| content |
HEADER HYDROLASE 29-JUN-09 2WM2
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 IN COMPLEX WITH CHLORIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 1-H-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 HYDROLASE, ALPHA/BETA HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.A.STEINER
REVDAT 1 26-JAN-10 2WM2 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. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0093
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) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.38
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.64
REMARK 3 NUMBER OF REFLECTIONS : 33360
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) : 0.21272
REMARK 3 R VALUE (WORKING SET) : 0.21094
REMARK 3 FREE R VALUE : 0.24569
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT : 1786
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) : 2.698
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.768
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2349
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.51
REMARK 3 BIN R VALUE (WORKING SET) : 0.407
REMARK 3 BIN FREE R VALUE SET COUNT : 98
REMARK 3 BIN FREE R VALUE : 0.513
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9012
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 142
REMARK 3 SOLVENT ATOMS : 162
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 70.1
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.303
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.67
REMARK 3 B22 (A**2) : 2.43
REMARK 3 B33 (A**2) : -4.10
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
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.076
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.260
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.071
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.924
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.890
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9408 ; 0.009 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 6454 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12791 ; 1.073 ; 1.948
REMARK 3 BOND ANGLES OTHERS (DEGREES): 15574 ; 0.808 ; 3.001
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1105 ; 5.742 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 489 ;37.564 ;23.374
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1480 ;14.389 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 73 ;18.887 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1304 ; 0.061 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 10499 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1994 ; 0.002 ; 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): 5512 ; 0.360 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2213 ; 0.065 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8902 ; 0.702 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3896 ; 0.944 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3886 ; 1.633 ; 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 ; 0.02 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 B (A): 1575 ; 0.02 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 C (A): 1575 ; 0.02 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 D (A): 1575 ; 0.02 ; 0.05
REMARK 3 LOOSE POSITIONAL 1 A (A): 2162 ; 0.02 ; 5.00
REMARK 3 LOOSE POSITIONAL 1 B (A): 2162 ; 0.02 ; 5.00
REMARK 3 LOOSE POSITIONAL 1 C (A): 2162 ; 0.02 ; 5.00
REMARK 3 LOOSE POSITIONAL 1 D (A): 2162 ; 0.02 ; 5.00
REMARK 3 TIGHT THERMAL 1 A (A**2): 1575 ; 0.04 ; 0.50
REMARK 3 TIGHT THERMAL 1 B (A**2): 1575 ; 0.04 ; 0.50
REMARK 3 TIGHT THERMAL 1 C (A**2): 1575 ; 0.04 ; 0.50
REMARK 3 TIGHT THERMAL 1 D (A**2): 1575 ; 0.04 ; 0.50
REMARK 3 LOOSE THERMAL 1 A (A**2): 2162 ; 0.04 ; 10.00
REMARK 3 LOOSE THERMAL 1 B (A**2): 2162 ; 0.04 ; 10.00
REMARK 3 LOOSE THERMAL 1 C (A**2): 2162 ; 0.05 ; 10.00
REMARK 3 LOOSE THERMAL 1 D (A**2): 2162 ; 0.04 ; 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 : 0.527
REMARK 3 TWIN DOMAIN : 2
REMARK 3 TWIN OPERATOR : -H, L, K
REMARK 3 TWIN FRACTION : 0.473
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH 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 3 EXTRA RESIDUES BELONGING TO THE N-TERMINAL PURIFICATION
REMARK 3 TAG ARE VISIBLE IN SOME OF THE CHAINS
REMARK 4
REMARK 4 2WM2 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 29-JUN-09.
