HEADER TRANSFERASE 15-APR-14 4CYU
TITLE STAPHYLOCOCCUS AUREUS 7,8-DIHYDRO-6-HYDROXYMETHYLPTERIN-
TITLE 2 PYROPHOSPHOKINASE IN COMPLEX WITH AMPCPP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 7,8-DIHYDRO-6-HYDROXYMETHYLPTERIN-PYROPHOSPHOKINASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: HPPK;
COMPND 5 EC: 2.7.6.3;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: 7,8-DIHYDRO-6-HYDROXYMETHYLPTERIN-PYROPHOSPHOKINASE;
COMPND 9 CHAIN: B, C, D;
COMPND 10 SYNONYM: HPPK;
COMPND 11 EC: 2.7.6.3;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;
SOURCE 3 ORGANISM_TAXID: 1280;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PET;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;
SOURCE 11 ORGANISM_TAXID: 1280;
SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 13 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 14 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 15 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 16 EXPRESSION_SYSTEM_VECTOR: PET
KEYWDS TRANSFERASE, S.AUREUS, FOLATE, STRUCTURE-BASED DRUG DESIGN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.L.DENNIS,J.D.SWARBRICK,T.S.PEAT
REVDAT 3 20-DEC-23 4CYU 1 REMARK LINK
REVDAT 2 08-MAY-19 4CYU 1 REMARK
REVDAT 1 28-JAN-15 4CYU 0
JRNL AUTH M.L.DENNIS,S.CHHABRA,Z.WANG,A.DEBONO,O.DOLEZAL,J.NEWMAN,
JRNL AUTH 2 N.P.PITCHER,R.RAHMANI,B.CLEARY,N.BARLOW,M.HATTARKI,B.GRAHAM,
JRNL AUTH 3 T.S.PEAT,J.B.BAELL,J.D.SWARBRICK
JRNL TITL STRUCTURE-BASED DESIGN AND DEVELOPMENT OF FUNCTIONALIZED
JRNL TITL 2 MERCAPTOGUANINE DERIVATIVES AS INHIBITORS OF THE FOLATE
JRNL TITL 3 BIOSYNTHESIS PATHWAY ENZYME
JRNL TITL 4 6-HYDROXYMETHYL-7,8-DIHYDROPTERIN PYROPHOSPHOKINASE FROM
JRNL TITL 5 STAPHYLOCOCCUS AUREUS.
JRNL REF J.MED.CHEM. V. 57 9612 2014
JRNL REFN ISSN 0022-2623
JRNL PMID 25357262
JRNL DOI 10.1021/JM501417F
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0029
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) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.53
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 17651
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) : 0.194
REMARK 3 R VALUE (WORKING SET) : 0.192
REMARK 3 FREE R VALUE : 0.242
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.500
REMARK 3 FREE R VALUE TEST SET COUNT : 838
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) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.77
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1303
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.3190
REMARK 3 BIN FREE R VALUE SET COUNT : 55
REMARK 3 BIN FREE R VALUE : 0.3830
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4999
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 148
REMARK 3 SOLVENT ATOMS : 13
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 54.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.16000
REMARK 3 B22 (A**2) : 0.06000
REMARK 3 B33 (A**2) : -0.98000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 2.65000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.361
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.960
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.932
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5293 ; 0.010 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 5116 ; 0.000 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7224 ; 1.493 ; 2.040
REMARK 3 BOND ANGLES OTHERS (DEGREES): 11796 ; 3.437 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 619 ; 6.304 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 233 ;33.791 ;24.807
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 943 ;14.635 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 36 ;16.655 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 839 ; 0.071 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5702 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1094 ; 0.005 ; 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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 NUMBER OF DIFFERENT NCS GROUPS : NULL
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 : 1.10
REMARK 3 ION PROBE RADIUS : 0.90
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS. U VALUES REFINED INDIVIDUALLY RESIDUES OF LOOP 2 ARE
REMARK 3 NOT MODELLED IN CHAINS A (RESIDUES 45-48) AND B (RESIDUES 46-48)
REMARK 3 DUE TO POOR DENSITY.
REMARK 4
REMARK 4 4CYU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-APR-14.
