HEADER LYASE 08-OCT-07 2RH9
TITLE TRYPTOPHAN SYNTHASE COMPLEXED WITH IGP, INTERNAL ALDIMINE, PH 9.0
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRYPTOPHAN SYNTHASE ALPHA CHAIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: TRYPTOPHAN SYNTHASE, ALPHA CHAIN;
COMPND 5 EC: 4.2.1.20;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: TRYPTOPHAN SYNTHASE BETA CHAIN;
COMPND 9 CHAIN: B;
COMPND 10 FRAGMENT: TRYPTOPHAN SYNTHASE, BETA CHAIN;
COMPND 11 EC: 4.2.1.20;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SALMONELLA TYPHIMURIUM;
SOURCE 3 ORGANISM_TAXID: 602;
SOURCE 4 GENE: TRPA, STM1727;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: CB149;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PSTB7;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: SALMONELLA TYPHIMURIUM;
SOURCE 12 ORGANISM_TAXID: 602;
SOURCE 13 GENE: TRPB, STM1726;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 16 EXPRESSION_SYSTEM_STRAIN: CB149;
SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PSTB7
KEYWDS AROMATIC AMINO ACID BIOSYNTHESIS, TRYPTOPHAN BIOSYNTHESIS, CARBON-
KEYWDS 2 OXYGEN LYASE, AMINOACID BIOSYNTHESIS, LYASE, ALLOSTERIC ENZYME,
KEYWDS 3 PYRIDOXAL PHOSPHATE, AMINO-ACID BIOSYNTHESIS
EXPDTA X-RAY DIFFRACTION
AUTHOR V.KULIK,T.R.M.BARENDS,I.SCHLICHTING
REVDAT 3 13-JUL-11 2RH9 1 VERSN
REVDAT 2 24-FEB-09 2RH9 1 VERSN
REVDAT 1 06-NOV-07 2RH9 0
JRNL AUTH V.KULIK,T.R.M.BARENDS,I.SCHLICHTING
JRNL TITL TRYPTOPHAN SYNTHASE COMPLEXED WITH IGP, INTERNAL ALDIMINE,
JRNL TITL 2 PH 9.0.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.73
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 73246
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.173
REMARK 3 R VALUE (WORKING SET) : 0.172
REMARK 3 FREE R VALUE : 0.200
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3922
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) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.74
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5384
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2390
REMARK 3 BIN FREE R VALUE SET COUNT : 296
REMARK 3 BIN FREE R VALUE : 0.2430
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4895
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 35
REMARK 3 SOLVENT ATOMS : 483
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 19.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.99
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.80000
REMARK 3 B22 (A**2) : 2.19000
REMARK 3 B33 (A**2) : -1.46000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.41000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.097
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.095
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.068
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.066
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.963
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.951
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5082 ; 0.011 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 4660 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6888 ; 1.426 ; 1.979
REMARK 3 BOND ANGLES OTHERS (DEGREES): 10841 ; 0.924 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 650 ; 5.407 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 219 ;35.480 ;24.110
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 836 ;13.281 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 32 ;19.246 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 762 ; 0.075 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5720 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 993 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1028 ; 0.219 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 4620 ; 0.185 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2476 ; 0.177 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 2725 ; 0.084 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 378 ; 0.131 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 3 ; 0.098 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 7 ; 0.135 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 58 ; 0.227 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 11 ; 0.115 ; 0.200
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): 3236 ; 0.714 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1332 ; 0.180 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5164 ; 1.308 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1877 ; 2.090 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1724 ; 3.452 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS. PROGRAM CNS HAS ALSO BEEN USED IN REFINEMENT
REMARK 4
REMARK 4 2RH9 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-OCT-07.