REMARK 100 THE PDBE ID CODE IS EBI-40282.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-MAY-09
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) : 2.06640
REMARK 200 MONOCHROMATOR : SI (111) DOUBLE CRYSTAL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD (Q315)
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 : 35477
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.70
REMARK 200 RESOLUTION RANGE LOW (A) : 55.64
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 200 DATA REDUNDANCY : 5.4
REMARK 200 R MERGE (I) : 0.13
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 12.80
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.1
REMARK 200 DATA REDUNDANCY IN SHELL : 5.1
REMARK 200 R MERGE FOR SHELL (I) : 0.44
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.30
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: NONE
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.32
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.45
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: HIS6-HOD AT 150 MG/ML IN
REMARK 280 STORAGE BUFFER IN THE PRESENCE OF A RESERVOIR COMPOSED OF
REMARK 280 1.65 M SODIUM/POTASSIUM TARTRATE, 0.1 M HEPES PH 7.0
REMARK 280 SOAKING WITH 1M NACL FOR 60 SECONDS
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 22.88500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 83.47000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 83.50000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 83.47000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 22.88500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 83.50000
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 HIS A -2
REMARK 465 GLY A -1
REMARK 465 SER A 0
REMARK 465 MET A 1
REMARK 465 GLN A 276
REMARK 465 HIS B -2
REMARK 465 GLY B -1
REMARK 465 SER B 0
REMARK 465 GLN B 276
REMARK 465 GLY C 275
REMARK 465 GLN C 276
REMARK 465 GLY D 275
REMARK 465 GLN D 276
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. = -15.0 DEGREES
REMARK 500 PRO B 59 C - N - CD ANGL. DEV. = -15.8 DEGREES
REMARK 500 PRO B 116 C - N - CD ANGL. DEV. = -13.4 DEGREES
REMARK 500 PRO C 59 C - N - CD ANGL. DEV. = -15.1 DEGREES
REMARK 500 PRO D 59 C - N - CD ANGL. DEV. = -14.5 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 -115.26 53.81
REMARK 500 ASP A 20 115.16 -164.84
REMARK 500 GLN A 22 12.43 50.44
REMARK 500 HIS A 40 -27.02 -39.56
REMARK 500 GLU A 93 -69.48 -103.62
REMARK 500 SER A 101 -129.32 44.45
REMARK 500 ASP A 126 75.62 34.13
REMARK 500 LEU A 128 107.35 -58.84
REMARK 500 ASP A 165 58.85 -94.64
REMARK 500 ASP B 3 61.22 -171.30
REMARK 500 PHE B 12 -115.75 54.05
REMARK 500 ASP B 20 114.64 -165.13
REMARK 500 GLN B 22 14.39 50.18
REMARK 500 GLU B 93 -69.26 -104.40
REMARK 500 SER B 101 -128.60 44.08
REMARK 500 ASP B 126 76.32 34.36
REMARK 500 ASP B 165 58.62 -96.12
REMARK 500 MET C 1 5.13 89.76
REMARK 500 THR C 2 -34.04 -39.42
REMARK 500 ASP C 3 -18.18 -48.76
REMARK 500 PHE C 12 -114.39 55.12
REMARK 500 ASP C 20 113.45 -167.00
