HEADER HYDROLASE 16-APR-14 4CZ1
TITLE CRYSTAL STRUCTURE OF KYNURENINE FORMAMIDASE FROM BACILLUS ANTHRACIS
TITLE 2 COMPLEXED WITH 2-AMINOACETOPHENONE.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: KYNURENINE FORMAMIDASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: KFA, KFASE, ARYLFORMAMIDASE, N-FORMYLKYNURENINE FORMAMIDASE,
COMPND 5 FKF;
COMPND 6 EC: 3.5.1.9;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS ANTHRACIS STR. AMES;
SOURCE 3 ORGANISM_TAXID: 198094;
SOURCE 4 GENE: KYNB;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS HYDROLASE, TRYPTOPHAN DEGRADATION PATHWAY VIA ANTHRANILATE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.DIAZ-SAEZ,V.SRIKANNATHASAN,M.ZOLTNER,W.N.HUNTER
REVDAT 5 20-DEC-23 4CZ1 1 REMARK LINK
REVDAT 4 06-MAR-19 4CZ1 1 REMARK
REVDAT 3 03-SEP-14 4CZ1 1 JRNL
REVDAT 2 02-JUL-14 4CZ1 1 JRNL REMARK HETATM CONECT
REVDAT 2 2 1 MASTER
REVDAT 1 30-APR-14 4CZ1 0
SPRSDE 30-APR-14 4CZ1 4COA
JRNL AUTH L.DIAZ-SAEZ,V.SRIKANNATHASAN,M.ZOLTNER,W.N.HUNTER
JRNL TITL STRUCTURE OF BACTERIAL KYNURENINE FORMAMIDASE REVEALS A
JRNL TITL 2 CROWDED BINUCLEAR-ZINC CATALYTIC SITE PRIMED TO GENERATE A
JRNL TITL 3 POTENT NUCLEOPHILE.
JRNL REF BIOCHEM.J. V. 462 581 2014
JRNL REFN ISSN 0264-6021
JRNL PMID 24942958
JRNL DOI 10.1042/BJ20140511
REMARK 2
REMARK 2 RESOLUTION. 2.24 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0049
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : 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) : 2.24
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.64
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.7
REMARK 3 NUMBER OF REFLECTIONS : 36106
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) : 0.186
REMARK 3 R VALUE (WORKING SET) : 0.184
REMARK 3 FREE R VALUE : 0.224
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1916
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) : 2.24
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.30
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2226
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 82.57
REMARK 3 BIN R VALUE (WORKING SET) : 0.2200
REMARK 3 BIN FREE R VALUE SET COUNT : 147
REMARK 3 BIN FREE R VALUE : 0.2870
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6467
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 21
REMARK 3 SOLVENT ATOMS : 412
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.69
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 7.17000
REMARK 3 B22 (A**2) : 5.74000
REMARK 3 B33 (A**2) : -12.91000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 6.27000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.082
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.048
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.110
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.232
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.927
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.898
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6677 ; 0.017 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 6443 ; 0.009 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9098 ; 1.684 ; 1.969
REMARK 3 BOND ANGLES OTHERS (DEGREES): 14909 ; 1.343 ; 3.001
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 821 ; 6.727 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 300 ;35.668 ;24.933
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1134 ;14.365 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 28 ;12.657 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1049 ; 0.100 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7431 ; 0.012 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1405 ; 0.008 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1618 ; 0.238 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 6205 ; 0.197 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3221 ; 0.176 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 3373 ; 0.088 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 163 ; 0.163 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): 6 ; 0.132 ; 0.200
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 1 ; 0.205 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 45 ; 0.312 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 73 ; 0.198 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 2 ; 0.509 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): 1 ; 0.145 ; 0.200
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): 3296 ; 2.008 ; 1.914
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3295 ; 2.006 ; 1.914
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4113 ; 3.090 ; 2.863
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3381 ; 2.495 ; 2.189
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 4985 ; 3.963 ; 3.164
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER 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 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 4 208 B 4 208 12607 0.07 0.05
REMARK 3 2 A 4 208 C 4 208 12801 0.05 0.05
REMARK 3 3 A 4 208 D 4 208 12447 0.09 0.05
REMARK 3 4 B 4 209 C 4 209 12757 0.07 0.05
REMARK 3 5 B 4 209 D 4 209 12810 0.06 0.05
REMARK 3 6 C 4 209 D 4 209 12562 0.09 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 : 0.842
REMARK 3 TWIN DOMAIN : 2
REMARK 3 TWIN OPERATOR : -H,-K,L
REMARK 3 TWIN FRACTION : 0.158
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS.