REMARK 100 THE DEPOSITION ID IS D_1290060352.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-DEC-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.008000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18506
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 45.530
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.500
REMARK 200 R MERGE (I) : 0.14000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.4000
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) : 2.83
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.30
REMARK 200 R MERGE FOR SHELL (I) : 0.90000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 4AD6
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.62
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN 6.9 MG/ML 1 MM AMPCPP, 2 MM
REMARK 280 MAGNESIUM CHLORIDE, MAGNESIUM ACETATE 0.119 M, PEG8000 12.6% W/V,
REMARK 280 TRIS CHLORIDE 0.12 M, SITTING DROP, 281 K, PH 8, VAPOR
REMARK 280 DIFFUSION, SITTING DROP
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 47.13150
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, 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 GLY A -2
REMARK 465 SER A -1
REMARK 465 PRO A 45
REMARK 465 VAL A 46
REMARK 465 GLY A 47
REMARK 465 TYR A 48
REMARK 465 LYS A 158
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 HIS B 0
REMARK 465 VAL B 46
REMARK 465 GLY B 47
REMARK 465 TYR B 48
REMARK 465 GLY C -2
REMARK 465 SER C -1
REMARK 465 LYS C 158
REMARK 465 GLY D -2
REMARK 465 SER D -1
REMARK 465 LYS D 158
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 OE2 GLU A 28 NH1 ARG B 88 2.14
REMARK 500 OE2 GLU C 50 NH2 ARG D 156 2.19
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 ALA A 132 33.79 -148.87
REMARK 500 ALA B 132 33.26 -148.11
REMARK 500 LYS C 86 156.07 -42.12
REMARK 500 ALA C 132 33.65 -148.37
REMARK 500 ALA D 132 33.48 -147.87
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 MG A 170 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 95 OD1
REMARK 620 2 ASP A 97 OD1 74.4
REMARK 620 3 APC A1158 O1A 77.6 150.2
REMARK 620 4 APC A1158 O1B 82.1 94.6 91.5
REMARK 620 5 HOH A2002 O 64.2 78.3 80.4 146.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 171 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 95 OD2
REMARK 620 2 ASP A 97 OD2 75.4
REMARK 620 3 APC A1158 O1B 69.7 73.8
REMARK 620 4 APC A1158 O1G 136.8 75.8 71.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 170 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 78 OE2
REMARK 620 2 ASP B 95 OD1 75.3
REMARK 620 3 ASP B 97 OD1 121.5 73.1
REMARK 620 4 APC B1159 O1A 113.1 75.2 104.5
REMARK 620 5 APC B1159 O1A 101.2 76.4 116.9 13.2
REMARK 620 6 HOH B2001 O 172.0 108.8 66.4 62.6 73.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 171 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 95 OD2
REMARK 620 2 ASP B 97 OD2 76.4
REMARK 620 3 APC B1159 O1B 123.3 104.7
REMARK 620 4 APC B1159 O2B 69.7 86.6 54.1
REMARK 620 5 APC B1159 O1B 72.9 77.8 53.1 10.2
REMARK 620 6 APC B1159 O1G 140.2 69.7 50.9 87.9 80.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 170 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 95 OD1
REMARK 620 2 ASP C 97 OD1 76.5
REMARK 620 3 APC C1158 O1B 86.0 88.7
REMARK 620 4 APC C1158 O1A 87.9 163.6 85.0
REMARK 620 5 HOH C2001 O 78.2 80.9 162.7 101.2
REMARK 620 6 HOH C2002 O 159.9 83.4 93.6 112.1 98.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 171 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 95 OD2
REMARK 620 2 ASP C 97 OD2 78.4
REMARK 620 3 APC C1158 O1G 139.6 77.5
REMARK 620 4 APC C1158 O1B 70.1 75.5 72.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D 170 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 95 OD1
REMARK 620 2 ASP D 97 OD1 74.8
