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HEADER OXIDOREDUCTASE 19-NOV-13 4CFS
TITLE CRYSTAL STRUCTURE OF THE COFACTOR-DEVOID 1-H-3-HYDROXY-4-
TITLE 2 OXOQUINALDINE 2,4-DIOXYGENASE (HOD) CATALYTICALLY INACTIVE
TITLE 3 H251A VARIANT COMPLEXED WITH ITS NATURAL SUBSTRATE 1-H-3-
TITLE 4 HYDROXY-4-OXOQUINALDINE
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_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PQE30
KEYWDS ALPHA-BETA HYDROLASE COMPLEX, OXIDOREDUCTASE, DIOXYGENASE, COFACTOR-
KEYWDS 2 DEVOID
EXPDTA X-RAY DIFFRACTION
AUTHOR S.BUI,R.A.STEINER
REVDAT 1 04-DEC-13 4CFS 0
JRNL AUTH S.BUI,R.A.STEINER
JRNL TITL CRYSTAL STRUCTURE OF THE COFACTOR-DEVOID 1-H-3-HYDROXY-4-
JRNL TITL 2 OXOQUINALDINE 2,4-DIOXYGENASE (HOD) CATALYTICALLY INACTIVE
JRNL TITL 3 H251A VARIANT COMPLEXED WITH ITS NATURAL SUBSTRATE 1-H-3-
JRNL TITL 4 HYDROXY-4-OXOQUINALDINE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH R.A.STEINER,H.J.JANSSEN,P.ROVERSI,A.J.OAKLEY,S.FETZNER
REMARK 1 TITL STRUCTURAL BASIS FOR COFACTOR-INDEPENDENT DIOXYGENATION OF
REMARK 1 TITL 2 N-HETEROAROMATIC COMPOUNDS AT THE ALPHA/BETA-HYDROLASE
REMARK 1 TITL 3 FOLD.
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 107 657 2010
REMARK 1 REFN ISSN 0027-8424
REMARK 1 PMID 20080731
REMARK 1 DOI 10.1073/PNAS.0909033107
REMARK 2
REMARK 2 RESOLUTION. 1.94 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0049
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,
REMARK 3 STEINER,NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.94
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.45
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.46
REMARK 3 NUMBER OF REFLECTIONS : 88008
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : THIN SHELLS TAKING TWIN
REMARK 3 LAW INTO CONSIDERATION
REMARK 3 R VALUE (WORKING + TEST SET) : 0.16464
REMARK 3 R VALUE (WORKING SET) : 0.16287
REMARK 3 FREE R VALUE : 0.19841
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.1
REMARK 3 FREE R VALUE TEST SET COUNT : 4709
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.940
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.990
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5341
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 81.98
REMARK 3 BIN R VALUE (WORKING SET) : 0.201
REMARK 3 BIN FREE R VALUE SET COUNT : 238
REMARK 3 BIN FREE R VALUE : 0.237
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8998
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 136
REMARK 3 SOLVENT ATOMS : 638
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.648
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.945
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -6.94
REMARK 3 B22 (A**2) : 3.29
REMARK 3 B33 (A**2) : 3.65
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): 0.031
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.028
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.078
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.588
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.963
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.944
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9427 ; 0.008 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 8598 ; 0.004 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12860 ; 1.199 ; 1.948
REMARK 3 BOND ANGLES OTHERS (DEGREES): 19817 ; 0.917 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1127 ; 5.828 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 491 ;37.019 ;23.483
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1492 ;14.312 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 74 ;17.144 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1310 ; 0.074 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 11022 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 2292 ; 0.004 ; 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): 4406 ; 1.792 ; 2.884
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 4407 ; 1.791 ; 2.884
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5517 ; 2.666 ; 4.312
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 5021 ; 1.990 ; 3.062
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : 6
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 6
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 3 275 B 3 275 17453 0.05 0.05
REMARK 3 2 A 3 275 C 3 275 17541 0.05 0.05
REMARK 3 3 A 4 274 D 4 274 17434 0.05 0.05
REMARK 3 4 B 3 275 C 3 275 17575 0.04 0.05
REMARK 3 5 B 4 274 D 4 274 17440 0.05 0.05
REMARK 3 6 C 4 274 D 4 274 17492 0.05 0.05
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 : 0.511
REMARK 3 TWIN DOMAIN : 2
REMARK 3 TWIN OPERATOR : -H, L, K
REMARK 3 TWIN FRACTION : 0.489
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. TNCS IS PRESENT FRAC 0.000 0.407 0.407
REMARK 4
REMARK 4 4CFS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-NOV-13.