REMARK 500 GLN C 22 13.85 50.45
REMARK 500 GLU C 93 -68.40 -105.08
REMARK 500 SER C 101 -129.27 43.51
REMARK 500 ASP C 126 75.49 35.42
REMARK 500 SER D 0 -178.90 -173.49
REMARK 500 PHE D 12 -115.48 54.90
REMARK 500 ASP D 20 113.24 -164.43
REMARK 500 GLN D 22 15.32 49.88
REMARK 500 GLU D 93 -69.17 -104.50
REMARK 500 SER D 101 -127.52 44.23
REMARK 500 ASP D 126 76.61 35.13
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 A1279 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA A 235 O
REMARK 620 2 HIS A 238 O 61.2
REMARK 620 3 PRO A 239 O 125.3 66.3
REMARK 620 4 PHE A 241 O 96.5 75.1 83.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K B1278 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA B 235 O
REMARK 620 2 PRO B 239 O 126.3
REMARK 620 3 HOH C2025 O 139.7 60.0
REMARK 620 4 HIS B 238 O 61.4 67.5 120.3
REMARK 620 5 PHE B 241 O 96.1 88.6 124.1 78.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K C1277 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA C 235 O
REMARK 620 2 HIS C 238 O 56.8
REMARK 620 3 PHE C 241 O 101.9 71.4
REMARK 620 N 1 2
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 ALA D 235 O
REMARK 620 2 HIS D 238 O 57.0
REMARK 620 3 PHE D 241 O 98.3 70.3
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA C1279 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR C 180 O
REMARK 620 2 MET C 177 O 94.3
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA D1279 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER D 220 OG
REMARK 620 2 THR D 250 O 94.4
REMARK 620 3 ASP D 256 OD1 137.7 127.5
REMARK 620 4 ASP D 256 OD2 153.5 86.6 45.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA C1278 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER C 220 OG
REMARK 620 2 THR C 250 O 94.9
REMARK 620 3 ASP C 256 OD1 132.0 129.8
REMARK 620 4 ASP C 256 OD2 143.2 88.4 44.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA D1278 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR D 180 O
REMARK 620 2 MET D 177 O 104.1
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA D1300 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SRT A1287 O2
REMARK 620 2 SRT A1287 O1 53.4
REMARK 620 N 1
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 SRT A1277
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1278
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 C1275
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C1276
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B1277
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D1275
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D1276
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C1277
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A1279
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K D1277
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B1278
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA D1278
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA D1279
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA C1278
