HEADER LYASE/LYASE INHIBITOR 11-APR-18 6D0V
TITLE TRYPTOPHAN SYNTHASE Q114A MUTANT IN COMPLEX WITH INHIBITOR N-(4'-
TITLE 2 TRIFLUOROMETHOXYBENZENESULFONYL)-2-AMINO-1-ETHYLPHOSPHATE (F9F) AT
TITLE 3 THE ALPHA-SITE, AMINOACRYLATE AT THE BETA SITE, AND CESIUM ION AT THE
TITLE 4 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 STR. LT2;
SOURCE 4 ORGANISM_TAXID: 99287;
SOURCE 5 STRAIN: LT2 / SGSC1412 / ATCC 700720;
SOURCE 6 GENE: TRPA, STM1727;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: CB149;
SOURCE 10 EXPRESSION_SYSTEM_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 STR. LT2;
SOURCE 15 ORGANISM_TAXID: 99287;
SOURCE 16 STRAIN: LT2 / SGSC1412 / ATCC 700720;
SOURCE 17 GENE: TRPB, STM1726;
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 LIGAND, CESIUM ION, MUTANT BETA-Q114A, LYASE, P1T LIGAND, LYASE-
KEYWDS 2 LYASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR E.HILARIO,M.F.DUNN,L.J.MUELLER,L.FAN
REVDAT 5 04-OCT-23 6D0V 1 REMARK
REVDAT 4 29-SEP-21 6D0V 1 REMARK LINK
REVDAT 3 29-APR-20 6D0V 1 TITLE COMPND AUTHOR JRNL
REVDAT 3 2 1 REMARK HET HETNAM HETSYN
REVDAT 3 3 1 FORMUL ATOM
REVDAT 2 18-DEC-19 6D0V 1 REMARK
REVDAT 1 17-APR-19 6D0V 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 AT THE BETA SITE, AND CESIUM ION AT THE METAL
JRNL TITL 5 COORDINATION SITE.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.64 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.64
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.32
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 89.6
REMARK 3 NUMBER OF REFLECTIONS : 77328
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) : 0.132
REMARK 3 R VALUE (WORKING SET) : 0.130
REMARK 3 FREE R VALUE : 0.175
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4044
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4996
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 168
REMARK 3 SOLVENT ATOMS : 744
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.93
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.73000
REMARK 3 B22 (A**2) : 1.72000
REMARK 3 B33 (A**2) : -1.02000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.22000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.118
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.085
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.049
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.195
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : NULL ; NULL
REMARK 3 ANGLE DISTANCE (A) : NULL ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: U VALUES : WITH TLS ADDED
REMARK 4
REMARK 4 6D0V COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-APR-18.
REMARK 100 THE DEPOSITION ID IS D_1000233842.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-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 HF
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM 7.2.2
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.22
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 81464
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.640
REMARK 200 RESOLUTION RANGE LOW (A) : 91.533
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.0
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.64
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.73
REMARK 200 COMPLETENESS FOR SHELL (%) : 83.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : 0.21300