REMARK 100 THE PDBE ID CODE IS EBI-59019.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-AUG-10
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) : 0.97630
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 92811
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.95
REMARK 200 RESOLUTION RANGE LOW (A) : 46.45
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -1.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.73
REMARK 200 R MERGE (I) : 0.09
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.50
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.84
REMARK 200 R MERGE FOR SHELL (I) : 0.64
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.90
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 (%): 51.96
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.56
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 22.36500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 83.87000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 83.42500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 83.87000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 22.36500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 83.42500
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 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: PISA
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: PISA
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: PISA
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: PISA
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 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 -10
REMARK 465 ARG A -9
REMARK 465 GLY A -8
REMARK 465 SER A -7
REMARK 465 HIS A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 GLY A 0
REMARK 465 SER A 1
REMARK 465 MET A 2
REMARK 465 ASN A 276
REMARK 465 MET B -10
REMARK 465 ARG B -9
REMARK 465 GLY B -8
REMARK 465 SER B -7
REMARK 465 HIS B -6
REMARK 465 HIS B -5
REMARK 465 HIS B -4
REMARK 465 HIS B -3
REMARK 465 HIS B -2
REMARK 465 HIS B -1
REMARK 465 GLY B 0
REMARK 465 SER B 1
REMARK 465 MET B 2
REMARK 465 ASN B 276
REMARK 465 MET C -10
REMARK 465 ARG C -9
REMARK 465 GLY C -8
REMARK 465 SER C -7
REMARK 465 HIS C -6
REMARK 465 HIS C -5
REMARK 465 HIS C -4
REMARK 465 HIS C -3
REMARK 465 HIS C -2
REMARK 465 HIS C -1
REMARK 465 GLY C 0
REMARK 465 SER C 1
REMARK 465 MET C 2
REMARK 465 ASN C 276
REMARK 465 MET D -10
REMARK 465 ARG D -9
REMARK 465 GLY D -8
REMARK 465 SER D -7
REMARK 465 HIS D -6
REMARK 465 HIS D -5
REMARK 465 HIS D -4
REMARK 465 HIS D -3
REMARK 465 HIS D -2
REMARK 465 HIS D -1
REMARK 465 GLY D 0
REMARK 465 SER D 1
REMARK 465 MET D 2
REMARK 465 ASP D 3
REMARK 465 ASN 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 GLU A 8 O HOH A 2006 2.11
REMARK 500 OE1A GLN A 221 O HOH A 2100 1.67
REMARK 500 NH1 ARG B 273 O HOH B 2173 2.01
REMARK 500 O HOH A 2030 O HOH A 2083 2.03
REMARK 500 O HOH A 2043 O HOH A 2046 1.90
REMARK 500 O HOH A 2053 O HOH A 2126 2.04
REMARK 500 O HOH A 2103 O HOH A 2104 1.50
REMARK 500 O HOH A 2121 O HOH A 2123 2.07
REMARK 500 O HOH B 2035 O HOH B 2119 1.64
REMARK 500 O HOH B 2040 O HOH B 2136 2.11
REMARK 500 O HOH C 2055 O HOH A 2094 1.80
REMARK 500 O HOH C 2056 O HOH C 2059 1.89