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA C1279
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B1279
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA C1280
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A1280
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA D1300
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA C1281
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B1281
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1281
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B1282
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C1282
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D1280
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1282
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1283
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D1302
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1284
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SRT A1285
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SRT B1283
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SRT C1283
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SRT A1286
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SRT B1284
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SRT A1287
REMARK 900
REMARK 900 RELATED ENTRIES
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
REMARK 900 RELATED ID: 2WJ6 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 COMPLEXED WITH ITS
REMARK 900 NATURAL SUBSTRATE N-ACETYLANTHRANILATE
DBREF 2WM2 A -2 0 PDB 2WM2 2WM2 -2 0
DBREF 2WM2 A 1 276 UNP A4V8M9 A4V8M9_9MICC 1 276
DBREF 2WM2 B -2 0 PDB 2WM2 2WM2 -2 0
DBREF 2WM2 B 1 276 UNP A4V8M9 A4V8M9_9MICC 1 276
DBREF 2WM2 C -2 0 PDB 2WM2 2WM2 -2 0
DBREF 2WM2 C 1 276 UNP A4V8M9 A4V8M9_9MICC 1 276
DBREF 2WM2 D -2 0 PDB 2WM2 2WM2 -2 0
DBREF 2WM2 D 1 276 UNP A4V8M9 A4V8M9_9MICC 1 276
SEQADV 2WM2 SER A 69 UNP A4V8M9 CYS 69 ENGINEERED MUTATION
SEQADV 2WM2 SER B 69 UNP A4V8M9 CYS 69 ENGINEERED MUTATION
SEQADV 2WM2 SER C 69 UNP A4V8M9 CYS 69 ENGINEERED MUTATION
SEQADV 2WM2 SER D 69 UNP A4V8M9 CYS 69 ENGINEERED MUTATION
SEQRES 1 A 279 HIS GLY SER MET THR ASP THR TYR LEU HIS GLU THR LEU
SEQRES 2 A 279 VAL PHE ASP ASN LYS LEU SER TYR ILE ASP ASN GLN ARG
SEQRES 3 A 279 ASP THR ASP GLY PRO ALA ILE LEU LEU LEU PRO GLY TRP
SEQRES 4 A 279 CYS HIS ASP HIS ARG VAL TYR LYS TYR LEU ILE GLN GLU
SEQRES 5 A 279 LEU ASP ALA ASP PHE ARG VAL ILE VAL PRO ASN TRP ARG
SEQRES 6 A 279 GLY HIS GLY LEU SER PRO SER GLU VAL PRO ASP PHE GLY
SEQRES 7 A 279 TYR GLN GLU GLN VAL LYS ASP ALA LEU GLU ILE LEU ASP
SEQRES 8 A 279 GLN LEU GLY VAL GLU THR PHE LEU PRO VAL SER HIS SER
SEQRES 9 A 279 HIS GLY GLY TRP VAL LEU VAL GLU LEU LEU GLU GLN ALA
SEQRES 10 A 279 GLY PRO GLU ARG ALA PRO ARG GLY ILE ILE MET ASP TRP
SEQRES 11 A 279 LEU MET TRP ALA PRO LYS PRO ASP PHE ALA LYS SER LEU
SEQRES 12 A 279 THR LEU LEU LYS ASP PRO GLU ARG TRP ARG GLU GLY THR
SEQRES 13 A 279 HIS GLY LEU PHE ASP VAL TRP LEU ASP GLY HIS ASP GLU