REMARK 200 R SYM FOR SHELL (I) : 0.21300
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.100
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, DM 2.1
REMARK 200 STARTING MODEL: PDB ENTRY 2CLL
REMARK 200
REMARK 200 REMARK: LARGE PLATE-LIKE CRYSTAL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.27
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.63
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM BICINE-CSOH, 8-10% PEG8000, 2-6
REMARK 280 MM SPERMINE, 1 MM DTT, PH 7.8, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 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 91.86500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 30.44000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 91.86500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 30.44000
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: 8910 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 42890 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 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 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 403 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 MET B 1
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 ALA A 268 CA C O CB
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 C2 DMS B 408 O HOH B 894 2.09
REMARK 500 OE2 GLU B 11 O HOH B 501 2.12
REMARK 500 NH1 ARG B 222 O HOH B 502 2.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 ARG A 225 NE ARG A 225 CZ 0.080
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 ARG A 225 NH1 - CZ - NH2 ANGL. DEV. = 7.7 DEGREES
REMARK 500 ARG A 225 NE - CZ - NH1 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ARG A 225 NE - CZ - NH2 ANGL. DEV. = -7.4 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 PHE A 212 119.11 100.72
REMARK 500 ASN B 64 -39.74 -134.89
REMARK 500 THR B 165 -159.54 -134.33
REMARK 500 ARG B 394 -87.85 -89.69
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG B 222 0.10 SIDE CHAIN
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 682 DISTANCE = 5.81 ANGSTROMS
REMARK 525 HOH A 683 DISTANCE = 6.38 ANGSTROMS
REMARK 525 HOH B 957 DISTANCE = 6.03 ANGSTROMS
REMARK 525 HOH B 958 DISTANCE = 6.08 ANGSTROMS
REMARK 525 HOH B 959 DISTANCE = 6.12 ANGSTROMS
REMARK 525 HOH B 960 DISTANCE = 6.56 ANGSTROMS
REMARK 525 HOH B 961 DISTANCE = 7.11 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 403 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 63.6 63.6
REMARK 620 4 PRO B 56 O 63.6 63.6 0.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CS B 404 CS
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR B 66 O
REMARK 620 2 THR B 66 OG1 58.4
REMARK 620 3 THR B 69 O 72.4 125.2
REMARK 620 4 THR B 71 O 87.9 66.0 91.1
REMARK 620 5 HOH B 664 O 78.7 56.7 136.9 119.4
REMARK 620 6 HOH B 860 O 153.5 143.6 81.1 91.5 123.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CS B 402 CS
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL B 231 O
REMARK 620 2 GLY B 232 O 66.2
REMARK 620 3 GLU B 256 OE2 110.1 143.9
REMARK 620 4 GLY B 268 O 99.3 141.1 74.4
REMARK 620 5 SER B 308 O 134.8 70.5 112.3 106.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CS B 402 CS
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY B 232 O
REMARK 620 2 GLY B 268 O 141.4