REMARK 500 O HOH C 2059 O HOH C 2110 2.17
REMARK 500 O HOH C 2088 O HOH C 2122 1.96
REMARK 500 O HOH D 2030 O HOH D 2091 1.84
REMARK 500 O HOH D 2086 O HOH D 2088 1.58
REMARK 500 O HOH D 2088 O HOH D 2153 2.04
REMARK 500 O HOH D 2120 O HOH A 2143 2.00
REMARK 500 O HOH D 2173 O HOH D 2174 1.74
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OG1 THR A 4 OD1 ASN A 208 1655 2.16
REMARK 500 O HOH C 2076 O HOH B 2171 3654 1.83
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 260 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG A 260 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG B 260 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG B 260 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 ARG C 260 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG C 260 NE - CZ - NH2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 ARG D 260 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 PHE A 12 -108.14 55.93
REMARK 500 GLU A 93 -75.20 -92.43
REMARK 500 SER A 101 -124.22 46.53
REMARK 500 ASP A 126 70.66 35.81
REMARK 500 LEU A 128 107.62 -58.66
REMARK 500 PHE A 252 70.14 -119.38
REMARK 500 GLN A 274 49.15 -104.54
REMARK 500 PHE B 12 -107.63 55.86
REMARK 500 GLU B 93 -76.29 -92.20
REMARK 500 SER B 101 -125.07 46.62
REMARK 500 ASP B 126 71.47 35.21
REMARK 500 PHE B 252 70.30 -119.75
REMARK 500 GLN B 274 48.66 -103.97
REMARK 500 PHE C 12 -107.48 55.72
REMARK 500 GLU C 93 -74.90 -91.98
REMARK 500 SER C 101 -124.44 46.74
REMARK 500 ASP C 126 71.63 36.45
REMARK 500 LEU C 128 107.03 -59.49
REMARK 500 PHE C 252 70.12 -118.91
REMARK 500 GLN C 274 49.54 -104.09
REMARK 500 TYR D 5 -2.98 81.41
REMARK 500 PHE D 12 -107.26 56.59
REMARK 500 GLU D 93 -75.30 -91.26
REMARK 500 SER D 101 -125.84 46.10
REMARK 500 ASP D 126 72.77 35.95
REMARK 500 LEU D 128 105.94 -58.01
REMARK 500 PHE D 252 69.60 -118.87
REMARK 500 GLN D 274 53.03 -103.34
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 A1276 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA A 235 O
REMARK 620 2 HOH A2147 O 52.6
REMARK 620 3 HIS A 238 O 69.0 74.1
REMARK 620 4 PHE A 241 O 105.0 148.6 77.2
REMARK 620 5 HOH A2060 O 103.6 124.5 151.5 78.4
REMARK 620 6 HOH A2149 O 139.0 88.7 117.5 116.0 86.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K B1276 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PHE B 241 O
REMARK 620 2 HOH B2050 O 85.8
REMARK 620 3 HOH B2159 O 108.0 88.3
REMARK 620 4 HIS B 238 O 80.0 154.4 116.3
REMARK 620 5 ALA B 235 O 107.7 95.6 144.3 69.0
REMARK 620 6 HOH B2154 O 154.8 113.3 89.7 75.9 56.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K C1276 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA C 235 O
REMARK 620 2 HIS C 238 O 63.3
REMARK 620 3 HOH C2116 O 66.5 79.2
REMARK 620 4 HOH A2099 O 146.8 119.8 81.3
REMARK 620 5 PHE C 241 O 100.5 74.4 153.6 112.3
REMARK 620 6 HOH A2031 O 77.5 139.7 76.6 87.8 124.7
REMARK 620 7 HOH C2117 O 95.7 143.6 121.4 94.3 81.4 44.8
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K D1276 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH D2161 O
REMARK 620 2 HOH D2162 O 66.2
REMARK 620 3 HOH D2166 O 122.2 57.0
REMARK 620 4 ALA D 235 O 67.2 71.5 101.9
REMARK 620 5 HIS D 238 O 81.1 134.2 149.1 66.5