SEQRES 14 A 279 LYS ARG VAL ARG HIS HIS LEU LEU GLU GLU MET ALA ASP
SEQRES 15 A 279 TYR GLY TYR ASP CYS TRP GLY ARG SER GLY ARG VAL ILE
SEQRES 16 A 279 GLU ASP ALA TYR GLY ARG ASN GLY SER PRO MET GLN MET
SEQRES 17 A 279 MET ALA ASN LEU THR LYS THR ARG PRO ILE ARG HIS ILE
SEQRES 18 A 279 PHE SER GLN PRO THR GLU PRO GLU TYR GLU LYS ILE ASN
SEQRES 19 A 279 SER ASP PHE ALA GLU GLN HIS PRO TRP PHE SER TYR ALA
SEQRES 20 A 279 LYS LEU GLY GLY PRO THR HIS PHE PRO ALA ILE ASP VAL
SEQRES 21 A 279 PRO ASP ARG ALA ALA VAL HIS ILE ARG GLU PHE ALA THR
SEQRES 22 A 279 ALA ILE ARG GLN GLY GLN
SEQRES 1 B 279 HIS GLY SER MET THR ASP THR TYR LEU HIS GLU THR LEU
SEQRES 2 B 279 VAL PHE ASP ASN LYS LEU SER TYR ILE ASP ASN GLN ARG
SEQRES 3 B 279 ASP THR ASP GLY PRO ALA ILE LEU LEU LEU PRO GLY TRP
SEQRES 4 B 279 CYS HIS ASP HIS ARG VAL TYR LYS TYR LEU ILE GLN GLU
SEQRES 5 B 279 LEU ASP ALA ASP PHE ARG VAL ILE VAL PRO ASN TRP ARG
SEQRES 6 B 279 GLY HIS GLY LEU SER PRO SER GLU VAL PRO ASP PHE GLY
SEQRES 7 B 279 TYR GLN GLU GLN VAL LYS ASP ALA LEU GLU ILE LEU ASP
SEQRES 8 B 279 GLN LEU GLY VAL GLU THR PHE LEU PRO VAL SER HIS SER
SEQRES 9 B 279 HIS GLY GLY TRP VAL LEU VAL GLU LEU LEU GLU GLN ALA
SEQRES 10 B 279 GLY PRO GLU ARG ALA PRO ARG GLY ILE ILE MET ASP TRP
SEQRES 11 B 279 LEU MET TRP ALA PRO LYS PRO ASP PHE ALA LYS SER LEU
SEQRES 12 B 279 THR LEU LEU LYS ASP PRO GLU ARG TRP ARG GLU GLY THR
SEQRES 13 B 279 HIS GLY LEU PHE ASP VAL TRP LEU ASP GLY HIS ASP GLU
SEQRES 14 B 279 LYS ARG VAL ARG HIS HIS LEU LEU GLU GLU MET ALA ASP
SEQRES 15 B 279 TYR GLY TYR ASP CYS TRP GLY ARG SER GLY ARG VAL ILE
SEQRES 16 B 279 GLU ASP ALA TYR GLY ARG ASN GLY SER PRO MET GLN MET
SEQRES 17 B 279 MET ALA ASN LEU THR LYS THR ARG PRO ILE ARG HIS ILE
SEQRES 18 B 279 PHE SER GLN PRO THR GLU PRO GLU TYR GLU LYS ILE ASN
SEQRES 19 B 279 SER ASP PHE ALA GLU GLN HIS PRO TRP PHE SER TYR ALA
SEQRES 20 B 279 LYS LEU GLY GLY PRO THR HIS PHE PRO ALA ILE ASP VAL
SEQRES 21 B 279 PRO ASP ARG ALA ALA VAL HIS ILE ARG GLU PHE ALA THR
SEQRES 22 B 279 ALA ILE ARG GLN GLY GLN
SEQRES 1 C 279 HIS GLY SER MET THR ASP THR TYR LEU HIS GLU THR LEU
SEQRES 2 C 279 VAL PHE ASP ASN LYS LEU SER TYR ILE ASP ASN GLN ARG
SEQRES 3 C 279 ASP THR ASP GLY PRO ALA ILE LEU LEU LEU PRO GLY TRP
SEQRES 4 C 279 CYS HIS ASP HIS ARG VAL TYR LYS TYR LEU ILE GLN GLU
SEQRES 5 C 279 LEU ASP ALA ASP PHE ARG VAL ILE VAL PRO ASN TRP ARG
SEQRES 6 C 279 GLY HIS GLY LEU SER PRO SER GLU VAL PRO ASP PHE GLY
SEQRES 7 C 279 TYR GLN GLU GLN VAL LYS ASP ALA LEU GLU ILE LEU ASP
SEQRES 8 C 279 GLN LEU GLY VAL GLU THR PHE LEU PRO VAL SER HIS SER
SEQRES 9 C 279 HIS GLY GLY TRP VAL LEU VAL GLU LEU LEU GLU GLN ALA
SEQRES 10 C 279 GLY PRO GLU ARG ALA PRO ARG GLY ILE ILE MET ASP TRP
SEQRES 11 C 279 LEU MET TRP ALA PRO LYS PRO ASP PHE ALA LYS SER LEU
SEQRES 12 C 279 THR LEU LEU LYS ASP PRO GLU ARG TRP ARG GLU GLY THR
SEQRES 13 C 279 HIS GLY LEU PHE ASP VAL TRP LEU ASP GLY HIS ASP GLU
SEQRES 14 C 279 LYS ARG VAL ARG HIS HIS LEU LEU GLU GLU MET ALA ASP