REMARK 620 3 LEU B 304 O 114.1 84.7
REMARK 620 4 PHE B 306 O 131.2 84.4 77.3
REMARK 620 5 SER B 308 O 70.9 115.4 142.2 73.5
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 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 CL A 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue F9F A 308
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 309
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 0JO B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CS B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CS B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CS B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS B 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS B 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS B 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS B 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS B 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS B 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS B 411
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS B 412
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS B 413
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS B 414
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS B 415
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 416
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 417
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 419
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 420
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 421
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 422
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 423
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 424
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 425
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SER B 426
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 427
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 428
DBREF 6D0V A 1 268 UNP P00929 TRPA_SALTY 1 268
DBREF 6D0V B 2 394 UNP P0A2K1 TRPB_SALTY 2 394
SEQADV 6D0V ALA B 114 UNP P0A2K1 GLN 114 ENGINEERED MUTATION
SEQADV 6D0V GLU B 395 UNP P0A2K1 EXPRESSION TAG
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 MET THR THR LEU LEU ASN PRO TYR PHE GLY GLU PHE GLY
SEQRES 2 B 395 GLY MET TYR VAL PRO GLN ILE LEU MET PRO ALA LEU ASN
SEQRES 3 B 395 GLN LEU GLU GLU ALA PHE VAL SER ALA GLN LYS ASP PRO
SEQRES 4 B 395 GLU PHE GLN ALA GLN PHE ALA ASP LEU LEU LYS ASN TYR
SEQRES 5 B 395 ALA GLY ARG PRO THR ALA LEU THR LYS CYS GLN ASN ILE
SEQRES 6 B 395 THR ALA GLY THR ARG THR THR LEU TYR LEU LYS ARG GLU
SEQRES 7 B 395 ASP LEU LEU HIS GLY GLY ALA HIS LYS THR ASN GLN VAL
SEQRES 8 B 395 LEU GLY GLN ALA LEU LEU ALA LYS ARG MET GLY LYS SER
SEQRES 9 B 395 GLU ILE ILE ALA GLU THR GLY ALA GLY ALA HIS GLY VAL
SEQRES 10 B 395 ALA SER ALA LEU ALA SER ALA LEU LEU GLY LEU LYS CYS
SEQRES 11 B 395 ARG ILE TYR MET GLY ALA LYS ASP VAL GLU ARG GLN SER
SEQRES 12 B 395 PRO ASN VAL PHE ARG MET ARG LEU MET GLY ALA GLU VAL
SEQRES 13 B 395 ILE PRO VAL HIS SER GLY SER ALA THR LEU LYS ASP ALA
SEQRES 14 B 395 CYS ASN GLU ALA LEU ARG ASP TRP SER GLY SER TYR GLU
SEQRES 15 B 395 THR ALA HIS TYR MET LEU GLY THR ALA ALA GLY PRO HIS
SEQRES 16 B 395 PRO TYR PRO THR ILE VAL ARG GLU PHE GLN ARG MET ILE
SEQRES 17 B 395 GLY GLU GLU THR LYS ALA GLN ILE LEU ASP LYS GLU GLY