REMARK 620 6 PHE D 241 O 158.0 130.5 78.0 102.1 76.9
REMARK 620 7 HOH D2164 O 85.9 90.3 84.7 151.8 119.5 106.1
REMARK 620 8 PRO D 239 O 86.2 135.6 127.8 130.2 68.3 87.0 52.0
REMARK 620 N 1 2 3 4 5 6 7
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K D1276
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C1276
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B1276
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A1276
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HQD A1277
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HQD B1277
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HQD C1277
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HQD D1277
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TAR C1278
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TAR C1279
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TAR C1280
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TAR D1278
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TAR A1278
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TAR D1279
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TAR D1280
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 MRGSHHHHHHGS N-TERMINAL PURIFICATION TAG C69S, ENGINEERED
REMARK 999 MUTATION H251A, ENGINEERED MUTATION
DBREF 4CFS A 3 275 UNP O31266 HOD_ARTNT 3 275
DBREF 4CFS B 3 275 UNP O31266 HOD_ARTNT 3 275
DBREF 4CFS C 3 275 UNP O31266 HOD_ARTNT 3 275
DBREF 4CFS D 3 275 UNP O31266 HOD_ARTNT 3 275
SEQADV 4CFS MET A -10 UNP O31266 EXPRESSION TAG
SEQADV 4CFS ARG A -9 UNP O31266 EXPRESSION TAG
SEQADV 4CFS GLY A -8 UNP O31266 EXPRESSION TAG
SEQADV 4CFS SER A -7 UNP O31266 EXPRESSION TAG
SEQADV 4CFS HIS A -6 UNP O31266 EXPRESSION TAG
SEQADV 4CFS HIS A -5 UNP O31266 EXPRESSION TAG
SEQADV 4CFS HIS A -4 UNP O31266 EXPRESSION TAG
SEQADV 4CFS HIS A -3 UNP O31266 EXPRESSION TAG
SEQADV 4CFS HIS A -2 UNP O31266 EXPRESSION TAG
SEQADV 4CFS HIS A -1 UNP O31266 EXPRESSION TAG
SEQADV 4CFS GLY A 0 UNP O31266 EXPRESSION TAG
SEQADV 4CFS SER A 1 UNP O31266 EXPRESSION TAG
SEQADV 4CFS MET A 2 UNP O31266 EXPRESSION TAG
SEQADV 4CFS ASN A 276 UNP O31266 EXPRESSION TAG
SEQADV 4CFS SER A 69 UNP O31266 CYS 69 ENGINEERED MUTATION
SEQADV 4CFS ALA A 251 UNP O31266 HIS 251 ENGINEERED MUTATION
SEQADV 4CFS MET B -10 UNP O31266 EXPRESSION TAG
SEQADV 4CFS ARG B -9 UNP O31266 EXPRESSION TAG
SEQADV 4CFS GLY B -8 UNP O31266 EXPRESSION TAG
SEQADV 4CFS SER B -7 UNP O31266 EXPRESSION TAG
SEQADV 4CFS HIS B -6 UNP O31266 EXPRESSION TAG
SEQADV 4CFS HIS B -5 UNP O31266 EXPRESSION TAG
SEQADV 4CFS HIS B -4 UNP O31266 EXPRESSION TAG
SEQADV 4CFS HIS B -3 UNP O31266 EXPRESSION TAG
SEQADV 4CFS HIS B -2 UNP O31266 EXPRESSION TAG
SEQADV 4CFS HIS B -1 UNP O31266 EXPRESSION TAG
SEQADV 4CFS GLY B 0 UNP O31266 EXPRESSION TAG
SEQADV 4CFS SER B 1 UNP O31266 EXPRESSION TAG
SEQADV 4CFS MET B 2 UNP O31266 EXPRESSION TAG
SEQADV 4CFS ASN B 276 UNP O31266 EXPRESSION TAG
SEQADV 4CFS SER B 69 UNP O31266 CYS 69 ENGINEERED MUTATION
SEQADV 4CFS ALA B 251 UNP O31266 HIS 251 ENGINEERED MUTATION
SEQADV 4CFS MET C -10 UNP O31266 EXPRESSION TAG
SEQADV 4CFS ARG C -9 UNP O31266 EXPRESSION TAG
SEQADV 4CFS GLY C -8 UNP O31266 EXPRESSION TAG