SEQRES 15 C 279 TYR GLY TYR ASP CYS TRP GLY ARG SER GLY ARG VAL ILE
SEQRES 16 C 279 GLU ASP ALA TYR GLY ARG ASN GLY SER PRO MET GLN MET
SEQRES 17 C 279 MET ALA ASN LEU THR LYS THR ARG PRO ILE ARG HIS ILE
SEQRES 18 C 279 PHE SER GLN PRO THR GLU PRO GLU TYR GLU LYS ILE ASN
SEQRES 19 C 279 SER ASP PHE ALA GLU GLN HIS PRO TRP PHE SER TYR ALA
SEQRES 20 C 279 LYS LEU GLY GLY PRO THR HIS PHE PRO ALA ILE ASP VAL
SEQRES 21 C 279 PRO ASP ARG ALA ALA VAL HIS ILE ARG GLU PHE ALA THR
SEQRES 22 C 279 ALA ILE ARG GLN GLY GLN
SEQRES 1 D 279 HIS GLY SER MET THR ASP THR TYR LEU HIS GLU THR LEU
SEQRES 2 D 279 VAL PHE ASP ASN LYS LEU SER TYR ILE ASP ASN GLN ARG
SEQRES 3 D 279 ASP THR ASP GLY PRO ALA ILE LEU LEU LEU PRO GLY TRP
SEQRES 4 D 279 CYS HIS ASP HIS ARG VAL TYR LYS TYR LEU ILE GLN GLU
SEQRES 5 D 279 LEU ASP ALA ASP PHE ARG VAL ILE VAL PRO ASN TRP ARG
SEQRES 6 D 279 GLY HIS GLY LEU SER PRO SER GLU VAL PRO ASP PHE GLY
SEQRES 7 D 279 TYR GLN GLU GLN VAL LYS ASP ALA LEU GLU ILE LEU ASP
SEQRES 8 D 279 GLN LEU GLY VAL GLU THR PHE LEU PRO VAL SER HIS SER
SEQRES 9 D 279 HIS GLY GLY TRP VAL LEU VAL GLU LEU LEU GLU GLN ALA
SEQRES 10 D 279 GLY PRO GLU ARG ALA PRO ARG GLY ILE ILE MET ASP TRP
SEQRES 11 D 279 LEU MET TRP ALA PRO LYS PRO ASP PHE ALA LYS SER LEU
SEQRES 12 D 279 THR LEU LEU LYS ASP PRO GLU ARG TRP ARG GLU GLY THR
SEQRES 13 D 279 HIS GLY LEU PHE ASP VAL TRP LEU ASP GLY HIS ASP GLU
SEQRES 14 D 279 LYS ARG VAL ARG HIS HIS LEU LEU GLU GLU MET ALA ASP
SEQRES 15 D 279 TYR GLY TYR ASP CYS TRP GLY ARG SER GLY ARG VAL ILE
SEQRES 16 D 279 GLU ASP ALA TYR GLY ARG ASN GLY SER PRO MET GLN MET
SEQRES 17 D 279 MET ALA ASN LEU THR LYS THR ARG PRO ILE ARG HIS ILE
SEQRES 18 D 279 PHE SER GLN PRO THR GLU PRO GLU TYR GLU LYS ILE ASN
SEQRES 19 D 279 SER ASP PHE ALA GLU GLN HIS PRO TRP PHE SER TYR ALA
SEQRES 20 D 279 LYS LEU GLY GLY PRO THR HIS PHE PRO ALA ILE ASP VAL
SEQRES 21 D 279 PRO ASP ARG ALA ALA VAL HIS ILE ARG GLU PHE ALA THR
SEQRES 22 D 279 ALA ILE ARG GLN GLY GLN
HET GOL A1276 6
HET SRT A1277 10
HET GOL A1278 6
HET GOL B1276 6
HET GOL C1275 6
HET GOL C1276 6
HET GOL B1277 6
HET GOL D1275 6
HET GOL D1276 6
HET K C1277 1
HET K A1279 1
HET K D1277 1
HET K B1278 1
HET NA D1278 1
HET NA D1279 1
HET NA C1278 1
HET NA C1279 1
HET NA B1279 1
HET NA C1280 1
HET NA A1280 1
HET NA B1280 1
HET NA D1300 1
HET NA C1281 1
HET NA D1301 1
HET NA B1281 1
HET CL A1281 1
HET CL B1282 1
HET CL C1282 1
HET CL D1280 1
HET CL A1282 1
HET CL A1283 1
HET CL D1302 1
HET CL A1284 1
HET SRT A1285 10
HET SRT B1283 10
HET SRT C1283 10
HET SRT A1286 10
HET SRT B1284 10
HET SRT A1287 10
HETNAM K POTASSIUM ION
HETNAM GOL GLYCEROL
HETNAM NA SODIUM ION
HETNAM CL CHLORIDE ION
HETNAM SRT S,R MESO-TARTARIC ACID
FORMUL 5 GOL 8(C3 H8 O3)
FORMUL 6 NA 12(NA 1+)
FORMUL 7 CL 8(CL 1-)
FORMUL 8 SRT 7(C4 H6 O6)
FORMUL 9 HOH *162(H2 O)
HELIX 1 1 ASP A 39 VAL A 42 5 4
HELIX 2 2 TYR A 43 ASP A 51 1 9
HELIX 3 3 GLY A 75 LEU A 90 1 16
HELIX 4 4 GLY A 103 ALA A 119 1 17
HELIX 5 5 LYS A 133 ASP A 145 1 13
HELIX 6 6 ARG A 148 ASP A 162 1 15
