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HEADER OXIDOREDUCTASE 22-MAY-09 2WJ6
TITLE CRYSTAL STRUCTURE OF THE COFACTOR-DEVOID 1-H-3-HYDROXY-4-
TITLE 2 OXOQUINALDINE 2,4-DIOXYGENASE (HOD) FROM ARTHROBACTER
TITLE 3 NITROGUAJACOLICUS RU61A COMPLEXED WITH ITS NATURAL
TITLE 4 SUBSTRATE N-ACETYLANTHRANILATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 1H-3-HYDROXY-4-OXOQUINALDINE 2,4-DIOXYGENASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 EC: 1.13.11.48;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARTHROBACTER NITROGUAJACOLICUS;
SOURCE 3 ORGANISM_TAXID: 211146;
SOURCE 4 STRAIN: RU61A;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: M15/PREP4;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PQE30
KEYWDS OXIDOREDUCTASE, ALPHA/BETA HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.A.STEINER
REVDAT 1 26-JAN-10 2WJ6 0
JRNL AUTH R.A.STEINER,H.J.JANSSEN,P.ROVERSI,A.J.OAKLEY,
JRNL AUTH 2 S.FETZNER
JRNL TITL STRUCTURAL BASIS FOR COFACTOR-INDEPENDENT
JRNL TITL 2 DIOXYGENATION OF N-HETEROAROMATIC COMPOUNDS AT THE
JRNL TITL 3 {ALPHA}/{BETA}-HYDROLASE FOLD.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 107 657 2010
JRNL REFN ISSN 0027-8424
JRNL PMID 20080731
JRNL DOI 10.1073/PNAS.0909033107
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH R.A.STEINER,U.FRERICHS-DEEKEN,S.FETZNER
REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY X-RAY ANALYSIS OF
REMARK 1 TITL 2 1H-3-HYDROXY-4-OXOQUINALDINE 2,4-DIOXYGENASE FROM
REMARK 1 TITL 3 ARTHROBACTER NITROGUAJACOLICUS RU61A: A COFACTOR-
REMARK 1 TITL 4 DEVOID DIOXYGENASE OF THE ALPHA/BETA-HYDROLASE-
REMARK 1 TITL 5 FOLD SUPERFAMILY.
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.F V. 63 382 2007
REMARK 1 REFN ISSN 1744-3091
REMARK 1 PMID 17565176
REMARK 1 DOI 10.1107/S174430910701353X
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0070
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.52
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.82
REMARK 3 NUMBER OF REFLECTIONS : 81912
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) : 0.18045
REMARK 3 R VALUE (WORKING SET) : 0.17853
REMARK 3 FREE R VALUE : 0.21650
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT : 4315
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) : 2.000
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.052
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6076
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.190
REMARK 3 BIN FREE R VALUE SET COUNT : 252
REMARK 3 BIN FREE R VALUE : 0.259
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8946
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 209
REMARK 3 SOLVENT ATOMS : 741
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 22.46
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.821
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.36
REMARK 3 B22 (A**2) : -0.42
REMARK 3 B33 (A**2) : 3.78
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : 0.00
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.037
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.032
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.105
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.846
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.944
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.924
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9419 ; 0.015 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 6473 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12792 ; 1.453 ; 1.956
REMARK 3 BOND ANGLES OTHERS (DEGREES): 15608 ; 2.458 ; 3.001
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1096 ; 6.350 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 487 ;37.914 ;23.429
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1466 ;15.530 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 72 ;18.703 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1293 ; 0.082 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 10483 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 2005 ; 0.010 ; 0.020
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): 5469 ; 0.618 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2193 ; 0.081 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8836 ; 1.093 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3950 ; 1.967 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3953 ; 2.958 ; 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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B C D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 5 A 274 3
REMARK 3 1 B 5 B 274 3
REMARK 3 1 C 5 C 274 3
REMARK 3 1 D 5 D 274 3
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 1575 ; 0.04 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 B (A): 1575 ; 0.05 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 C (A): 1575 ; 0.05 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 D (A): 1575 ; 0.05 ; 0.05
REMARK 3 LOOSE POSITIONAL 1 A (A): 2171 ; 0.09 ; 5.00
REMARK 3 LOOSE POSITIONAL 1 B (A): 2171 ; 0.14 ; 5.00
REMARK 3 LOOSE POSITIONAL 1 C (A): 2171 ; 0.12 ; 5.00
REMARK 3 LOOSE POSITIONAL 1 D (A): 2171 ; 0.09 ; 5.00
REMARK 3 TIGHT THERMAL 1 A (A**2): 1575 ; 0.16 ; 0.50
REMARK 3 TIGHT THERMAL 1 B (A**2): 1575 ; 0.14 ; 0.50
REMARK 3 TIGHT THERMAL 1 C (A**2): 1575 ; 0.16 ; 0.50
REMARK 3 TIGHT THERMAL 1 D (A**2): 1575 ; 0.15 ; 0.50
REMARK 3 LOOSE THERMAL 1 A (A**2): 2171 ; 0.13 ; 10.00
REMARK 3 LOOSE THERMAL 1 B (A**2): 2171 ; 0.13 ; 10.00
REMARK 3 LOOSE THERMAL 1 C (A**2): 2171 ; 0.14 ; 10.00
REMARK 3 LOOSE THERMAL 1 D (A**2): 2171 ; 0.13 ; 10.00
REMARK 3
REMARK 3 TWIN DETAILS
REMARK 3 NUMBER OF TWIN DOMAINS : 2
REMARK 3 TWIN DOMAIN : 1
REMARK 3 TWIN OPERATOR : H, K, L
REMARK 3 TWIN FRACTION : 0.486
REMARK 3 TWIN DOMAIN : 2
REMARK 3 TWIN OPERATOR : -H, L, K
REMARK 3 TWIN FRACTION : 0.514
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
REMARK 3 RIDING POSITIONS.