REMARK 4
REMARK 4 4CZ1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-APR-14.
REMARK 100 THE DEPOSITION ID IS D_1290060359.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-SEP-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I03
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9791
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38046
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.250
REMARK 200 RESOLUTION RANGE LOW (A) : 42.640
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 200 DATA REDUNDANCY : 2.700
REMARK 200 R MERGE (I) : 0.16000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 4.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.32
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.7
REMARK 200 DATA REDUNDANCY IN SHELL : 2.70
REMARK 200 R MERGE FOR SHELL (I) : 0.55000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 4CO9
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.88
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS-HCL PH 8.5, 140 MM MGCL2
REMARK 280 AND 30 % (W/V) PEG 4000. 293 K. PROTEIN WAS PREVIOUSLY INCUBATED
REMARK 280 WITH 5 % (V/V) 2-AMINOACETOPHENONE.
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 33.28050
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5850 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16470 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -195.7 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5360 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16560 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -191.1 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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 1
REMARK 465 LYS A 2
REMARK 465 MET B 1
REMARK 465 LYS B 2
REMARK 465 THR B 3
REMARK 465 MET C 1
REMARK 465 LYS C 2
REMARK 465 THR C 3
REMARK 465 MET D 1
REMARK 465 LYS D 2
REMARK 465 THR D 3
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 O HOH D 2002 O HOH D 2005 2.09
REMARK 500 OD2 ASP A 130 O HOH A 2078 2.14
REMARK 500 O GLU D 102 O HOH D 2052 2.15
REMARK 500 OE2 GLU A 105 O HOH A 2083 2.15
REMARK 500 OD1 ASP C 72 O HOH C 2068 2.17
REMARK 500 O LYS D 138 O HOH D 2063 2.18
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 O HOH B 2034 O HOH D 2024 2656 2.04
REMARK 500 ND2 ASN B 87 O LYS C 166 1665 2.19
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 TRP B 20 CB TRP B 20 CG -0.109
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 SER A 4 69.83 65.16
REMARK 500 SER A 39 -44.26 -152.62
REMARK 500 HIS A 50 51.14 -94.65
REMARK 500 HIS A 114 -83.48 -135.91
REMARK 500 ASP A 146 30.47 -91.20
REMARK 500 ALA A 189 70.10 -155.67
REMARK 500 SER B 39 -43.44 -153.71
REMARK 500 HIS B 50 46.08 -92.51
REMARK 500 HIS B 114 -85.61 -135.31
REMARK 500 ALA B 189 69.37 -159.22
REMARK 500 SER C 39 -44.59 -152.13
REMARK 500 HIS C 50 55.82 -97.46
REMARK 500 HIS C 114 -82.94 -134.63