SEQADV 4CFS SER C -7 UNP O31266 EXPRESSION TAG
SEQADV 4CFS HIS C -6 UNP O31266 EXPRESSION TAG
SEQADV 4CFS HIS C -5 UNP O31266 EXPRESSION TAG
SEQADV 4CFS HIS C -4 UNP O31266 EXPRESSION TAG
SEQADV 4CFS HIS C -3 UNP O31266 EXPRESSION TAG
SEQADV 4CFS HIS C -2 UNP O31266 EXPRESSION TAG
SEQADV 4CFS HIS C -1 UNP O31266 EXPRESSION TAG
SEQADV 4CFS GLY C 0 UNP O31266 EXPRESSION TAG
SEQADV 4CFS SER C 1 UNP O31266 EXPRESSION TAG
SEQADV 4CFS MET C 2 UNP O31266 EXPRESSION TAG
SEQADV 4CFS ASN C 276 UNP O31266 EXPRESSION TAG
SEQADV 4CFS SER C 69 UNP O31266 CYS 69 ENGINEERED MUTATION
SEQADV 4CFS ALA C 251 UNP O31266 HIS 251 ENGINEERED MUTATION
SEQADV 4CFS MET D -10 UNP O31266 EXPRESSION TAG
SEQADV 4CFS ARG D -9 UNP O31266 EXPRESSION TAG
SEQADV 4CFS GLY D -8 UNP O31266 EXPRESSION TAG
SEQADV 4CFS SER D -7 UNP O31266 EXPRESSION TAG
SEQADV 4CFS HIS D -6 UNP O31266 EXPRESSION TAG
SEQADV 4CFS HIS D -5 UNP O31266 EXPRESSION TAG
SEQADV 4CFS HIS D -4 UNP O31266 EXPRESSION TAG
SEQADV 4CFS HIS D -3 UNP O31266 EXPRESSION TAG
SEQADV 4CFS HIS D -2 UNP O31266 EXPRESSION TAG
SEQADV 4CFS HIS D -1 UNP O31266 EXPRESSION TAG
SEQADV 4CFS GLY D 0 UNP O31266 EXPRESSION TAG
SEQADV 4CFS SER D 1 UNP O31266 EXPRESSION TAG
SEQADV 4CFS MET D 2 UNP O31266 EXPRESSION TAG
SEQADV 4CFS ASN D 276 UNP O31266 EXPRESSION TAG
SEQADV 4CFS SER D 69 UNP O31266 CYS 69 ENGINEERED MUTATION
SEQADV 4CFS ALA D 251 UNP O31266 HIS 251 ENGINEERED MUTATION
SEQRES 1 A 287 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER MET
SEQRES 2 A 287 ASP THR TYR LEU HIS GLU THR LEU VAL PHE ASP ASN LYS
SEQRES 3 A 287 LEU SER TYR ILE ASP ASN GLN ARG ASP THR ASP GLY PRO
SEQRES 4 A 287 ALA ILE LEU LEU LEU PRO GLY TRP CYS HIS ASP HIS ARG
SEQRES 5 A 287 VAL TYR LYS TYR LEU ILE GLN GLU LEU ASP ALA ASP PHE
SEQRES 6 A 287 ARG VAL ILE VAL PRO ASN TRP ARG GLY HIS GLY LEU SER
SEQRES 7 A 287 PRO SER GLU VAL PRO ASP PHE GLY TYR GLN GLU GLN VAL
SEQRES 8 A 287 LYS ASP ALA LEU GLU ILE LEU ASP GLN LEU GLY VAL GLU
SEQRES 9 A 287 THR PHE LEU PRO VAL SER HIS SER HIS GLY GLY TRP VAL
SEQRES 10 A 287 LEU VAL GLU LEU LEU GLU GLN ALA GLY PRO GLU ARG ALA
SEQRES 11 A 287 PRO ARG GLY ILE ILE MET ASP TRP LEU MET TRP ALA PRO
SEQRES 12 A 287 LYS PRO ASP PHE ALA LYS SER LEU THR LEU LEU LYS ASP
SEQRES 13 A 287 PRO GLU ARG TRP ARG GLU GLY THR HIS GLY LEU PHE ASP
SEQRES 14 A 287 VAL TRP LEU ASP GLY HIS ASP GLU LYS ARG VAL ARG HIS
SEQRES 15 A 287 HIS LEU LEU GLU GLU MET ALA ASP TYR GLY TYR ASP CYS
SEQRES 16 A 287 TRP GLY ARG SER GLY ARG VAL ILE GLU ASP ALA TYR GLY
SEQRES 17 A 287 ARG ASN GLY SER PRO MET GLN MET MET ALA ASN LEU THR
SEQRES 18 A 287 LYS THR ARG PRO ILE ARG HIS ILE PHE SER GLN PRO THR
SEQRES 19 A 287 GLU PRO GLU TYR GLU LYS ILE ASN SER ASP PHE ALA GLU
SEQRES 20 A 287 GLN HIS PRO TRP PHE SER TYR ALA LYS LEU GLY GLY PRO
SEQRES 21 A 287 THR ALA PHE PRO ALA ILE ASP VAL PRO ASP ARG ALA ALA
SEQRES 22 A 287 VAL HIS ILE ARG GLU PHE ALA THR ALA ILE ARG GLN GLY
SEQRES 23 A 287 ASN
SEQRES 1 B 287 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER MET
SEQRES 2 B 287 ASP THR TYR LEU HIS GLU THR LEU VAL PHE ASP ASN LYS
SEQRES 3 B 287 LEU SER TYR ILE ASP ASN GLN ARG ASP THR ASP GLY PRO
SEQRES 4 B 287 ALA ILE LEU LEU LEU PRO GLY TRP CYS HIS ASP HIS ARG