REMARK 4
REMARK 4 2WJ6 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-MAY-09.
REMARK 100 THE PDBE ID CODE IS EBI-39904.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-DEC-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9796
REMARK 200 MONOCHROMATOR : SI (111) DOUBLE CRYSTAL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 86312
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.00
REMARK 200 RESOLUTION RANGE LOW (A) : 30.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 5.6
REMARK 200 R MERGE (I) : 0.05
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 19.00
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.7
REMARK 200 R MERGE FOR SHELL (I) : 0.21
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 5.70
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.29
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN AT 150 MG/ML IN STORAGE
REMARK 280 BUFFER 1,65M NA/K TARTRATE, 0.1M HEPES, PH 7.0
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 22.47000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 83.61500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 83.54500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 83.61500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 22.47000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 83.54500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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 GENERATING THE BIOMOLECULE
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
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 400
REMARK 400 COMPOUND
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, CYS 69 TO SER
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, CYS 69 TO SER
REMARK 400 ENGINEERED RESIDUE IN CHAIN C, CYS 69 TO SER
REMARK 400 ENGINEERED RESIDUE IN CHAIN D, CYS 69 TO SER
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 A 1
REMARK 465 GLN A 276
REMARK 465 MET B 1
REMARK 465 GLN B 276
REMARK 465 MET C 1
REMARK 465 GLY C 275
REMARK 465 GLN C 276
REMARK 465 MET D 1
REMARK 465 GLY D 275
REMARK 465 GLN D 276
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 OE1 GLN C 274 O HOH C 2213 2.19
REMARK 500 O HOH C 2208 O HOH C 2213 2.20
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 LYS B 167 CB LYS B 167 CG -0.192
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 PRO A 59 C - N - CD ANGL. DEV. = -14.7 DEGREES
REMARK 500 PRO A 97 C - N - CD ANGL. DEV. = -16.0 DEGREES
REMARK 500 PRO B 59 C - N - CD ANGL. DEV. = -14.8 DEGREES
REMARK 500 PRO B 97 C - N - CD ANGL. DEV. = -15.1 DEGREES
REMARK 500 PRO C 97 C - N - CD ANGL. DEV. = -13.4 DEGREES
REMARK 500 PRO D 59 C - N - CD ANGL. DEV. = -14.1 DEGREES
REMARK 500 PRO D 97 C - N - CD ANGL. DEV. = -14.3 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 12 -107.21 51.67
REMARK 500 GLU A 93 -76.70 -97.40
REMARK 500 SER A 101 -116.91 41.14
REMARK 500 ASP A 126 68.27 38.27
REMARK 500 LEU A 128 106.62 -59.14
REMARK 500 PHE A 252 72.12 -119.32
REMARK 500 VAL A 257 56.27 -140.22
REMARK 500 PHE B 12 -107.34 54.80
REMARK 500 GLU B 93 -83.02 -97.21
REMARK 500 SER B 101 -116.70 39.90
REMARK 500 PHE B 252 73.46 -115.85
REMARK 500 GLN B 274 75.07 -68.59
REMARK 500 PHE C 12 -106.40 50.50
REMARK 500 GLU C 93 -80.68 -92.87
REMARK 500 SER C 101 -118.19 46.45
REMARK 500 PHE C 252 68.65 -115.46
REMARK 500 VAL C 257 56.25 -140.22
REMARK 500 PHE D 12 -110.73 50.04
REMARK 500 GLU D 93 -77.01 -95.02
REMARK 500 SER D 101 -116.32 48.68