REMARK 500 ASP C 146 33.39 -90.78
REMARK 500 ALA C 189 70.05 -158.51
REMARK 500 SER D 39 -44.99 -154.92
REMARK 500 HIS D 50 49.90 -91.51
REMARK 500 HIS D 114 -84.63 -135.68
REMARK 500 ASP D 146 33.64 -94.19
REMARK 500 ALA D 189 67.29 -158.07
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A2045 DISTANCE = 7.08 ANGSTROMS
REMARK 525 HOH A2133 DISTANCE = 6.58 ANGSTROMS
REMARK 525 HOH B2066 DISTANCE = 6.14 ANGSTROMS
REMARK 525 HOH B2067 DISTANCE = 6.27 ANGSTROMS
REMARK 525 HOH B2068 DISTANCE = 7.60 ANGSTROMS
REMARK 525 HOH B2069 DISTANCE = 7.50 ANGSTROMS
REMARK 525 HOH C2015 DISTANCE = 5.92 ANGSTROMS
REMARK 525 HOH C2116 DISTANCE = 8.26 ANGSTROMS
REMARK 525 HOH C2117 DISTANCE = 9.70 ANGSTROMS
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 ZINC ION (ZN): ZN2+ BINDING ACTIVE SITE RESIDUES
REMARK 600 2-AMINOACETOPHENONE (2AT): PLACE AT THE ACTIVE SITE
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 ZN A 402 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 50 ND1
REMARK 620 2 HIS A 54 NE2 95.0
REMARK 620 3 ASP A 56 OD1 100.0 106.8
REMARK 620 4 GLU A 173 OE1 171.2 77.4 86.5
REMARK 620 5 HOH A2027 O 105.1 75.5 154.6 69.0
REMARK 620 6 HOH A2046 O 95.3 143.6 105.6 88.4 68.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 56 OD2
REMARK 620 2 HIS A 161 NE2 88.5
REMARK 620 3 GLU A 173 OE2 107.0 101.2
REMARK 620 4 GLU A 173 OE1 95.0 154.5 53.7
REMARK 620 5 HOH A2046 O 107.8 113.6 130.7 89.3
REMARK 620 6 HOH A2103 O 167.0 78.6 75.2 96.4 78.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1210 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 64 OD1
REMARK 620 2 HOH A2054 O 89.3
REMARK 620 3 HOH A2055 O 85.8 172.9
REMARK 620 4 HOH A2132 O 104.4 75.1 111.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 402 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 50 ND1
REMARK 620 2 HIS B 54 NE2 95.2
REMARK 620 3 ASP B 56 OD1 87.5 105.3
REMARK 620 4 GLU B 173 OE1 176.8 83.4 90.1
REMARK 620 5 HOH B2016 O 108.1 80.3 163.1 74.5
REMARK 620 6 HOH B2022 O 85.3 167.4 87.3 96.7 87.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 56 OD2
REMARK 620 2 HIS B 161 NE2 87.2
REMARK 620 3 GLU B 173 OE1 95.9 161.5
REMARK 620 4 GLU B 173 OE2 111.0 107.1 54.8
REMARK 620 5 HOH B2022 O 87.0 108.3 90.0 140.8
REMARK 620 6 HOH B2053 O 164.5 101.9 79.4 78.5 78.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C1210 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY C 38 O
REMARK 620 2 HOH C2049 O 97.8
REMARK 620 3 HOH C2050 O 83.3 119.7
REMARK 620 4 HOH C2051 O 73.1 161.0 76.6
REMARK 620 5 HOH C2052 O 87.4 87.6 152.1 75.5
REMARK 620 6 HOH C2115 O 153.9 107.8 79.8 83.7 98.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 402 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 50 ND1
REMARK 620 2 HIS C 54 NE2 97.4
REMARK 620 3 ASP C 56 OD1 95.2 108.9
REMARK 620 4 GLU C 173 OE1 176.2 79.6 87.9