SEQRES 5 B 287 VAL TYR LYS TYR LEU ILE GLN GLU LEU ASP ALA ASP PHE
SEQRES 6 B 287 ARG VAL ILE VAL PRO ASN TRP ARG GLY HIS GLY LEU SER
SEQRES 7 B 287 PRO SER GLU VAL PRO ASP PHE GLY TYR GLN GLU GLN VAL
SEQRES 8 B 287 LYS ASP ALA LEU GLU ILE LEU ASP GLN LEU GLY VAL GLU
SEQRES 9 B 287 THR PHE LEU PRO VAL SER HIS SER HIS GLY GLY TRP VAL
SEQRES 10 B 287 LEU VAL GLU LEU LEU GLU GLN ALA GLY PRO GLU ARG ALA
SEQRES 11 B 287 PRO ARG GLY ILE ILE MET ASP TRP LEU MET TRP ALA PRO
SEQRES 12 B 287 LYS PRO ASP PHE ALA LYS SER LEU THR LEU LEU LYS ASP
SEQRES 13 B 287 PRO GLU ARG TRP ARG GLU GLY THR HIS GLY LEU PHE ASP
SEQRES 14 B 287 VAL TRP LEU ASP GLY HIS ASP GLU LYS ARG VAL ARG HIS
SEQRES 15 B 287 HIS LEU LEU GLU GLU MET ALA ASP TYR GLY TYR ASP CYS
SEQRES 16 B 287 TRP GLY ARG SER GLY ARG VAL ILE GLU ASP ALA TYR GLY
SEQRES 17 B 287 ARG ASN GLY SER PRO MET GLN MET MET ALA ASN LEU THR
SEQRES 18 B 287 LYS THR ARG PRO ILE ARG HIS ILE PHE SER GLN PRO THR
SEQRES 19 B 287 GLU PRO GLU TYR GLU LYS ILE ASN SER ASP PHE ALA GLU
SEQRES 20 B 287 GLN HIS PRO TRP PHE SER TYR ALA LYS LEU GLY GLY PRO
SEQRES 21 B 287 THR ALA PHE PRO ALA ILE ASP VAL PRO ASP ARG ALA ALA
SEQRES 22 B 287 VAL HIS ILE ARG GLU PHE ALA THR ALA ILE ARG GLN GLY
SEQRES 23 B 287 ASN
SEQRES 1 C 287 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER MET
SEQRES 2 C 287 ASP THR TYR LEU HIS GLU THR LEU VAL PHE ASP ASN LYS
SEQRES 3 C 287 LEU SER TYR ILE ASP ASN GLN ARG ASP THR ASP GLY PRO
SEQRES 4 C 287 ALA ILE LEU LEU LEU PRO GLY TRP CYS HIS ASP HIS ARG
SEQRES 5 C 287 VAL TYR LYS TYR LEU ILE GLN GLU LEU ASP ALA ASP PHE
SEQRES 6 C 287 ARG VAL ILE VAL PRO ASN TRP ARG GLY HIS GLY LEU SER
SEQRES 7 C 287 PRO SER GLU VAL PRO ASP PHE GLY TYR GLN GLU GLN VAL
SEQRES 8 C 287 LYS ASP ALA LEU GLU ILE LEU ASP GLN LEU GLY VAL GLU
SEQRES 9 C 287 THR PHE LEU PRO VAL SER HIS SER HIS GLY GLY TRP VAL
SEQRES 10 C 287 LEU VAL GLU LEU LEU GLU GLN ALA GLY PRO GLU ARG ALA
SEQRES 11 C 287 PRO ARG GLY ILE ILE MET ASP TRP LEU MET TRP ALA PRO
SEQRES 12 C 287 LYS PRO ASP PHE ALA LYS SER LEU THR LEU LEU LYS ASP
SEQRES 13 C 287 PRO GLU ARG TRP ARG GLU GLY THR HIS GLY LEU PHE ASP
SEQRES 14 C 287 VAL TRP LEU ASP GLY HIS ASP GLU LYS ARG VAL ARG HIS
SEQRES 15 C 287 HIS LEU LEU GLU GLU MET ALA ASP TYR GLY TYR ASP CYS
SEQRES 16 C 287 TRP GLY ARG SER GLY ARG VAL ILE GLU ASP ALA TYR GLY
SEQRES 17 C 287 ARG ASN GLY SER PRO MET GLN MET MET ALA ASN LEU THR
SEQRES 18 C 287 LYS THR ARG PRO ILE ARG HIS ILE PHE SER GLN PRO THR
SEQRES 19 C 287 GLU PRO GLU TYR GLU LYS ILE ASN SER ASP PHE ALA GLU
SEQRES 20 C 287 GLN HIS PRO TRP PHE SER TYR ALA LYS LEU GLY GLY PRO
SEQRES 21 C 287 THR ALA PHE PRO ALA ILE ASP VAL PRO ASP ARG ALA ALA
SEQRES 22 C 287 VAL HIS ILE ARG GLU PHE ALA THR ALA ILE ARG GLN GLY
SEQRES 23 C 287 ASN
SEQRES 1 D 287 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER MET
SEQRES 2 D 287 ASP THR TYR LEU HIS GLU THR LEU VAL PHE ASP ASN LYS
SEQRES 3 D 287 LEU SER TYR ILE ASP ASN GLN ARG ASP THR ASP GLY PRO
SEQRES 4 D 287 ALA ILE LEU LEU LEU PRO GLY TRP CYS HIS ASP HIS ARG
SEQRES 5 D 287 VAL TYR LYS TYR LEU ILE GLN GLU LEU ASP ALA ASP PHE
SEQRES 6 D 287 ARG VAL ILE VAL PRO ASN TRP ARG GLY HIS GLY LEU SER