REMARK 500 PHE D 252 66.90 -118.31
REMARK 500 VAL D 257 55.65 -142.29
REMARK 500
REMARK 500 REMARK: NULL
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 K A1282 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 238 O
REMARK 620 2 HOH A2169 O 81.6
REMARK 620 3 ALA A 235 O 74.5 80.8
REMARK 620 4 GOL A1276 O3 149.0 81.6 77.2
REMARK 620 5 HOH D2086 O 108.5 77.4 157.3 93.0
REMARK 620 6 PHE A 241 O 77.6 152.4 110.4 125.0 92.1
REMARK 620 7 GOL A1276 O2 146.6 131.6 103.5 53.8 86.3 72.0
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A1283 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SRT A1286 O41
REMARK 620 2 ASP A 165 O 82.7
REMARK 620 3 SRT A1286 O11 62.7 137.3
REMARK 620 4 HOH A2099 O 91.6 88.3 69.7
REMARK 620 5 SRT A1286 O3 52.5 117.4 60.8 127.9
REMARK 620 6 HOH A2098 O 111.7 85.6 128.7 154.9 76.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K B1281 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 238 O
REMARK 620 2 ALA B 235 O 75.0
REMARK 620 3 HOH B2158 O 74.5 60.1
REMARK 620 4 PHE B 241 O 79.4 109.5 153.7
REMARK 620 5 GOL C1276 O2 154.0 98.5 124.6 79.3
REMARK 620 6 GOL C1276 O3 141.9 75.1 70.3 133.2 54.4
REMARK 620 7 HOH C2126 O 112.7 155.8 98.8 94.6 83.6 87.0
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K C1279 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH C2185 O
REMARK 620 2 HIS C 238 O 129.0
REMARK 620 3 HOH C2184 O 57.7 84.2
REMARK 620 4 ALA C 235 O 68.8 64.9 66.0
REMARK 620 5 HOH C2191 O 95.4 106.4 74.6 140.1
REMARK 620 6 PHE C 241 O 133.4 77.5 161.3 102.0 114.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K D1277 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH D2134 O
REMARK 620 2 ALA D 235 O 61.4
REMARK 620 3 HIS D 238 O 82.2 65.3
REMARK 620 4 HOH D2137 O 72.5 132.9 100.9
REMARK 620 5 PHE D 241 O 157.6 102.4 76.6 118.4
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 GOL A1276
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C1275
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D1275
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B1276
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C1276
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1277
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1278
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1279
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1280
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1281
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C1277
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B1277
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D1276
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C1278
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B1278
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B1279
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B1280
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C1279
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A1282
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K D1277
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B1281
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A1283
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZZ8 A1284
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZZ8 B1282
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZZ8 C1280
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZZ8 D1278
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SRT A1285