REMARK 620 5 HOH C2024 O 111.3 75.2 152.6 65.8
REMARK 620 6 HOH C2055 O 93.0 147.4 100.8 88.4 72.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 56 OD2
REMARK 620 2 HIS C 161 NE2 85.5
REMARK 620 3 GLU C 173 OE2 109.6 103.9
REMARK 620 4 GLU C 173 OE1 96.9 161.1 57.5
REMARK 620 5 HOH C2055 O 97.7 119.1 130.4 79.2
REMARK 620 6 HOH C2092 O 161.7 101.0 85.6 82.4 64.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 402 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 50 ND1
REMARK 620 2 HIS D 54 NE2 93.5
REMARK 620 3 ASP D 56 OD1 90.8 102.0
REMARK 620 4 GLU D 173 OE1 172.7 79.3 90.8
REMARK 620 5 HOH D2022 O 107.6 74.9 161.3 70.5
REMARK 620 6 HOH D2033 O 94.2 148.5 108.4 92.0 73.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 56 OD2
REMARK 620 2 HIS D 161 NE2 87.7
REMARK 620 3 GLU D 173 OE2 110.2 105.6
REMARK 620 4 GLU D 173 OE1 95.5 159.9 54.6
REMARK 620 5 HOH D2033 O 102.4 115.3 127.9 83.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D1210 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ILE D 209 O
REMARK 620 2 HOH D2090 O 98.9
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 ZN A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VNJ A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 1210
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1210
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 1210
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4CO9 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF KYNURENINE FORMAMIDASE FROM BACILLUS ANTHRACIS
REMARK 900 RELATED ID: 4COB RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE KYNURENINE FORMAMIDASE FROM PSEUDOMONAS AERUGINOSA
REMARK 900 RELATED ID: 4COG RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF KYNURENINE FORMAMIDASE FROM BURKHOLDERIA
REMARK 900 CENOCEPACIA
DBREF 4CZ1 A 1 209 UNP Q81PP9 KYNB_BACAN 1 209
DBREF 4CZ1 B 1 209 UNP Q81PP9 KYNB_BACAN 1 209
DBREF 4CZ1 C 1 209 UNP Q81PP9 KYNB_BACAN 1 209
DBREF 4CZ1 D 1 209 UNP Q81PP9 KYNB_BACAN 1 209
SEQRES 1 A 209 MET LYS THR SER LYS TRP ILE ASP ILE SER GLN PRO LEU
SEQRES 2 A 209 ASN ASN ASP ILE ALA THR TRP PRO GLY ASP THR PRO PHE
SEQRES 3 A 209 SER TYR GLU VAL LEU TRP SER LYS GLU GLU SER GLY SER
SEQRES 4 A 209 VAL ASN VAL GLY LYS LEU THR MET SER ILE HIS THR GLY
SEQRES 5 A 209 THR HIS ILE ASP ALA PRO PHE HIS PHE ASP ASN ASP GLY
SEQRES 6 A 209 LYS LYS VAL LEU ASP LEU ASP ILE GLN VAL TYR VAL GLY
SEQRES 7 A 209 PRO THR ARG ILE ILE ASP VAL SER ASN LEU GLU SER ILE
SEQRES 8 A 209 GLY LYS LYS GLU LEU GLU LYS PHE HIS LEU GLU GLY VAL
SEQRES 9 A 209 GLU ARG LEU LEU LEU ARG THR SER SER HIS GLY LYS ALA
SEQRES 10 A 209 ASN GLU PHE PRO ASP ILE ILE PRO HIS LEU ARG ALA ASP
SEQRES 11 A 209 ILE ALA PRO PHE LEU SER GLU LYS GLY ILE ARG LEU ILE
SEQRES 12 A 209 GLY VAL ASP VAL PRO SER VAL ASP PRO LEU ASP ASP LYS
SEQRES 13 A 209 GLU LEU ALA ALA HIS HIS GLN LEU PHE LYS HIS SER ILE