SEQRES 7 D 287 PRO SER GLU VAL PRO ASP PHE GLY TYR GLN GLU GLN VAL
SEQRES 8 D 287 LYS ASP ALA LEU GLU ILE LEU ASP GLN LEU GLY VAL GLU
SEQRES 9 D 287 THR PHE LEU PRO VAL SER HIS SER HIS GLY GLY TRP VAL
SEQRES 10 D 287 LEU VAL GLU LEU LEU GLU GLN ALA GLY PRO GLU ARG ALA
SEQRES 11 D 287 PRO ARG GLY ILE ILE MET ASP TRP LEU MET TRP ALA PRO
SEQRES 12 D 287 LYS PRO ASP PHE ALA LYS SER LEU THR LEU LEU LYS ASP
SEQRES 13 D 287 PRO GLU ARG TRP ARG GLU GLY THR HIS GLY LEU PHE ASP
SEQRES 14 D 287 VAL TRP LEU ASP GLY HIS ASP GLU LYS ARG VAL ARG HIS
SEQRES 15 D 287 HIS LEU LEU GLU GLU MET ALA ASP TYR GLY TYR ASP CYS
SEQRES 16 D 287 TRP GLY ARG SER GLY ARG VAL ILE GLU ASP ALA TYR GLY
SEQRES 17 D 287 ARG ASN GLY SER PRO MET GLN MET MET ALA ASN LEU THR
SEQRES 18 D 287 LYS THR ARG PRO ILE ARG HIS ILE PHE SER GLN PRO THR
SEQRES 19 D 287 GLU PRO GLU TYR GLU LYS ILE ASN SER ASP PHE ALA GLU
SEQRES 20 D 287 GLN HIS PRO TRP PHE SER TYR ALA LYS LEU GLY GLY PRO
SEQRES 21 D 287 THR ALA PHE PRO ALA ILE ASP VAL PRO ASP ARG ALA ALA
SEQRES 22 D 287 VAL HIS ILE ARG GLU PHE ALA THR ALA ILE ARG GLN GLY
SEQRES 23 D 287 ASN
HET K D1276 1
HET K C1276 1
HET K B1276 1
HET K A1276 1
HET HQD A1277 13
HET HQD B1277 13
HET HQD C1277 13
HET HQD D1277 13
HET TAR C1278 10
HET TAR C1279 20
HET TAR C1280 10
HET TAR D1278 10
HET TAR A1278 10
HET TAR D1279 10
HET TAR D1280 10
HETNAM K POTASSIUM ION
HETNAM HQD 3-HYDROXY-2-METHYLQUINOLIN-4(1H)-ONE
HETNAM TAR D(-)-TARTARIC ACID
FORMUL 2 HQD 4(C10 H9 N O2)
FORMUL 3 TAR 7(C4 H6 O6)
FORMUL 4 K 4(K 1+)
FORMUL 5 HOH *638(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 GLY A 91 1 17
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 GLN A 274 1 18
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 GLY B 91 1 17
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 GLN B 274 1 18
HELIX 25 25 ASP C 39 VAL C 42 5 4
HELIX 26 26 TYR C 43 ASP C 51 1 9
HELIX 27 27 GLY C 75 GLY C 91 1 17
HELIX 28 28 GLY C 103 ALA C 119 1 17
HELIX 29 29 LYS C 133 ASP C 145 1 13
HELIX 30 30 ARG C 148 ASP C 162 1 15
HELIX 31 31 GLU C 166 GLU C 175 1 10
HELIX 32 32 GLY C 181 GLY C 200 1 20
HELIX 33 33 SER C 201 ASN C 208 1 8
HELIX 34 34 GLU C 224 HIS C 238 1 15
HELIX 35 35 PHE C 252 VAL C 257 1 6
HELIX 36 36 VAL C 257 GLN C 274 1 18
HELIX 37 37 ASP D 39 VAL D 42 5 4
HELIX 38 38 TYR D 43 ASP D 51 1 9
HELIX 39 39 GLY D 75 GLY D 91 1 17
HELIX 40 40 GLY D 103 ALA D 119 1 17
HELIX 41 41 LYS D 133 ASP D 145 1 13
HELIX 42 42 ARG D 148 ASP D 162 1 15
HELIX 43 43 GLU D 166 GLU D 175 1 10
HELIX 44 44 GLY D 181 GLY D 200 1 20
HELIX 45 45 SER D 201 ASN D 208 1 8
HELIX 46 46 GLU D 224 HIS D 238 1 15
HELIX 47 47 PHE D 252 VAL D 257 1 6
HELIX 48 48 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 2.05
SSBOND 2 CYS B 37 CYS B 184 1555 1555 2.05
SSBOND 3 CYS C 37 CYS C 184 1555 1555 2.07
SSBOND 4 CYS D 37 CYS D 184 1555 1555 2.05
LINK K K A1276 O ALA A 235 1555 1555 2.63
LINK K K A1276 O HOH A2147 1555 1555 3.00
LINK K K A1276 O HIS A 238 1555 1555 2.97
LINK K K A1276 O PHE A 241 1555 1555 2.63
LINK K K A1276 O HOH A2060 1555 1555 3.36
LINK K K A1276 O HOH A2149 1555 1555 2.65
LINK K K B1276 O PHE B 241 1555 1555 2.48
LINK K K B1276 O HOH B2050 1555 1555 3.05
