442 0.00000
SCALE2 0.000000 0.016655 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014908 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