REMARK 100 THE RCSB ID CODE IS RCSB044857.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-SEP-00
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 9.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.93000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 77139
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 55.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.3
REMARK 200 DATA REDUNDANCY : 2.400
REMARK 200 R MERGE (I) : 0.05500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.0100
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.1
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.31300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.460
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.63
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN: 50 MM BICINE PH 7.8, 10 MM NA
REMARK 280 -EDTA, 1 MM DTE, 20 UM PLP. RESERVOIR: 50 MM BICINE PH 7.8, 5 MM
REMARK 280 DTE, 5 MM NA-EDTA, 0.1 M PLP, 2 MM SPERMINE, 2 MM NAN3, 8-12% PEG
REMARK 280 8000. CRYSTAL SOAKED IN 15% PEG 8000, 20% GLYCEROL, 23 MM IGP, PH
REMARK 280 CONTROLLED AT PH 9.0 BEFORE FLASH-COOLING, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 293K
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 91.53550
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 29.64050
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 91.53550
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 29.64050
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: 10950 ANGSTROM**2
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 183.07100
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 LEU A 191
REMARK 465 PRO A 192
REMARK 465 MET B 1
REMARK 465 GLU B 396
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 PHE A 212 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASP B 305 CG OD1 OD2
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 691 2.19
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 31.13 -78.45
REMARK 500 PHE A 212 111.18 93.63
REMARK 500 SER B 308 -155.96 -138.77
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 429 DISTANCE = 5.13 ANGSTROMS
REMARK 525 HOH B 503 DISTANCE = 5.07 ANGSTROMS
REMARK 525 HOH B 512 DISTANCE = 5.11 ANGSTROMS
REMARK 525 HOH B 569 DISTANCE = 5.06 ANGSTROMS
REMARK 525 HOH B 622 DISTANCE = 5.16 ANGSTROMS
REMARK 525 HOH B 704 DISTANCE = 5.36 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 398 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY B 232 O
REMARK 620 2 PHE B 306 O 110.7
REMARK 620 3 SER B 308 O 92.2 87.8
REMARK 620 4 HOH B 425 O 85.4 161.9 100.1
REMARK 620 5 HOH B 488 O 118.0 70.8 147.3 94.7
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 NA B 398
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IGP A 269
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP B 399
DBREF 2RH9 A 1 268 UNP P00929 TRPA_SALTY 1 268
DBREF 2RH9 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 NA B 398 1
HET IGP A 269 19
HET PLP B 399 15
HETNAM NA SODIUM ION
HETNAM IGP INDOLE-3-GLYCEROL PHOSPHATE
HETNAM PLP PYRIDOXAL-5'-PHOSPHATE
HETSYN PLP VITAMIN B6 PHOSPHATE
FORMUL 3 NA NA 1+
FORMUL 4 IGP C11 H14 N O6 P
FORMUL 5 PLP C8 H10 N O6 P
FORMUL 6 HOH *483(H2 O)
HELIX 1 1 MET A 1 ARG A 14 1 14
HELIX 2 2 GLY A 29 ALA A 43 1 15
HELIX 3 3 GLY A 61 ALA A 74 1 14
HELIX 4 4 THR A 77 HIS A 92 1 16
HELIX 5 5 TYR A 102 ASN A 108 1 7
HELIX 6 6 GLY A 110 GLY A 122 1 13