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SRT B1283
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SRT C1281
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SRT D1279
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SRT A1286
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2WM2 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE COFACTOR-DEVOID 1-
REMARK 900 H-3-HYDROXY-4-OXOQUINALDINE 2,4-
REMARK 900 DIOXYGENASE (HOD) FROM ARTHROBACTER
REMARK 900 NITROGUAJACOLICUS RU61A IN COMPLEX WITH
REMARK 900 CHLORIDE
REMARK 900 RELATED ID: 2WJ3 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE COFACTOR-DEVOID 1-
REMARK 900 H-3-HYDROXY-4-OXOQUINALDINE 2,4-
REMARK 900 DIOXYGENASE (HOD) FROM ARTHROBACTER
REMARK 900 NITROGUAJACOLICUS RU61A
REMARK 900 RELATED ID: 2WJ4 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE COFACTOR-DEVOID 1-
REMARK 900 H-3-HYDROXY-4-OXOQUINALDINE 2,4-
REMARK 900 DIOXYGENASE (HOD) FROM ARTHROBACTER
REMARK 900 NITROGUAJACOLICUS RU61A ANAEROBICALLY COMPLEXED
REMARK 900 WITH ITS NATURAL SUBSTRATE 1-H-3-HYDROXY-
REMARK 900 4-OXOQUINALDINE
DBREF 2WJ6 A 1 276 UNP A4V8M9 A4V8M9_9MICC 1 276
DBREF 2WJ6 B 1 276 UNP A4V8M9 A4V8M9_9MICC 1 276
DBREF 2WJ6 C 1 276 UNP A4V8M9 A4V8M9_9MICC 1 276
DBREF 2WJ6 D 1 276 UNP A4V8M9 A4V8M9_9MICC 1 276
SEQADV 2WJ6 SER A 69 UNP A4V8M9 CYS 69 ENGINEERED MUTATION
SEQADV 2WJ6 SER B 69 UNP A4V8M9 CYS 69 ENGINEERED MUTATION
SEQADV 2WJ6 SER C 69 UNP A4V8M9 CYS 69 ENGINEERED MUTATION
SEQADV 2WJ6 SER D 69 UNP A4V8M9 CYS 69 ENGINEERED MUTATION
SEQRES 1 A 276 MET THR ASP THR TYR LEU HIS GLU THR LEU VAL PHE ASP
SEQRES 2 A 276 ASN LYS LEU SER TYR ILE ASP ASN GLN ARG ASP THR ASP
SEQRES 3 A 276 GLY PRO ALA ILE LEU LEU LEU PRO GLY TRP CYS HIS ASP
SEQRES 4 A 276 HIS ARG VAL TYR LYS TYR LEU ILE GLN GLU LEU ASP ALA
SEQRES 5 A 276 ASP PHE ARG VAL ILE VAL PRO ASN TRP ARG GLY HIS GLY
SEQRES 6 A 276 LEU SER PRO SER GLU VAL PRO ASP PHE GLY TYR GLN GLU
SEQRES 7 A 276 GLN VAL LYS ASP ALA LEU GLU ILE LEU ASP GLN LEU GLY
SEQRES 8 A 276 VAL GLU THR PHE LEU PRO VAL SER HIS SER HIS GLY GLY
SEQRES 9 A 276 TRP VAL LEU VAL GLU LEU LEU GLU GLN ALA GLY PRO GLU
SEQRES 10 A 276 ARG ALA PRO ARG GLY ILE ILE MET ASP TRP LEU MET TRP
SEQRES 11 A 276 ALA PRO LYS PRO ASP PHE ALA LYS SER LEU THR LEU LEU
SEQRES 12 A 276 LYS ASP PRO GLU ARG TRP ARG GLU GLY THR HIS GLY LEU
SEQRES 13 A 276 PHE ASP VAL TRP LEU ASP GLY HIS ASP GLU LYS ARG VAL
SEQRES 14 A 276 ARG HIS HIS LEU LEU GLU GLU MET ALA ASP TYR GLY TYR
SEQRES 15 A 276 ASP CYS TRP GLY ARG SER GLY ARG VAL ILE GLU ASP ALA
SEQRES 16 A 276 TYR GLY ARG ASN GLY SER PRO MET GLN MET MET ALA ASN
SEQRES 17 A 276 LEU THR LYS THR ARG PRO ILE ARG HIS ILE PHE SER GLN
SEQRES 18 A 276 PRO THR GLU PRO GLU TYR GLU LYS ILE ASN SER ASP PHE
SEQRES 19 A 276 ALA GLU GLN HIS PRO TRP PHE SER TYR ALA LYS LEU GLY
SEQRES 20 A 276 GLY PRO THR HIS PHE PRO ALA ILE ASP VAL PRO ASP ARG
SEQRES 21 A 276 ALA ALA VAL HIS ILE ARG GLU PHE ALA THR ALA ILE ARG
SEQRES 22 A 276 GLN GLY GLN
SEQRES 1 B 276 MET THR ASP THR TYR LEU HIS GLU THR LEU VAL PHE ASP
SEQRES 2 B 276 ASN LYS LEU SER TYR ILE ASP ASN GLN ARG ASP THR ASP
SEQRES 3 B 276 GLY PRO ALA ILE LEU LEU LEU PRO GLY TRP CYS HIS ASP
SEQRES 4 B 276 HIS ARG VAL TYR LYS TYR LEU ILE GLN GLU LEU ASP ALA
SEQRES 5 B 276 ASP PHE ARG VAL ILE VAL PRO ASN TRP ARG GLY HIS GLY
SEQRES 6 B 276 LEU SER PRO SER GLU VAL PRO ASP PHE GLY TYR GLN GLU
SEQRES 7 B 276 GLN VAL LYS ASP ALA LEU GLU ILE LEU ASP GLN LEU GLY