LINK K K B1276 O HOH B2159 1555 1555 2.60
LINK K K B1276 O HIS B 238 1555 1555 2.91
LINK K K B1276 O ALA B 235 1555 1555 2.70
LINK K K B1276 O HOH B2154 1555 1555 3.26
LINK K K C1276 O HOH A2099 1555 1555 2.29
LINK K K C1276 O HIS C 238 1555 1555 3.18
LINK K K C1276 O HOH C2116 1555 1555 2.75
LINK K K C1276 O PHE C 241 1555 1555 2.55
LINK K K C1276 O HOH A2031 1555 1555 3.28
LINK K K C1276 O HOH C2117 1555 1555 2.94
LINK K K C1276 O ALA C 235 1555 1555 2.85
LINK K K D1276 O HOH D2162 1555 1555 3.22
LINK K K D1276 O HOH D2166 1555 1555 2.81
LINK K K D1276 O ALA D 235 1555 1555 2.78
LINK K K D1276 O HIS D 238 1555 1555 3.01
LINK K K D1276 O PHE D 241 1555 1555 2.56
LINK K K D1276 O HOH D2164 1555 1555 2.50
LINK K K D1276 O PRO D 239 1555 1555 3.46
LINK K K D1276 O HOH D2161 1555 1555 2.87
CISPEP 1 GLY A 27 PRO A 28 0 1.95
CISPEP 2 GLN A 221 PRO A 222 0 -4.28
CISPEP 3 GLY B 27 PRO B 28 0 3.61
CISPEP 4 GLN B 221 PRO B 222 0 -4.17
CISPEP 5 GLY C 27 PRO C 28 0 3.47
CISPEP 6 GLN C 221 PRO C 222 0 -3.20
CISPEP 7 GLY D 27 PRO D 28 0 3.23
CISPEP 8 GLN D 221 PRO D 222 0 -5.25
SITE 1 AC1 7 ALA D 235 HIS D 238 PRO D 239 PHE D 241
SITE 2 AC1 7 HOH D2161 HOH D2164 HOH D2166
SITE 1 AC2 7 HOH A2099 ALA C 235 HIS C 238 PRO C 239
SITE 2 AC2 7 PHE C 241 HOH C2116 HOH C2117
SITE 1 AC3 6 ALA B 235 HIS B 238 PRO B 239 PHE B 241
SITE 2 AC3 6 HOH B2050 HOH B2159
SITE 1 AC4 6 ALA A 235 HIS A 238 PRO A 239 PHE A 241
SITE 2 AC4 6 HOH A2147 HOH A2149
SITE 1 AC5 12 TRP A 36 HIS A 38 HIS A 100 SER A 101
SITE 2 AC5 12 HIS A 102 TRP A 160 MET A 177 TRP A 185
SITE 3 AC5 12 SER A 188 ILE A 192 HOH A2069 HOH A2072
SITE 1 AC6 11 TRP B 36 HIS B 38 HIS B 100 SER B 101
SITE 2 AC6 11 HIS B 102 LEU B 143 TRP B 160 TRP B 185
SITE 3 AC6 11 SER B 188 HOH B2058 HOH B2060
SITE 1 AC7 12 TRP C 36 HIS C 38 HIS C 100 SER C 101
SITE 2 AC7 12 HIS C 102 TRP C 160 MET C 177 TRP C 185
SITE 3 AC7 12 SER C 188 ILE C 192 HOH C2048 HOH C2050
SITE 1 AC8 13 TRP D 36 HIS D 38 HIS D 100 SER D 101
SITE 2 AC8 13 HIS D 102 LEU D 143 TRP D 160 MET D 177
SITE 3 AC8 13 TRP D 185 SER D 188 ILE D 192 HOH D2072
SITE 4 AC8 13 HOH D2073
SITE 1 AC9 5 ARG B 260 VAL B 263 LYS C 167 ARG C 170
SITE 2 AC9 5 HIS C 171
SITE 1 BC1 8 LYS B 245 LEU B 246 GLY B 247 HOH B2163
SITE 2 BC1 8 ASP C 165 HOH C2087 HOH C2089 HOH C2125
SITE 1 BC2 7 HIS A 164 ASP A 165 HOH A2108 HOH A2110
SITE 2 BC2 7 LYS C 245 LEU C 246 GLY C 247
SITE 1 BC3 5 ARG A 260 VAL A 263 LYS D 167 ARG D 170
SITE 2 BC3 5 HOH D2126
SITE 1 BC4 5 LYS A 167 ARG A 170 HIS A 171 ARG C 260
SITE 2 BC4 5 VAL C 263
SITE 1 BC5 9 LYS A 245 LEU A 246 GLY A 247 HIS D 164
SITE 2 BC5 9 ASP D 165 HOH D2120 HOH D2121 HOH D2123
SITE 3 BC5 9 HOH D2174
SITE 1 BC6 9 HIS B 164 ASP B 165 HOH B2109 HOH B2110
SITE 2 BC6 9 HOH B2111 LYS D 245 LEU D 246 GLY D 247
SITE 3 BC6 9 HOH D2176
CRYST1 44.730 166.850 167.740 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 0.022356 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005993 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005962 0.00000
TER 2241 GLY A 275
TER 4504 GLY B 275
TER 6749 GLY C 275
TER 9002 GLY D 275
MASTER 587 0 15 48 32 0 37 6 9772 4 168 92
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