SEQRES 14 A 209 HIS ILE LEU GLU ASN VAL VAL LEU ASP HIS VAL ALA ASP
SEQRES 15 A 209 GLY ASP TYR GLU LEU ILE ALA LEU PRO LEU ALA LEU SER
SEQRES 16 A 209 ASP ALA ASP GLY SER PRO VAL ARG ALA VAL ILE ARG PRO
SEQRES 17 A 209 ILE
SEQRES 1 B 209 MET LYS THR SER LYS TRP ILE ASP ILE SER GLN PRO LEU
SEQRES 2 B 209 ASN ASN ASP ILE ALA THR TRP PRO GLY ASP THR PRO PHE
SEQRES 3 B 209 SER TYR GLU VAL LEU TRP SER LYS GLU GLU SER GLY SER
SEQRES 4 B 209 VAL ASN VAL GLY LYS LEU THR MET SER ILE HIS THR GLY
SEQRES 5 B 209 THR HIS ILE ASP ALA PRO PHE HIS PHE ASP ASN ASP GLY
SEQRES 6 B 209 LYS LYS VAL LEU ASP LEU ASP ILE GLN VAL TYR VAL GLY
SEQRES 7 B 209 PRO THR ARG ILE ILE ASP VAL SER ASN LEU GLU SER ILE
SEQRES 8 B 209 GLY LYS LYS GLU LEU GLU LYS PHE HIS LEU GLU GLY VAL
SEQRES 9 B 209 GLU ARG LEU LEU LEU ARG THR SER SER HIS GLY LYS ALA
SEQRES 10 B 209 ASN GLU PHE PRO ASP ILE ILE PRO HIS LEU ARG ALA ASP
SEQRES 11 B 209 ILE ALA PRO PHE LEU SER GLU LYS GLY ILE ARG LEU ILE
SEQRES 12 B 209 GLY VAL ASP VAL PRO SER VAL ASP PRO LEU ASP ASP LYS
SEQRES 13 B 209 GLU LEU ALA ALA HIS HIS GLN LEU PHE LYS HIS SER ILE
SEQRES 14 B 209 HIS ILE LEU GLU ASN VAL VAL LEU ASP HIS VAL ALA ASP
SEQRES 15 B 209 GLY ASP TYR GLU LEU ILE ALA LEU PRO LEU ALA LEU SER
SEQRES 16 B 209 ASP ALA ASP GLY SER PRO VAL ARG ALA VAL ILE ARG PRO
SEQRES 17 B 209 ILE
SEQRES 1 C 209 MET LYS THR SER LYS TRP ILE ASP ILE SER GLN PRO LEU
SEQRES 2 C 209 ASN ASN ASP ILE ALA THR TRP PRO GLY ASP THR PRO PHE
SEQRES 3 C 209 SER TYR GLU VAL LEU TRP SER LYS GLU GLU SER GLY SER
SEQRES 4 C 209 VAL ASN VAL GLY LYS LEU THR MET SER ILE HIS THR GLY
SEQRES 5 C 209 THR HIS ILE ASP ALA PRO PHE HIS PHE ASP ASN ASP GLY
SEQRES 6 C 209 LYS LYS VAL LEU ASP LEU ASP ILE GLN VAL TYR VAL GLY
SEQRES 7 C 209 PRO THR ARG ILE ILE ASP VAL SER ASN LEU GLU SER ILE
SEQRES 8 C 209 GLY LYS LYS GLU LEU GLU LYS PHE HIS LEU GLU GLY VAL
SEQRES 9 C 209 GLU ARG LEU LEU LEU ARG THR SER SER HIS GLY LYS ALA
SEQRES 10 C 209 ASN GLU PHE PRO ASP ILE ILE PRO HIS LEU ARG ALA ASP
SEQRES 11 C 209 ILE ALA PRO PHE LEU SER GLU LYS GLY ILE ARG LEU ILE
SEQRES 12 C 209 GLY VAL ASP VAL PRO SER VAL ASP PRO LEU ASP ASP LYS
SEQRES 13 C 209 GLU LEU ALA ALA HIS HIS GLN LEU PHE LYS HIS SER ILE
SEQRES 14 C 209 HIS ILE LEU GLU ASN VAL VAL LEU ASP HIS VAL ALA ASP
SEQRES 15 C 209 GLY ASP TYR GLU LEU ILE ALA LEU PRO LEU ALA LEU SER
SEQRES 16 C 209 ASP ALA ASP GLY SER PRO VAL ARG ALA VAL ILE ARG PRO
SEQRES 17 C 209 ILE
SEQRES 1 D 209 MET LYS THR SER LYS TRP ILE ASP ILE SER GLN PRO LEU
SEQRES 2 D 209 ASN ASN ASP ILE ALA THR TRP PRO GLY ASP THR PRO PHE
SEQRES 3 D 209 SER TYR GLU VAL LEU TRP SER LYS GLU GLU SER GLY SER
SEQRES 4 D 209 VAL ASN VAL GLY LYS LEU THR MET SER ILE HIS THR GLY
SEQRES 5 D 209 THR HIS ILE ASP ALA PRO PHE HIS PHE ASP ASN ASP GLY
SEQRES 6 D 209 LYS LYS VAL LEU ASP LEU ASP ILE GLN VAL TYR VAL GLY
SEQRES 7 D 209 PRO THR ARG ILE ILE ASP VAL SER ASN LEU GLU SER ILE