SEQRES 8 B 276 VAL GLU THR PHE LEU PRO VAL SER HIS SER HIS GLY GLY
SEQRES 9 B 276 TRP VAL LEU VAL GLU LEU LEU GLU GLN ALA GLY PRO GLU
SEQRES 10 B 276 ARG ALA PRO ARG GLY ILE ILE MET ASP TRP LEU MET TRP
SEQRES 11 B 276 ALA PRO LYS PRO ASP PHE ALA LYS SER LEU THR LEU LEU
SEQRES 12 B 276 LYS ASP PRO GLU ARG TRP ARG GLU GLY THR HIS GLY LEU
SEQRES 13 B 276 PHE ASP VAL TRP LEU ASP GLY HIS ASP GLU LYS ARG VAL
SEQRES 14 B 276 ARG HIS HIS LEU LEU GLU GLU MET ALA ASP TYR GLY TYR
SEQRES 15 B 276 ASP CYS TRP GLY ARG SER GLY ARG VAL ILE GLU ASP ALA
SEQRES 16 B 276 TYR GLY ARG ASN GLY SER PRO MET GLN MET MET ALA ASN
SEQRES 17 B 276 LEU THR LYS THR ARG PRO ILE ARG HIS ILE PHE SER GLN
SEQRES 18 B 276 PRO THR GLU PRO GLU TYR GLU LYS ILE ASN SER ASP PHE
SEQRES 19 B 276 ALA GLU GLN HIS PRO TRP PHE SER TYR ALA LYS LEU GLY
SEQRES 20 B 276 GLY PRO THR HIS PHE PRO ALA ILE ASP VAL PRO ASP ARG
SEQRES 21 B 276 ALA ALA VAL HIS ILE ARG GLU PHE ALA THR ALA ILE ARG
SEQRES 22 B 276 GLN GLY GLN
SEQRES 1 C 276 MET THR ASP THR TYR LEU HIS GLU THR LEU VAL PHE ASP
SEQRES 2 C 276 ASN LYS LEU SER TYR ILE ASP ASN GLN ARG ASP THR ASP
SEQRES 3 C 276 GLY PRO ALA ILE LEU LEU LEU PRO GLY TRP CYS HIS ASP
SEQRES 4 C 276 HIS ARG VAL TYR LYS TYR LEU ILE GLN GLU LEU ASP ALA
SEQRES 5 C 276 ASP PHE ARG VAL ILE VAL PRO ASN TRP ARG GLY HIS GLY
SEQRES 6 C 276 LEU SER PRO SER GLU VAL PRO ASP PHE GLY TYR GLN GLU
SEQRES 7 C 276 GLN VAL LYS ASP ALA LEU GLU ILE LEU ASP GLN LEU GLY
SEQRES 8 C 276 VAL GLU THR PHE LEU PRO VAL SER HIS SER HIS GLY GLY
SEQRES 9 C 276 TRP VAL LEU VAL GLU LEU LEU GLU GLN ALA GLY PRO GLU
SEQRES 10 C 276 ARG ALA PRO ARG GLY ILE ILE MET ASP TRP LEU MET TRP
SEQRES 11 C 276 ALA PRO LYS PRO ASP PHE ALA LYS SER LEU THR LEU LEU
SEQRES 12 C 276 LYS ASP PRO GLU ARG TRP ARG GLU GLY THR HIS GLY LEU
SEQRES 13 C 276 PHE ASP VAL TRP LEU ASP GLY HIS ASP GLU LYS ARG VAL
SEQRES 14 C 276 ARG HIS HIS LEU LEU GLU GLU MET ALA ASP TYR GLY TYR
SEQRES 15 C 276 ASP CYS TRP GLY ARG SER GLY ARG VAL ILE GLU ASP ALA
SEQRES 16 C 276 TYR GLY ARG ASN GLY SER PRO MET GLN MET MET ALA ASN
SEQRES 17 C 276 LEU THR LYS THR ARG PRO ILE ARG HIS ILE PHE SER GLN
SEQRES 18 C 276 PRO THR GLU PRO GLU TYR GLU LYS ILE ASN SER ASP PHE
SEQRES 19 C 276 ALA GLU GLN HIS PRO TRP PHE SER TYR ALA LYS LEU GLY
SEQRES 20 C 276 GLY PRO THR HIS PHE PRO ALA ILE ASP VAL PRO ASP ARG
SEQRES 21 C 276 ALA ALA VAL HIS ILE ARG GLU PHE ALA THR ALA ILE ARG
SEQRES 22 C 276 GLN GLY GLN
SEQRES 1 D 276 MET THR ASP THR TYR LEU HIS GLU THR LEU VAL PHE ASP
SEQRES 2 D 276 ASN LYS LEU SER TYR ILE ASP ASN GLN ARG ASP THR ASP
SEQRES 3 D 276 GLY PRO ALA ILE LEU LEU LEU PRO GLY TRP CYS HIS ASP
SEQRES 4 D 276 HIS ARG VAL TYR LYS TYR LEU ILE GLN GLU LEU ASP ALA
SEQRES 5 D 276 ASP PHE ARG VAL ILE VAL PRO ASN TRP ARG GLY HIS GLY
SEQRES 6 D 276 LEU SER PRO SER GLU VAL PRO ASP PHE GLY TYR GLN GLU
SEQRES 7 D 276 GLN VAL LYS ASP ALA LEU GLU ILE LEU ASP GLN LEU GLY
SEQRES 8 D 276 VAL GLU THR PHE LEU PRO VAL SER HIS SER HIS GLY GLY
SEQRES 9 D 276 TRP VAL LEU VAL GLU LEU LEU GLU GLN ALA GLY PRO GLU
SEQRES 10 D 276 ARG ALA PRO ARG GLY ILE ILE MET ASP TRP LEU MET TRP
SEQRES 11 D 276 ALA PRO LYS PRO ASP PHE ALA LYS SER LEU THR LEU LEU
SEQRES 12 D 276 LYS ASP PRO GLU ARG TRP ARG GLU GLY THR HIS GLY LEU
SEQRES 13 D 276 PHE ASP VAL TRP LEU ASP GLY HIS ASP GLU LYS ARG VAL
SEQRES 14 D 276 ARG HIS HIS LEU LEU GLU GLU MET ALA ASP TYR GLY TYR
SEQRES 15 D 276 ASP CYS TRP GLY ARG SER GLY ARG VAL ILE GLU ASP ALA