SEQRES 18 B 395 ARG LEU PRO ASP ALA VAL ILE ALA CYS VAL GLY GLY GLY
SEQRES 19 B 395 SER ASN ALA ILE GLY MET PHE ALA ASP PHE ILE ASN ASP
SEQRES 20 B 395 THR SER VAL GLY LEU ILE GLY VAL GLU PRO GLY GLY HIS
SEQRES 21 B 395 GLY ILE GLU THR GLY GLU HIS GLY ALA PRO LEU LYS HIS
SEQRES 22 B 395 GLY ARG VAL GLY ILE TYR PHE GLY MET LYS ALA PRO MET
SEQRES 23 B 395 MET GLN THR ALA ASP GLY GLN ILE GLU GLU SER TYR SER
SEQRES 24 B 395 ILE SER ALA GLY LEU ASP PHE PRO SER VAL GLY PRO GLN
SEQRES 25 B 395 HIS ALA TYR LEU ASN SER ILE GLY ARG ALA ASP TYR VAL
SEQRES 26 B 395 SER ILE THR ASP ASP GLU ALA LEU GLU ALA PHE LYS THR
SEQRES 27 B 395 LEU CYS ARG HIS GLU GLY ILE ILE PRO ALA LEU GLU SER
SEQRES 28 B 395 SER HIS ALA LEU ALA HIS ALA LEU LYS MET MET ARG GLU
SEQRES 29 B 395 GLN PRO GLU LYS GLU GLN LEU LEU VAL VAL ASN LEU SER
SEQRES 30 B 395 GLY ARG GLY ASP LYS ASP ILE PHE THR VAL HIS ASP ILE
SEQRES 31 B 395 LEU LYS ALA ARG 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 CL A 306 1
HET CL A 307 1
HET F9F A 308 22
HET EDO A 309 4
HET 0JO B 401 21
HET CS B 402 2
HET CS B 403 1
HET CS B 404 1
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 DMS B 413 4
HET DMS B 414 4
HET DMS B 415 4
HET CL B 416 1
HET CL B 417 1
HET CL B 418 1
HET EDO B 419 4
HET EDO B 420 4
HET EDO B 421 4
HET EDO B 422 4
HET EDO B 423 4
HET EDO B 424 4
HET EDO B 425 4
HET SER B 426 7
HET PEG B 427 7
HET PEG B 428 7
HETNAM DMS DIMETHYL SULFOXIDE
HETNAM CL CHLORIDE ION
HETNAM F9F 2-({[4-(TRIFLUOROMETHOXY)PHENYL]SULFONYL}AMINO)ETHYL
HETNAM 2 F9F DIHYDROGEN PHOSPHATE
HETNAM EDO 1,2-ETHANEDIOL
HETNAM 0JO 2-{[(E)-{3-HYDROXY-2-METHYL-5-[(PHOSPHONOOXY)
HETNAM 2 0JO METHYL]PYRIDIN-4-YL}METHYLIDENE]AMINO}PROP-2-ENOIC
HETNAM 3 0JO ACID
HETNAM CS CESIUM ION
HETNAM SER SERINE
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETSYN F9F N-(4'-TRIFLUOROMETHOXYBENZENESULFONYL)-2-AMINO-1-
HETSYN 2 F9F ETHYLPHOSPHATE, F9
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 DMS 16(C2 H6 O S)
FORMUL 8 CL 5(CL 1-)
FORMUL 10 F9F C9 H11 F3 N O7 P S
FORMUL 11 EDO 8(C2 H6 O2)
FORMUL 12 0JO C11 H13 N2 O7 P
FORMUL 13 CS 3(CS 1+)
FORMUL 37 SER C3 H7 N O3
FORMUL 38 PEG 2(C4 H10 O3)
FORMUL 40 HOH *744(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 GLY B 179 1 15
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 GLU 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 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 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 ILE B 157
SHEET 3 AA4 4 GLU B 105 THR B 110 1 N ILE B 106 O ARG B 131
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 403 1555 1555 3.30
LINK O GLY B 54 CS CS B 403 1555 2555 3.30
LINK O PRO B 56 CS CS B 403 1555 1555 3.14
LINK O PRO B 56 CS CS B 403 1555 2555 3.14
LINK O THR B 66 CS CS B 404 1555 1555 3.28
LINK OG1 THR B 66 CS CS B 404 1555 1555 3.35
LINK O THR B 69 CS CS B 404 1555 1555 3.10
LINK O THR B 71 CS CS B 404 1555 1555 3.00
LINK O VAL B 231 CS B CS B 402 1555 1555 3.26
LINK O GLY B 232 CS A CS B 402 1555 1555 3.23
LINK O GLY B 232 CS B CS B 402 1555 1555 3.08
LINK OE2 GLU B 256 CS B CS B 402 1555 1555 3.27
LINK O GLY B 268 CS A CS B 402 1555 1555 3.08
LINK O GLY B 268 CS B CS B 402 1555 1555 3.24
LINK O LEU B 304 CS A CS B 402 1555 1555 3.47
LINK O PHE B 306 CS A CS B 402 1555 1555 3.01
LINK O SER B 308 CS A CS B 402 1555 1555 3.18