SEQRES 8 D 209 GLY LYS LYS GLU LEU GLU LYS PHE HIS LEU GLU GLY VAL
SEQRES 9 D 209 GLU ARG LEU LEU LEU ARG THR SER SER HIS GLY LYS ALA
SEQRES 10 D 209 ASN GLU PHE PRO ASP ILE ILE PRO HIS LEU ARG ALA ASP
SEQRES 11 D 209 ILE ALA PRO PHE LEU SER GLU LYS GLY ILE ARG LEU ILE
SEQRES 12 D 209 GLY VAL ASP VAL PRO SER VAL ASP PRO LEU ASP ASP LYS
SEQRES 13 D 209 GLU LEU ALA ALA HIS HIS GLN LEU PHE LYS HIS SER ILE
SEQRES 14 D 209 HIS ILE LEU GLU ASN VAL VAL LEU ASP HIS VAL ALA ASP
SEQRES 15 D 209 GLY ASP TYR GLU LEU ILE ALA LEU PRO LEU ALA LEU SER
SEQRES 16 D 209 ASP ALA ASP GLY SER PRO VAL ARG ALA VAL ILE ARG PRO
SEQRES 17 D 209 ILE
HET ZN A 401 1
HET ZN A 402 1
HET VNJ A 501 10
HET MG A1210 1
HET ZN B 401 1
HET ZN B 402 1
HET ZN C 401 1
HET ZN C 402 1
HET MG C1210 1
HET ZN D 401 1
HET ZN D 402 1
HET MG D1210 1
HETNAM ZN ZINC ION
HETNAM VNJ 2-AMINOACETOPHENONE
HETNAM MG MAGNESIUM ION
FORMUL 5 ZN 8(ZN 2+)
FORMUL 7 VNJ C8 H9 N O
FORMUL 8 MG 3(MG 2+)
FORMUL 17 HOH *412(H2 O)
HELIX 1 1 SER A 33 GLY A 38 1 6
HELIX 2 2 PRO A 58 PHE A 61 5 4
HELIX 3 3 LYS A 67 LEU A 71 5 5
HELIX 4 4 ASP A 72 VAL A 75 5 4
HELIX 5 5 GLY A 92 GLU A 97 1 6
HELIX 6 6 ASP A 130 LYS A 138 1 9
HELIX 7 7 LEU A 158 HIS A 167 1 10
HELIX 8 8 SER B 33 GLY B 38 1 6
HELIX 9 9 PRO B 58 PHE B 61 5 4
HELIX 10 10 LYS B 67 LEU B 71 5 5
HELIX 11 11 ASP B 72 VAL B 75 5 4
HELIX 12 12 GLY B 92 GLU B 97 1 6
HELIX 13 13 ASP B 130 GLY B 139 1 10
HELIX 14 14 LEU B 158 HIS B 167 1 10
HELIX 15 15 SER C 33 GLY C 38 1 6
HELIX 16 16 PRO C 58 PHE C 61 5 4
HELIX 17 17 LYS C 67 LEU C 71 5 5
HELIX 18 18 ASP C 72 VAL C 75 5 4
HELIX 19 19 GLY C 92 GLU C 97 1 6
HELIX 20 20 ASP C 130 GLY C 139 1 10
HELIX 21 21 LEU C 158 HIS C 167 1 10
HELIX 22 22 SER D 33 GLY D 38 1 6
HELIX 23 23 PRO D 58 PHE D 61 5 4
HELIX 24 24 LYS D 67 LEU D 71 5 5
HELIX 25 25 ASP D 72 VAL D 75 5 4
HELIX 26 26 GLY D 92 GLU D 97 1 6
HELIX 27 27 ASP D 130 GLY D 139 1 10
HELIX 28 28 LEU D 158 HIS D 167 1 10
SHEET 1 AA 9 ILE A 7 ASP A 8 0
SHEET 2 AA 9 VAL A 205 PRO A 208 -1 O ILE A 206 N ILE A 7
SHEET 3 AA 9 GLY A 183 ILE A 188 -1 O GLU A 186 N ARG A 207
SHEET 4 AA 9 VAL A 77 ASP A 84 -1 O GLY A 78 N LEU A 187
SHEET 5 AA 9 ARG A 106 ARG A 110 1 O ARG A 106 N ARG A 81
SHEET 6 AA 9 LEU A 142 VAL A 145 1 O LEU A 142 N LEU A 107
SHEET 7 AA 9 HIS A 170 GLU A 173 1 O HIS A 170 N ILE A 143
SHEET 8 AA 9 HIS A 54 ASP A 56 -1 O HIS A 54 N GLU A 173
SHEET 9 AA 9 GLY A 199 PRO A 201 -1 O SER A 200 N ILE A 55
SHEET 1 AB 4 SER A 27 TRP A 32 0
SHEET 2 AB 4 VAL A 42 SER A 48 -1 O VAL A 42 N LEU A 31
SHEET 3 AB 4 VAL B 42 MET B 47 -1 O LEU B 45 N MET A 47
SHEET 4 AB 4 SER B 27 TRP B 32 -1 O SER B 27 N THR B 46
SHEET 1 AC 2 SER A 90 ILE A 91 0
SHEET 2 AC 2 HIS A 126 LEU A 127 1 O HIS A 126 N ILE A 91
SHEET 1 BA 9 ILE B 7 ASP B 8 0
SHEET 2 BA 9 VAL B 205 PRO B 208 -1 O ILE B 206 N ILE B 7