SEQRES 16 D 276 TYR GLY ARG ASN GLY SER PRO MET GLN MET MET ALA ASN
SEQRES 17 D 276 LEU THR LYS THR ARG PRO ILE ARG HIS ILE PHE SER GLN
SEQRES 18 D 276 PRO THR GLU PRO GLU TYR GLU LYS ILE ASN SER ASP PHE
SEQRES 19 D 276 ALA GLU GLN HIS PRO TRP PHE SER TYR ALA LYS LEU GLY
SEQRES 20 D 276 GLY PRO THR HIS PHE PRO ALA ILE ASP VAL PRO ASP ARG
SEQRES 21 D 276 ALA ALA VAL HIS ILE ARG GLU PHE ALA THR ALA ILE ARG
SEQRES 22 D 276 GLN GLY GLN
HET GOL A1276 6
HET GOL C1275 6
HET GOL D1275 6
HET GOL B1276 6
HET GOL C1276 6
HET GOL A1277 6
HET GOL A1278 6
HET GOL A1279 6
HET GOL A1280 6
HET GOL A1281 6
HET GOL C1277 6
HET GOL B1277 6
HET GOL D1276 6
HET GOL C1278 6
HET GOL B1278 6
HET GOL B1279 6
HET GOL B1280 6
HET K C1279 1
HET K A1282 1
HET K D1277 1
HET K B1281 1
HET K A1283 1
HET ZZ8 A1284 13
HET ZZ8 B1282 13
HET ZZ8 C1280 13
HET ZZ8 D1278 13
HET SRT A1285 10
HET SRT B1283 10
HET SRT C1281 10
HET SRT D1279 10
HET SRT A1286 10
HETNAM K POTASSIUM ION
HETNAM ZZ8 2-(ACETYLAMINO)BENZOIC ACID
HETNAM GOL GLYCEROL
HETNAM SRT S,R MESO-TARTARIC ACID
HETSYN ZZ8 N-ACETYLANTHRANILATE
FORMUL 5 ZZ8 4(C9 H9 N O3)
FORMUL 6 GOL 17(C3 H8 O3)
FORMUL 7 SRT 5(C4 H6 O6)
FORMUL 8 HOH *741(H2 O)
HELIX 1 1 THR A 2 THR A 4 5 3
HELIX 2 2 ASP A 39 VAL A 42 5 4
HELIX 3 3 TYR A 43 ASP A 51 1 9
HELIX 4 4 GLY A 75 GLY A 91 1 17
HELIX 5 5 GLY A 103 ALA A 119 1 17
HELIX 6 6 LYS A 133 ASP A 145 1 13
HELIX 7 7 ARG A 148 ASP A 162 1 15
HELIX 8 8 GLU A 166 GLU A 175 1 10
HELIX 9 9 GLY A 181 GLY A 200 1 20
HELIX 10 10 SER A 201 ASN A 208 1 8
HELIX 11 11 GLU A 224 HIS A 238 1 15
HELIX 12 12 PHE A 252 VAL A 257 1 6
HELIX 13 13 VAL A 257 GLN A 274 1 18
HELIX 14 14 ASP B 39 VAL B 42 5 4
HELIX 15 15 TYR B 43 ASP B 51 1 9
HELIX 16 16 GLY B 75 GLY B 91 1 17
HELIX 17 17 GLY B 103 ALA B 119 1 17
HELIX 18 18 LYS B 133 ASP B 145 1 13
HELIX 19 19 ARG B 148 ASP B 162 1 15
HELIX 20 20 GLU B 166 GLU B 175 1 10
HELIX 21 21 GLY B 181 GLY B 200 1 20
HELIX 22 22 SER B 201 ASN B 208 1 8
HELIX 23 23 GLU B 224 HIS B 238 1 15
HELIX 24 24 PHE B 252 VAL B 257 1 6
HELIX 25 25 VAL B 257 GLN B 274 1 18
HELIX 26 26 ASP C 39 VAL C 42 5 4
HELIX 27 27 TYR C 43 ASP C 51 1 9
HELIX 28 28 GLY C 75 GLY C 91 1 17
HELIX 29 29 GLY C 103 ALA C 119 1 17
HELIX 30 30 LYS C 133 ASP C 145 1 13
HELIX 31 31 ARG C 148 ASP C 162 1 15
HELIX 32 32 GLU C 166 GLU C 175 1 10
HELIX 33 33 GLY C 181 GLY C 200 1 20
HELIX 34 34 SER C 201 ASN C 208 1 8
HELIX 35 35 GLU C 224 HIS C 238 1 15
HELIX 36 36 PHE C 252 VAL C 257 1 6
HELIX 37 37 VAL C 257 GLN C 274 1 18
HELIX 38 38 THR D 2 THR D 4 5 3
HELIX 39 39 ASP D 39 VAL D 42 5 4
HELIX 40 40 TYR D 43 ASP D 51 1 9
HELIX 41 41 GLY D 75 GLY D 91 1 17
HELIX 42 42 GLY D 103 ALA D 119 1 17
HELIX 43 43 LYS D 133 ASP D 145 1 13
HELIX 44 44 ARG D 148 ASP D 162 1 15
HELIX 45 45 GLU D 166 GLU D 175 1 10
HELIX 46 46 GLY D 181 GLY D 200 1 20
HELIX 47 47 SER D 201 ASN D 208 1 8
HELIX 48 48 GLU D 224 HIS D 238 1 15
HELIX 49 49 PHE D 252 VAL D 257 1 6
HELIX 50 50 VAL D 257 GLN D 274 1 18
SHEET 1 AA 8 LEU A 6 VAL A 11 0
SHEET 2 AA 8 ASN A 14 ASP A 20 -1 O ASN A 14 N VAL A 11
SHEET 3 AA 8 VAL A 56 PRO A 59 -1 O VAL A 58 N ILE A 19
SHEET 4 AA 8 ALA A 29 LEU A 33 1 O ILE A 30 N ILE A 57
SHEET 5 AA 8 PHE A 95 HIS A 100 1 O LEU A 96 N LEU A 31
SHEET 6 AA 8 GLY A 122 MET A 125 1 O ILE A 123 N SER A 99
SHEET 7 AA 8 ILE A 215 PHE A 219 1 O ARG A 216 N ILE A 124
SHEET 8 AA 8 PHE A 241 LYS A 245 1 O SER A 242 N HIS A 217
SHEET 1 BA 8 LEU B 6 VAL B 11 0