LINK O SER B 308 CS B CS B 402 1555 1555 3.37
LINK CS CS B 404 O HOH B 664 1555 1555 3.11
LINK CS CS B 404 O HOH B 860 1555 1555 2.54
CISPEP 1 ASP A 27 PRO A 28 0 9.76
CISPEP 2 ARG B 55 PRO B 56 0 5.32
CISPEP 3 HIS B 195 PRO B 196 0 19.79
SITE 1 AC1 6 SER A 55 PHE A 72 HOH A 616 HOH A 656
SITE 2 AC1 6 GLN B 293 HOH B 780
SITE 1 AC2 6 MET A 1 ARG A 3 VAL A 123 ASP A 124
SITE 2 AC2 6 ASN A 147 HOH A 415
SITE 1 AC3 4 PHE A 82 ARG A 117 HOH A 408 HOH A 496
SITE 1 AC4 6 ALA A 265 ALA A 268 HOH A 640 HOH A 662
SITE 2 AC4 6 LYS B 99 ARG B 100
SITE 1 AC5 6 PHE A 139 ARG A 140 PRO A 150 ILE A 151
SITE 2 AC5 6 PHE A 152 HOH A 426
SITE 1 AC6 4 ALA A 167 GLY A 170 HIS A 204 HOH A 531
SITE 1 AC7 20 PHE A 22 GLU A 49 ALA A 59 ILE A 64
SITE 2 AC7 20 LEU A 100 LEU A 127 ALA A 129 ILE A 153
SITE 3 AC7 20 TYR A 175 THR A 183 GLY A 184 PHE A 212
SITE 4 AC7 20 GLY A 213 ILE A 232 GLY A 234 SER A 235
SITE 5 AC7 20 HOH A 422 HOH A 428 HOH A 487 PRO B 18
SITE 1 AC8 6 SER A 180 GLY A 181 ASN A 187 HOH A 526
SITE 2 AC8 6 GLY B 179 DMS B 405
SITE 1 AC9 22 HIS B 86 LYS B 87 THR B 110 GLY B 111
SITE 2 AC9 22 ALA B 112 GLY B 113 ALA B 114 HIS B 115
SITE 3 AC9 22 LEU B 166 THR B 190 CYS B 230 GLY B 232
SITE 4 AC9 22 GLY B 233 GLY B 234 SER B 235 ASN B 236
SITE 5 AC9 22 GLY B 303 GLU B 350 SER B 377 HOH B 543
SITE 6 AC9 22 HOH B 592 HOH B 596
SITE 1 AD1 7 VAL B 231 GLY B 232 GLU B 256 GLY B 268
SITE 2 AD1 7 LEU B 304 PHE B 306 SER B 308
SITE 1 AD2 4 GLY B 54 PRO B 56 DMS B 406 HOH B 762
SITE 1 AD3 4 THR B 66 THR B 69 THR B 71 HOH B 860
SITE 1 AD4 7 SER A 180 EDO A 309 GLY B 179 SER B 180
SITE 2 AD4 7 TYR B 181 GLU B 182 PEG B 428
SITE 1 AD5 7 LYS B 50 ARG B 55 PRO B 56 THR B 57
SITE 2 AD5 7 GLN B 215 CS B 403 HOH B 762
SITE 1 AD6 5 LYS B 137 TYR B 298 HOH B 517 HOH B 669
SITE 2 AD6 5 HOH B 749
SITE 1 AD7 6 GLN B 42 ALA B 46 LEU B 49 HOH B 637
SITE 2 AD7 6 HOH B 894 HOH B 937
SITE 1 AD8 5 ALA B 124 LEU B 128 CYS B 130 GLY B 153
SITE 2 AD8 5 ALA B 154
SITE 1 AD9 3 ASN B 64 HIS B 342 HOH B 608
SITE 1 AE1 2 GLU B 331 HOH B 560
SITE 1 AE2 4 ILE B 262 HIS B 267 HIS B 273 HOH B 615
SITE 1 AE3 1 TYR B 8
SITE 1 AE4 4 PHE B 147 ARG B 150 HIS B 388 HOH B 721
SITE 1 AE5 3 GLN B 36 LYS B 37 HOH B 903
SITE 1 AE6 1 GLN B 36
SITE 1 AE7 1 GLY B 153
SITE 1 AE8 2 GLU B 295 GLU B 296
SITE 1 AE9 4 GLU B 211 ALA B 214 HOH B 719 HOH B 767
SITE 1 AF1 5 TYR B 133 GLU B 172 ARG B 175 ASP B 176
SITE 2 AF1 5 HOH B 614
SITE 1 AF2 2 ARG B 363 HOH B 774
SITE 1 AF3 6 TYR B 8 PHE B 9 TYR B 315 HOH B 574
SITE 2 AF3 6 HOH B 619 HOH B 723
SITE 1 AF4 3 VAL B 159 HIS B 160 HOH B 783
SITE 1 AF5 7 HIS B 273 ARG B 275 MET B 286 MET B 287
SITE 2 AF5 7 GLN B 288 HOH B 522 HOH B 684
SITE 1 AF6 13 SER A 55 ASP A 56 PRO A 57 GLN A 65
SITE 2 AF6 13 SER B 161 GLY B 162 ASN B 171 ARG B 175
SITE 3 AF6 13 HOH B 532 HOH B 549 HOH B 662 HOH B 711
SITE 4 AF6 13 HOH B 832
SITE 1 AF7 8 ASN B 51 TYR B 52 THR B 60 LYS B 61
SITE 2 AF7 8 LEU B 125 GLU B 343 HOH B 609 HOH B 805
SITE 1 AF8 6 GLY B 179 SER B 180 GLU B 182 THR B 183
SITE 2 AF8 6 DMS B 405 HOH B 725
CRYST1 183.730 60.880 67.320 90.00 94.87 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 0.005443 0.000000 0.000464 0.00000
SCALE2 0.000000 0.016426 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014908 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