HELIX 7 7 PRO A 132 GLU A 135 5 4
HELIX 8 8 SER A 136 HIS A 146 1 11
HELIX 9 9 ASP A 159 GLY A 170 1 12
HELIX 10 10 LEU A 193 TYR A 203 1 11
HELIX 11 11 SER A 216 ALA A 226 1 11
HELIX 12 12 GLY A 234 ASN A 244 1 11
HELIX 13 13 SER A 247 ALA A 265 1 19
HELIX 14 14 PRO B 18 ILE B 20 5 3
HELIX 15 15 LEU B 21 LYS B 37 1 17
HELIX 16 16 ASP B 38 TYR B 52 1 15
HELIX 17 17 ASP B 79 LEU B 81 5 3
HELIX 18 18 LYS B 87 MET B 101 1 15
HELIX 19 19 GLY B 113 GLY B 127 1 15
HELIX 20 20 ALA B 136 GLN B 142 1 7
HELIX 21 21 GLN B 142 MET B 152 1 11
HELIX 22 22 THR B 165 TYR B 181 1 17
HELIX 23 23 PRO B 196 ARG B 206 1 11
HELIX 24 24 ARG B 206 GLY B 221 1 16
HELIX 25 25 GLY B 234 ALA B 242 1 9
HELIX 26 26 ASP B 243 ILE B 245 5 3
HELIX 27 27 GLY B 261 GLY B 265 5 5
HELIX 28 28 ALA B 269 GLY B 274 1 6
HELIX 29 29 SER B 301 ASP B 305 5 5
HELIX 30 30 GLY B 310 ILE B 319 1 10
HELIX 31 31 ASP B 329 GLY B 344 1 16
HELIX 32 32 ALA B 348 GLN B 365 1 18
HELIX 33 33 GLY B 380 LYS B 382 5 3
HELIX 34 34 ASP B 383 GLY B 395 1 13
SHEET 1 A 9 ALA A 149 ILE A 151 0
SHEET 2 A 9 SER A 125 VAL A 128 1 N VAL A 126 O ILE A 151
SHEET 3 A 9 ILE A 97 MET A 101 1 N MET A 101 O LEU A 127
SHEET 4 A 9 LEU A 48 GLY A 51 1 N LEU A 48 O GLY A 98
SHEET 5 A 9 ALA A 18 THR A 24 1 N VAL A 23 O GLY A 51
SHEET 6 A 9 GLY A 230 SER A 233 1 O ALA A 231 N VAL A 20
SHEET 7 A 9 ALA A 208 GLY A 211 1 N GLN A 210 O ILE A 232
SHEET 8 A 9 THR A 174 LEU A 177 1 N THR A 174 O LEU A 209
SHEET 9 A 9 ILE A 153 CYS A 154 1 N CYS A 154 O TYR A 175
SHEET 1 B 4 TYR B 8 PHE B 9 0
SHEET 2 B 4 PHE B 12 TYR B 16 -1 O PHE B 12 N PHE B 9
SHEET 3 B 4 GLY B 281 MET B 286 -1 O LYS B 283 N GLY B 13
SHEET 4 B 4 ARG B 275 TYR B 279 -1 N TYR B 279 O MET B 282
SHEET 1 C 6 LEU B 59 LYS B 61 0
SHEET 2 C 6 THR B 71 ARG B 77 -1 O LEU B 75 N THR B 60
SHEET 3 C 6 GLN B 370 LEU B 376 1 O GLN B 370 N THR B 72
SHEET 4 C 6 ALA B 226 CYS B 230 1 N ILE B 228 O ASN B 375
SHEET 5 C 6 GLY B 251 GLY B 259 1 O ILE B 253 N VAL B 227
SHEET 6 C 6 ASP B 323 THR B 328 1 O ILE B 327 N GLY B 258
SHEET 1 D 4 GLU B 155 VAL B 159 0
SHEET 2 D 4 LYS B 129 GLY B 135 1 N ILE B 132 O ILE B 157
SHEET 3 D 4 GLU B 105 GLU B 109 1 N ILE B 106 O LYS B 129
SHEET 4 D 4 ALA B 184 TYR B 186 1 O HIS B 185 N ILE B 107
LINK O GLY B 232 NA NA B 398 1555 1555 2.26
LINK O PHE B 306 NA NA B 398 1555 1555 2.38
LINK O SER B 308 NA NA B 398 1555 1555 2.34
LINK NA NA B 398 O HOH B 425 1555 1555 2.46
LINK NA NA B 398 O HOH B 488 1555 1555 2.47
LINK NZ LYS B 87 C4A PLP B 399 1555 1555 1.39
CISPEP 1 ASP A 27 PRO A 28 0 0.19
CISPEP 2 ARG B 55 PRO B 56 0 -3.35
CISPEP 3 HIS B 195 PRO B 196 0 7.71
SITE 1 AC1 5 GLY B 232 PHE B 306 SER B 308 HOH B 425
SITE 2 AC1 5 HOH B 488
SITE 1 AC2 13 GLU A 49 ASP A 60 LEU A 100 ILE A 153
SITE 2 AC2 13 TYR A 175 PHE A 212 GLY A 213 GLY A 234
SITE 3 AC2 13 SER A 235 HOH A 298 HOH A 333 HOH A 424
SITE 4 AC2 13 HOH A 425
SITE 1 AC3 17 HIS B 86 LYS B 87 GLN B 114 THR B 190
SITE 2 AC3 17 GLY B 232 GLY B 233 GLY B 234 SER B 235
SITE 3 AC3 17 ASN B 236 GLY B 303 GLU B 350 SER B 377
SITE 4 AC3 17 GLY B 378 HOH B 405 HOH B 541 HOH B 620
SITE 5 AC3 17 HOH B 708
CRYST1 183.071 59.281 67.345 90.00 94.67 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 0.005462 0.000000 0.000446 0.00000
SCALE2 0.000000 0.016869 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014898 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