SHEET 3 BA 9 GLY B 183 ILE B 188 -1 O GLU B 186 N ARG B 207
SHEET 4 BA 9 VAL B 77 ASP B 84 -1 O GLY B 78 N LEU B 187
SHEET 5 BA 9 ARG B 106 ARG B 110 1 O ARG B 106 N ARG B 81
SHEET 6 BA 9 LEU B 142 VAL B 145 1 O LEU B 142 N LEU B 107
SHEET 7 BA 9 HIS B 170 GLU B 173 1 O HIS B 170 N ILE B 143
SHEET 8 BA 9 HIS B 54 ASP B 56 -1 O HIS B 54 N GLU B 173
SHEET 9 BA 9 GLY B 199 PRO B 201 -1 O SER B 200 N ILE B 55
SHEET 1 BB 2 SER B 90 ILE B 91 0
SHEET 2 BB 2 HIS B 126 LEU B 127 1 O HIS B 126 N ILE B 91
SHEET 1 CA 9 ILE C 7 ASP C 8 0
SHEET 2 CA 9 VAL C 205 PRO C 208 -1 O ILE C 206 N ILE C 7
SHEET 3 CA 9 GLY C 183 ILE C 188 -1 O GLU C 186 N ARG C 207
SHEET 4 CA 9 VAL C 77 ASP C 84 -1 O GLY C 78 N LEU C 187
SHEET 5 CA 9 ARG C 106 ARG C 110 1 O ARG C 106 N ARG C 81
SHEET 6 CA 9 LEU C 142 VAL C 145 1 O LEU C 142 N LEU C 107
SHEET 7 CA 9 HIS C 170 GLU C 173 1 O HIS C 170 N ILE C 143
SHEET 8 CA 9 HIS C 54 ASP C 56 -1 O HIS C 54 N GLU C 173
SHEET 9 CA 9 GLY C 199 PRO C 201 -1 O SER C 200 N ILE C 55
SHEET 1 CB 4 SER C 27 TRP C 32 0
SHEET 2 CB 4 VAL C 42 SER C 48 -1 O VAL C 42 N LEU C 31
SHEET 3 CB 4 VAL D 42 MET D 47 -1 O LEU D 45 N MET C 47
SHEET 4 CB 4 SER D 27 TRP D 32 -1 O SER D 27 N THR D 46
SHEET 1 CC 2 SER C 90 ILE C 91 0
SHEET 2 CC 2 HIS C 126 LEU C 127 1 O HIS C 126 N ILE C 91
SHEET 1 DA 9 ILE D 7 ASP D 8 0
SHEET 2 DA 9 VAL D 205 PRO D 208 -1 O ILE D 206 N ILE D 7
SHEET 3 DA 9 GLY D 183 ILE D 188 -1 O GLU D 186 N ARG D 207
SHEET 4 DA 9 VAL D 77 ASP D 84 -1 O GLY D 78 N LEU D 187
SHEET 5 DA 9 ARG D 106 ARG D 110 1 O ARG D 106 N ARG D 81
SHEET 6 DA 9 LEU D 142 VAL D 145 1 O LEU D 142 N LEU D 107
SHEET 7 DA 9 HIS D 170 GLU D 173 1 O HIS D 170 N ILE D 143
SHEET 8 DA 9 HIS D 54 ASP D 56 -1 O HIS D 54 N GLU D 173
SHEET 9 DA 9 GLY D 199 PRO D 201 -1 O SER D 200 N ILE D 55
SHEET 1 DB 2 SER D 90 ILE D 91 0
SHEET 2 DB 2 HIS D 126 LEU D 127 1 O HIS D 126 N ILE D 91
LINK ND1 HIS A 50 ZN ZN A 402 1555 1555 2.26
LINK NE2 HIS A 54 ZN ZN A 402 1555 1555 2.39
LINK OD2 ASP A 56 ZN ZN A 401 1555 1555 2.02
LINK OD1 ASP A 56 ZN ZN A 402 1555 1555 2.17
LINK OD1 ASP A 64 MG MG A1210 1555 1555 2.65
LINK NE2 HIS A 161 ZN ZN A 401 1555 1555 2.24
LINK OE2 GLU A 173 ZN ZN A 401 1555 1555 2.24
LINK OE1 GLU A 173 ZN ZN A 401 1555 1555 2.67
LINK OE1 GLU A 173 ZN ZN A 402 1555 1555 2.49
LINK ZN ZN A 401 O HOH A2046 1555 1555 2.25
LINK ZN ZN A 401 O HOH A2103 1555 1555 2.17
LINK ZN ZN A 402 O HOH A2027 1555 1555 2.32
LINK ZN ZN A 402 O HOH A2046 1555 1555 2.48
LINK MG MG A1210 O HOH A2054 1555 1555 2.24
LINK MG MG A1210 O HOH A2055 1555 1555 2.24
LINK MG MG A1210 O HOH A2132 1555 1555 2.06
LINK ND1 HIS B 50 ZN ZN B 402 1555 1555 2.40
LINK NE2 HIS B 54 ZN ZN B 402 1555 1555 2.27
LINK OD2 ASP B 56 ZN ZN B 401 1555 1555 2.08
LINK OD1 ASP B 56 ZN ZN B 402 1555 1555 2.33
LINK NE2 HIS B 161 ZN ZN B 401 1555 1555 2.20
LINK OE1 GLU B 173 ZN ZN B 401 1555 1555 2.61