SHEET 2 BA 8 ASN B 14 ASP B 20 -1 O ASN B 14 N VAL B 11
SHEET 3 BA 8 VAL B 56 PRO B 59 -1 O VAL B 58 N ILE B 19
SHEET 4 BA 8 ALA B 29 LEU B 33 1 O ILE B 30 N ILE B 57
SHEET 5 BA 8 PHE B 95 HIS B 100 1 O LEU B 96 N LEU B 31
SHEET 6 BA 8 GLY B 122 MET B 125 1 O ILE B 123 N SER B 99
SHEET 7 BA 8 ILE B 215 PHE B 219 1 O ARG B 216 N ILE B 124
SHEET 8 BA 8 PHE B 241 LYS B 245 1 O SER B 242 N HIS B 217
SHEET 1 CA 8 LEU C 6 VAL C 11 0
SHEET 2 CA 8 ASN C 14 ASP C 20 -1 O ASN C 14 N VAL C 11
SHEET 3 CA 8 VAL C 56 PRO C 59 -1 O VAL C 58 N ILE C 19
SHEET 4 CA 8 ALA C 29 LEU C 33 1 O ILE C 30 N ILE C 57
SHEET 5 CA 8 PHE C 95 HIS C 100 1 O LEU C 96 N LEU C 31
SHEET 6 CA 8 GLY C 122 MET C 125 1 O ILE C 123 N SER C 99
SHEET 7 CA 8 ILE C 215 PHE C 219 1 O ARG C 216 N ILE C 124
SHEET 8 CA 8 PHE C 241 LYS C 245 1 O SER C 242 N HIS C 217
SHEET 1 DA 8 LEU D 6 VAL D 11 0
SHEET 2 DA 8 ASN D 14 ASP D 20 -1 O ASN D 14 N VAL D 11
SHEET 3 DA 8 VAL D 56 PRO D 59 -1 O VAL D 58 N ILE D 19
SHEET 4 DA 8 ALA D 29 LEU D 33 1 O ILE D 30 N ILE D 57
SHEET 5 DA 8 PHE D 95 HIS D 100 1 O LEU D 96 N LEU D 31
SHEET 6 DA 8 GLY D 122 MET D 125 1 O ILE D 123 N SER D 99
SHEET 7 DA 8 ILE D 215 PHE D 219 1 O ARG D 216 N ILE D 124
SHEET 8 DA 8 PHE D 241 LYS D 245 1 O SER D 242 N HIS D 217
SSBOND 1 CYS A 37 CYS A 184 1555 1555 2.04
SSBOND 2 CYS B 37 CYS B 184 1555 1555 2.05
SSBOND 3 CYS C 37 CYS C 184 1555 1555 2.12
SSBOND 4 CYS D 37 CYS D 184 1555 1555 2.08
LINK K K A1282 O HIS A 238 1555 1555 2.74
LINK K K A1282 O HOH A2169 1555 1555 2.44
LINK K K A1282 O ALA A 235 1555 1555 2.53
LINK K K A1282 O3 GOL A1276 1555 1555 2.36
LINK K K A1282 O HOH D2086 1555 4456 3.00
LINK K K A1282 O PHE A 241 1555 1555 2.60
LINK K K A1282 O2 GOL A1276 1555 1555 3.04
LINK K K A1283 O41 SRT A1286 1555 1555 2.88
LINK K K A1283 O ASP A 165 1555 1555 2.67
LINK K K A1283 O11 SRT A1286 1555 1555 2.86
LINK K K A1283 O HOH A2099 1555 1555 3.07
LINK K K A1283 O3 SRT A1286 1555 1555 3.01
LINK K K A1283 O HOH A2098 1555 1555 3.16
LINK K K B1281 O HIS B 238 1555 1555 2.68
LINK K K B1281 O ALA B 235 1555 1555 2.50
LINK K K B1281 O HOH B2158 1555 1555 2.77
LINK K K B1281 O PHE B 241 1555 1555 2.59
LINK K K B1281 O2 GOL C1276 1555 4456 2.98
LINK K K B1281 O3 GOL C1276 1555 4456 2.53
LINK K K B1281 O HOH C2126 1555 4456 2.95
LINK O3 GOL C1276 K K B1281 1555 4556 2.53
LINK O2 GOL C1276 K K B1281 1555 4556 2.98
LINK K K C1279 O ALA C 235 1555 1555 2.84
LINK K K C1279 O HOH C2191 1555 1555 2.45
LINK K K C1279 O PHE C 241 1555 1555 2.43
LINK K K C1279 O HOH C2184 1555 1555 2.72
LINK K K C1279 O HIS C 238 1555 1555 2.99
LINK K K C1279 O HOH C2185 1555 1555 2.99
LINK K K D1277 O HOH D2137 1555 1555 2.37
LINK K K D1277 O PHE D 241 1555 1555 2.48
LINK K K D1277 O HIS D 238 1555 1555 3.07
LINK K K D1277 O ALA D 235 1555 1555 2.87
LINK K K D1277 O HOH D2134 1555 1555 2.74
CISPEP 1 GLY A 27 PRO A 28 0 0.32
CISPEP 2 GLN A 221 PRO A 222 0 -4.40
CISPEP 3 GLY B 27 PRO B 28 0 -1.80
CISPEP 4 GLN B 221 PRO B 222 0 -7.15
CISPEP 5 GLY C 27 PRO C 28 0 0.51
CISPEP 6 GLN C 221 PRO C 222 0 -7.22
CISPEP 7 GLY D 27 PRO D 28 0 -2.50
CISPEP 8 GLN D 221 PRO D 222 0 -8.76
SITE 1 AC1 6 ALA A 235 PHE A 241 K A1282 ASP D 158
SITE 2 AC1 6 ASP D 162 GLY D 163
SITE 1 AC2 4 ASP C 53 ARG C 273 HOH C2048 HOH C2214
SITE 1 AC3 4 THR D 4 TYR D 5 ALA D 207 HIS D 238
SITE 1 AC4 3 THR B 2 PHE B 234 HIS B 238
SITE 1 AC5 6 ALA B 235 PHE B 241 TYR B 243 K B1281
SITE 2 AC5 6 HOH B2158 ASP C 158
SITE 1 AC6 3 TRP A 149 ARG A 150 HOH A2170