HELIX 7 7 GLU A 166 GLU A 175 1 10
HELIX 8 8 GLY A 181 GLY A 200 1 20
HELIX 9 9 SER A 201 ASN A 208 1 8
HELIX 10 10 GLU A 224 HIS A 238 1 15
HELIX 11 11 PHE A 252 VAL A 257 1 6
HELIX 12 12 VAL A 257 ARG A 273 1 17
HELIX 13 13 ASP B 39 VAL B 42 5 4
HELIX 14 14 TYR B 43 ASP B 51 1 9
HELIX 15 15 GLY B 75 LEU B 90 1 16
HELIX 16 16 GLY B 103 ALA B 119 1 17
HELIX 17 17 LYS B 133 ASP B 145 1 13
HELIX 18 18 ARG B 148 ASP B 162 1 15
HELIX 19 19 GLU B 166 GLU B 175 1 10
HELIX 20 20 GLY B 181 GLY B 200 1 20
HELIX 21 21 SER B 201 ASN B 208 1 8
HELIX 22 22 GLU B 224 HIS B 238 1 15
HELIX 23 23 PHE B 252 VAL B 257 1 6
HELIX 24 24 VAL B 257 ARG B 273 1 17
HELIX 25 25 MET C 1 THR C 4 5 4
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 LEU C 90 1 16
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 ARG C 273 1 17
HELIX 38 38 ASP D 39 VAL D 42 5 4
HELIX 39 39 TYR D 43 ASP D 51 1 9
HELIX 40 40 GLY D 75 LEU D 90 1 16
HELIX 41 41 GLY D 103 ALA D 119 1 17
HELIX 42 42 LYS D 133 ASP D 145 1 13
HELIX 43 43 ARG D 148 ASP D 162 1 15
HELIX 44 44 GLU D 166 GLU D 175 1 10
HELIX 45 45 GLY D 181 GLY D 200 1 20
HELIX 46 46 SER D 201 ASN D 208 1 8
HELIX 47 47 GLU D 224 HIS D 238 1 15
HELIX 48 48 PHE D 252 VAL D 257 1 6
HELIX 49 49 VAL D 257 ARG D 273 1 17
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 2.06
SSBOND 2 CYS B 37 CYS B 184 1555 1555 2.06
SSBOND 3 CYS C 37 CYS C 184 1555 1555 2.05
SSBOND 4 CYS D 37 CYS D 184 1555 1555 2.04
LINK K K A1279 O ALA A 235 1555 1555 3.00
LINK K K A1279 O HIS A 238 1555 1555 3.07
LINK K K A1279 O PRO A 239 1555 1555 3.29
LINK K K A1279 O PHE A 241 1555 1555 2.76
LINK NA NA A1280 O HIS A 164 1555 1555 2.79
LINK K K B1278 O PRO B 239 1555 1555 3.10
LINK K K B1278 O HOH C2025 1555 4456 2.91
LINK K K B1278 O HIS B 238 1555 1555 3.00
LINK K K B1278 O PHE B 241 1555 1555 2.66
LINK K K B1278 O ALA B 235 1555 1555 3.06
LINK NA NA B1279 O HOH B2019 1555 1555 2.94
LINK NA NA B1281 O3 SRT B1284 1555 1555 3.11
LINK K K C1277 O PHE C 241 1555 1555 2.47
LINK K K C1277 O ALA C 235 1555 1555 3.12
LINK K K C1277 O HIS C 238 1555 1555 3.49
LINK NA NA C1278 OD1 ASP C 256 1555 1555 2.78
LINK NA NA C1278 OG SER C 220 1555 1555 2.83
LINK NA NA C1278 O THR C 250 1555 1555 2.79
LINK NA NA C1278 OD2 ASP C 256 1555 1555 3.02
LINK NA NA C1279 O MET C 177 1555 1555 2.81
LINK NA NA C1279 O TYR C 180 1555 1555 2.75
LINK NA NA C1280 O GLU C 112 1555 1555 2.65
LINK K K D1277 O PHE D 241 1555 1555 2.60
LINK K K D1277 O HIS D 238 1555 1555 3.48
LINK K K D1277 O ALA D 235 1555 1555 3.16
LINK NA NA D1278 O TYR D 180 1555 1555 2.72
LINK NA NA D1278 O MET D 177 1555 1555 2.51
LINK NA NA D1279 OD2 ASP D 256 1555 1555 2.93
LINK NA NA D1279 OD1 ASP D 256 1555 1555 2.75
LINK NA NA D1279 O THR D 250 1555 1555 2.91
LINK NA NA D1279 OG SER D 220 1555 1555 2.74
LINK NA NA D1300 O1 SRT A1287 1555 1555 3.07
LINK NA NA D1300 O2 SRT A1287 1555 1555 3.17
CISPEP 1 GLY A 27 PRO A 28 0 0.87
CISPEP 2 GLN A 221 PRO A 222 0 -10.93
CISPEP 3 GLY B 27 PRO B 28 0 1.97
CISPEP 4 GLN B 221 PRO B 222 0 -9.11