LINK OE2 GLU B 173 ZN ZN B 401 1555 1555 2.08
LINK OE1 GLU B 173 ZN ZN B 402 1555 1555 2.27
LINK ZN ZN B 401 O HOH B2022 1555 1555 2.21
LINK ZN ZN B 401 O HOH B2053 1555 1555 2.59
LINK ZN ZN B 402 O HOH B2016 1555 1555 2.45
LINK ZN ZN B 402 O HOH B2022 1555 1555 2.31
LINK O GLY C 38 MG MG C1210 1555 1555 2.10
LINK ND1 HIS C 50 ZN ZN C 402 1555 1555 2.24
LINK NE2 HIS C 54 ZN ZN C 402 1555 1555 2.35
LINK OD2 ASP C 56 ZN ZN C 401 1555 1555 2.10
LINK OD1 ASP C 56 ZN ZN C 402 1555 1555 2.24
LINK NE2 HIS C 161 ZN ZN C 401 1555 1555 2.27
LINK OE2 GLU C 173 ZN ZN C 401 1555 1555 2.10
LINK OE1 GLU C 173 ZN ZN C 401 1555 1555 2.57
LINK OE1 GLU C 173 ZN ZN C 402 1555 1555 2.44
LINK ZN ZN C 401 O HOH C2055 1555 1555 2.34
LINK ZN ZN C 401 O HOH C2092 1555 1555 2.54
LINK ZN ZN C 402 O HOH C2024 1555 1555 2.40
LINK ZN ZN C 402 O HOH C2055 1555 1555 2.04
LINK MG MG C1210 O HOH C2049 1555 1555 2.06
LINK MG MG C1210 O HOH C2050 1555 1555 2.21
LINK MG MG C1210 O HOH C2051 1555 1555 2.55
LINK MG MG C1210 O HOH C2052 1555 1555 2.09
LINK MG MG C1210 O HOH C2115 1555 1555 2.31
LINK ND1 HIS D 50 ZN ZN D 402 1555 1555 2.42
LINK NE2 HIS D 54 ZN ZN D 402 1555 1555 2.39
LINK OD2 ASP D 56 ZN ZN D 401 1555 1555 2.08
LINK OD1 ASP D 56 ZN ZN D 402 1555 1555 2.23
LINK NE2 HIS D 161 ZN ZN D 401 1555 1555 2.16
LINK OE2 GLU D 173 ZN ZN D 401 1555 1555 2.15
LINK OE1 GLU D 173 ZN ZN D 401 1555 1555 2.62
LINK OE1 GLU D 173 ZN ZN D 402 1555 1555 2.32
LINK O ILE D 209 MG MG D1210 1555 1555 2.84
LINK ZN ZN D 401 O HOH D2033 1555 1555 2.27
LINK ZN ZN D 402 O HOH D2022 1555 1555 2.38
LINK ZN ZN D 402 O HOH D2033 1555 1555 2.21
LINK MG MG D1210 O HOH D2090 1555 1555 1.79
SITE 1 AC1 6 ASP A 56 HIS A 161 GLU A 173 ZN A 402
SITE 2 AC1 6 HOH A2046 HOH A2103
SITE 1 AC2 7 HIS A 50 HIS A 54 ASP A 56 GLU A 173
SITE 2 AC2 7 ZN A 401 HOH A2027 HOH A2046
SITE 1 AC3 6 TRP A 20 ASP A 23 HIS A 50 HIS A 60
SITE 2 AC3 6 HOH A2046 VAL B 40
SITE 1 AC4 6 ASP B 56 HIS B 161 GLU B 173 ZN B 402
SITE 2 AC4 6 HOH B2022 HOH B2053
SITE 1 AC5 7 HIS B 50 HIS B 54 ASP B 56 GLU B 173
SITE 2 AC5 7 ZN B 401 HOH B2016 HOH B2022
SITE 1 AC6 6 ASP C 56 HIS C 161 GLU C 173 ZN C 402
SITE 2 AC6 6 HOH C2055 HOH C2092
SITE 1 AC7 7 HIS C 50 HIS C 54 ASP C 56 GLU C 173
SITE 2 AC7 7 ZN C 401 HOH C2024 HOH C2055
SITE 1 AC8 5 ASP D 56 HIS D 161 GLU D 173 ZN D 402
SITE 2 AC8 5 HOH D2033
SITE 1 AC9 7 HIS D 50 HIS D 54 ASP D 56 GLU D 173
SITE 2 AC9 7 ZN D 401 HOH D2022 HOH D2033
SITE 1 BC1 6 GLY C 38 HOH C2049 HOH C2050 HOH C2051
SITE 2 BC1 6 HOH C2052 HOH C2115
SITE 1 BC2 4 ASP A 64 HOH A2054 HOH A2055 HOH A2132
SITE 1 BC3 3 ILE D 209 HOH D2090 HOH D2091
CRYST1 73.695 66.561 84.061 90.00 90.24 90.00 P 1 21 1 8
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 0.013569 0.000000 0.000057 0.00000
SCALE2 0.000000 0.015024 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011896 0.00000
(ATOM LINES ARE NOT SHOWN.)
END