SITE 1 AC7 8 LEU A 128 TRP A 130 ALA A 131 PRO A 132
SITE 2 AC7 8 LYS A 133 PHE A 136 TYR A 196 GOL A1279
SITE 1 AC8 7 LEU A 128 PHE A 136 VAL A 159 TRP A 160
SITE 2 AC8 7 GOL A1278 HOH A2141 HOH A2173
SITE 1 AC9 4 LYS A 245 LEU A 246 GLY A 247 GOL A1281
SITE 1 BC1 7 LYS A 245 GOL A1280 HOH A2171 HIS D 164
SITE 2 BC1 7 ASP D 165 GLU D 166 HOH D2093
SITE 1 BC2 12 SER C 101 HIS C 102 ASP C 126 TRP C 127
SITE 2 BC2 12 LEU C 128 PHE C 136 TRP C 160 HIS C 251
SITE 3 BC2 12 ZZ8 C1280 HOH C2100 HOH C2173 HOH C2215
SITE 1 BC3 5 LYS B 245 LEU B 246 GLY B 247 GOL B1280
SITE 2 BC3 5 HOH B2181
SITE 1 BC4 10 SER D 101 HIS D 102 ASP D 126 TRP D 127
SITE 2 BC4 10 LEU D 128 PHE D 136 TRP D 160 HIS D 251
SITE 3 BC4 10 ZZ8 D1278 HOH D2125
SITE 1 BC5 6 GLY C 75 TYR C 76 GLN C 77 VAL C 191
SITE 2 BC5 6 ASP C 194 ALA C 195
SITE 1 BC6 8 HIS B 164 ASP B 165 GOL B1279 HOH B2110
SITE 2 BC6 8 HOH B2184 LYS D 245 LEU D 246 GLY D 247
SITE 1 BC7 3 GOL B1278 HOH B2185 GLY D 247
SITE 1 BC8 5 LYS B 245 GOL B1277 HIS C 164 ASP C 165
SITE 2 BC8 5 GLU C 166
SITE 1 BC9 6 ALA C 235 HIS C 238 PHE C 241 HOH C2184
SITE 2 BC9 6 HOH C2185 HOH C2191
SITE 1 CC1 7 ALA A 235 HIS A 238 PRO A 239 PHE A 241
SITE 2 CC1 7 GOL A1276 HOH A2169 HOH D2086
SITE 1 CC2 6 ALA D 235 HIS D 238 PRO D 239 PHE D 241
SITE 2 CC2 6 HOH D2134 HOH D2137
SITE 1 CC3 7 ALA B 235 HIS B 238 PRO B 239 PHE B 241
SITE 2 CC3 7 HOH B2158 GOL C1276 HOH C2126
SITE 1 CC4 3 ASP A 165 SRT A1286 HOH A2099
SITE 1 CC5 12 TRP A 36 HIS A 38 HIS A 100 SER A 101
SITE 2 CC5 12 HIS A 102 TRP A 160 TRP A 185 SER A 188
SITE 3 CC5 12 ILE A 192 HIS A 251 HOH A2172 HOH A2173
SITE 1 CC6 11 TRP B 36 HIS B 38 HIS B 100 SER B 101
SITE 2 CC6 11 HIS B 102 TRP B 160 TRP B 185 SER B 188
SITE 3 CC6 11 ILE B 192 HIS B 251 HOH B2188
SITE 1 CC7 12 TRP C 36 HIS C 38 HIS C 100 SER C 101
SITE 2 CC7 12 HIS C 102 TRP C 160 TRP C 185 SER C 188
SITE 3 CC7 12 ILE C 192 HIS C 251 GOL C1277 HOH C2036
SITE 1 CC8 11 TRP D 36 HIS D 38 HIS D 100 SER D 101
SITE 2 CC8 11 HIS D 102 TRP D 160 TRP D 185 SER D 188
SITE 3 CC8 11 ILE D 192 HIS D 251 GOL D1276
SITE 1 CC9 7 LYS A 167 ARG A 170 HIS A 171 HOH A2175
SITE 2 CC9 7 HOH A2176 ARG C 260 VAL C 263
SITE 1 DC1 7 LYS B 167 ARG B 170 HIS B 171 HOH B2189
SITE 2 DC1 7 HOH B2190 ARG D 260 VAL D 263
SITE 1 DC2 6 ARG B 260 VAL B 263 LYS C 167 ARG C 170
SITE 2 DC2 6 HIS C 171 HOH C2216
SITE 1 DC3 6 ARG A 260 VAL A 263 LYS D 167 ARG D 170
SITE 2 DC3 6 HIS D 171 HOH D2156
SITE 1 DC4 9 HIS A 164 ASP A 165 K A1283 HOH A2177
SITE 2 DC4 9 HOH A2178 HOH A2179 LYS C 245 LEU C 246
SITE 3 DC4 9 GLY C 247
CRYST1 44.940 167.090 167.230 90.00 90.00 90.00 P 21 21 21 16
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 0.022252 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005985 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005980 0.00000
MTRIX1 1 0.999720 0.023660 0.001690 -0.31260 1
MTRIX2 1 -0.023640 0.999650 -0.012140 69.46461 1
MTRIX3 1 -0.001980 0.012100 0.999920 -68.01957 1
MTRIX1 2 0.999840 -0.011960 0.013200 -10.93569 1
MTRIX2 2 -0.013030 0.014550 0.999810 25.12310 1
MTRIX3 2 -0.012150 -0.999820 0.014390 124.95824 1
MTRIX1 3 0.999930 0.004060 0.011140 -12.39966 1
MTRIX2 3 -0.011120 -0.005370 0.999920 -41.50198 1
MTRIX3 3 0.004120 -0.999980 -0.005330 57.89408 1
TER 2235 GLY A 275
TER 4470 GLY B 275
TER 6707 GLN C 274
TER 8950 GLN D 274
MASTER 627 0 31 50 32 0 62 15 9896 4 242 88
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