CISPEP 5 GLY C 27 PRO C 28 0 0.29
CISPEP 6 GLN C 221 PRO C 222 0 -7.41
CISPEP 7 GLY D 27 PRO D 28 0 1.16
CISPEP 8 GLN D 221 PRO D 222 0 -7.84
SITE 1 AC1 3 LEU A 174 GLU C 267 THR C 270
SITE 1 AC2 1 HOH A2042
SITE 1 AC3 5 SER A 232 TYR A 243 ASP D 158 VAL D 159
SITE 2 AC3 5 GOL D1276
SITE 1 AC4 5 SER B 101 HIS B 102 LEU B 128 PHE B 136
SITE 2 AC4 5 TRP B 160
SITE 1 AC5 2 ALA B 235 ASP C 162
SITE 1 AC6 6 HIS C 102 LEU C 128 PHE C 136 TRP C 160
SITE 2 AC6 6 GLN C 221 HIS C 251
SITE 1 AC7 5 ASP B 165 HOH B2039 LYS D 245 LEU D 246
SITE 2 AC7 5 GLY D 247
SITE 1 AC8 5 ARG A 260 VAL A 263 LYS D 167 ARG D 170
SITE 2 AC8 5 HIS D 171
SITE 1 AC9 8 ARG A 216 SER A 242 TYR A 243 GOL A1278
SITE 2 AC9 8 ASP D 158 LEU D 161 ASP D 162 GLY D 163
SITE 1 BC1 5 ASP A 158 ALA C 235 HIS C 238 PRO C 239
SITE 2 BC1 5 PHE C 241
SITE 1 BC2 4 ALA A 235 HIS A 238 PRO A 239 PHE A 241
SITE 1 BC3 4 ALA D 235 HIS D 238 PRO D 239 PHE D 241
SITE 1 BC4 5 ALA B 235 HIS B 238 PRO B 239 PHE B 241
SITE 2 BC4 5 HOH C2025
SITE 1 BC5 4 MET D 177 ALA D 178 TYR D 180 TRP D 185
SITE 1 BC6 5 SER D 220 GLY D 248 THR D 250 PRO D 253
SITE 2 BC6 5 ASP D 256
SITE 1 BC7 4 SER C 220 THR C 250 PRO C 253 ASP C 256
SITE 1 BC8 4 MET C 177 ALA C 178 TYR C 180 TRP C 185
SITE 1 BC9 1 HOH B2019
SITE 1 CC1 3 GLU C 112 GLY C 115 ARG C 213
SITE 1 CC2 4 LEU A 161 HIS A 164 ARG A 170 HIS C 264
SITE 1 CC3 2 GLY A 247 SRT A1287
SITE 1 CC4 2 GLY C 247 PRO C 249
SITE 1 CC5 2 GLY B 247 SRT B1284
SITE 1 CC6 4 GLY A 35 TRP A 36 SER A 101 HIS A 102
SITE 1 CC7 2 GLY B 35 TRP B 36
SITE 1 CC8 1 SER C 101
SITE 1 CC9 2 TRP D 36 SER D 101
SITE 1 DC1 2 PHE A 136 ILE A 192
SITE 1 DC2 2 TRP A 130 HOH A2011
SITE 1 DC3 2 ASP A 259 ARG A 260
SITE 1 DC4 2 ARG A 121 HOH A2018
SITE 1 DC5 5 LYS A 167 ARG A 170 HIS A 171 ARG C 260
SITE 2 DC5 5 VAL C 263
SITE 1 DC6 5 LYS B 167 ARG B 170 HIS B 171 ARG D 260
SITE 2 DC6 5 VAL D 263
SITE 1 DC7 4 ARG B 260 VAL B 263 ARG C 170 HOH C2050
SITE 1 DC8 6 HIS A 164 ASP A 165 HOH A2044 HOH A2045
SITE 2 DC8 6 HOH A2046 LYS C 245
SITE 1 DC9 6 LYS B 245 LEU B 246 NA B1281 HIS C 164
SITE 2 DC9 6 ASP C 165 GLU C 166
SITE 1 EC1 8 LYS A 245 LEU A 246 GLY A 247 HOH A2047
SITE 2 EC1 8 HIS D 164 ASP D 165 GLU D 166 NA D1300
CRYST1 45.770 167.000 166.940 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 0.021848 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005988 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005990 0.00000
MTRIX1 1 0.999780 0.014690 0.015140 -1.72376 1
MTRIX2 1 -0.014400 0.999720 -0.018850 70.07345 1
MTRIX3 1 -0.015420 0.018630 0.999710 -68.28546 1
MTRIX1 2 0.999820 -0.018990 0.001390 -9.89228 1
MTRIX2 2 -0.001020 0.019430 0.999810 24.85552 1
MTRIX3 2 -0.019010 -0.999630 0.019410 124.54890 1
MTRIX1 3 0.999980 -0.003690 0.004260 -11.77406 1
MTRIX2 3 -0.004230 0.006620 0.999970 -41.83904 1
MTRIX3 3 -0.003720 -0.999970 0.006610 56.37671 1
TER 2235 GLY A 275
TER 4484 GLY B 275
TER 6749 GLN C 274
TER 9016 GLN D 274
MASTER 655 0 39 49 32 0 51 15 9316 4 168 88
END |