REMARK 620 3 APC D1158 O1B 81.5 87.7
REMARK 620 4 APC D1158 O1A 73.3 146.9 79.1
REMARK 620 5 APC D1158 O2B 71.4 92.9 13.1 68.7
REMARK 620 6 APC D1158 O1A 84.9 151.5 69.3 16.0 61.2
REMARK 620 7 HOH D2002 O 84.8 85.6 166.0 100.1 155.6 112.8
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D 171 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 95 OD2
REMARK 620 2 ASP D 97 OD2 78.0
REMARK 620 3 APC D1158 O1G 153.4 84.8
REMARK 620 4 APC D1158 O1B 76.8 76.4 79.5
REMARK 620 5 APC D1158 O2B 70.7 87.4 88.5 13.8
REMARK 620 6 APC D1158 O1B 124.4 113.3 46.0 56.3 56.6
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 170
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 171
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 170
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 171
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 170
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 171
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 170
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 171
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE APC A 1158
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE APC B 1159
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE APC C 1158
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE APC D 1158
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS B 1160
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS A 1159
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 HEXAHISTIDINE-TAG WITH THROMBIN CLEAVAGE AT THE N-TERMINUS
DBREF 4CYU A 1 158 UNP C8MLE4 C8MLE4_STAAU 1 158
DBREF 4CYU B 1 158 UNP C8MLE4 C8MLE4_STAAU 1 158
DBREF 4CYU C 1 158 UNP C8MLE4 C8MLE4_STAAU 1 158
DBREF 4CYU D 1 158 UNP C8MLE4 C8MLE4_STAAU 1 158
SEQADV 4CYU GLY A -2 UNP C8MLE4 EXPRESSION TAG
SEQADV 4CYU SER A -1 UNP C8MLE4 EXPRESSION TAG
SEQADV 4CYU HIS A 0 UNP C8MLE4 EXPRESSION TAG
SEQADV 4CYU ASN A 151 UNP C8MLE4 ASP 151 CONFLICT
SEQADV 4CYU GLY B -2 UNP C8MLE4 EXPRESSION TAG
SEQADV 4CYU SER B -1 UNP C8MLE4 EXPRESSION TAG
SEQADV 4CYU HIS B 0 UNP C8MLE4 EXPRESSION TAG
SEQADV 4CYU GLY C -2 UNP C8MLE4 EXPRESSION TAG
SEQADV 4CYU SER C -1 UNP C8MLE4 EXPRESSION TAG
SEQADV 4CYU HIS C 0 UNP C8MLE4 EXPRESSION TAG
SEQADV 4CYU GLY D -2 UNP C8MLE4 EXPRESSION TAG
SEQADV 4CYU SER D -1 UNP C8MLE4 EXPRESSION TAG
SEQADV 4CYU HIS D 0 UNP C8MLE4 EXPRESSION TAG
SEQRES 1 A 161 GLY SER HIS MET ILE GLN ALA TYR LEU GLY LEU GLY SER
SEQRES 2 A 161 ASN ILE GLY ASP ARG GLU SER GLN LEU ASN ASP ALA ILE
SEQRES 3 A 161 LYS ILE LEU ASN GLU TYR ASP GLY ILE SER VAL SER ASN
SEQRES 4 A 161 ILE SER PRO ILE TYR GLU THR ALA PRO VAL GLY TYR THR
SEQRES 5 A 161 GLU GLN PRO ASN PHE LEU ASN LEU CYS VAL GLU ILE GLN
SEQRES 6 A 161 THR THR LEU THR VAL LEU GLN LEU LEU GLU CYS CYS LEU
SEQRES 7 A 161 LYS THR GLU GLU CYS LEU HIS ARG ILE ARG LYS GLU ARG
SEQRES 8 A 161 TRP GLY PRO ARG THR LEU ASP VAL ASP ILE LEU LEU TYR
SEQRES 9 A 161 GLY GLU GLU MET ILE ASP LEU PRO LYS LEU SER VAL PRO
SEQRES 10 A 161 HIS PRO ARG MET ASN GLU ARG ALA PHE VAL LEU ILE PRO
SEQRES 11 A 161 LEU ASN ASP ILE ALA ALA ASN VAL VAL GLU PRO ARG SER
SEQRES 12 A 161 LYS LEU LYS VAL LYS ASP LEU VAL PHE VAL ASN ASP SER
SEQRES 13 A 161 VAL LYS ARG TYR LYS
SEQRES 1 B 161 GLY SER HIS MET ILE GLN ALA TYR LEU GLY LEU GLY SER
SEQRES 2 B 161 ASN ILE GLY ASP ARG GLU SER GLN LEU ASN ASP ALA ILE
SEQRES 3 B 161 LYS ILE LEU ASN GLU TYR ASP GLY ILE SER VAL SER ASN
SEQRES 4 B 161 ILE SER PRO ILE TYR GLU THR ALA PRO VAL GLY TYR THR
SEQRES 5 B 161 GLU GLN PRO ASN PHE LEU ASN LEU CYS VAL GLU ILE GLN
SEQRES 6 B 161 THR THR LEU THR VAL LEU GLN LEU LEU GLU CYS CYS LEU
SEQRES 7 B 161 LYS THR GLU GLU CYS LEU HIS ARG ILE ARG LYS GLU ARG
SEQRES 8 B 161 TRP GLY PRO ARG THR LEU ASP VAL ASP ILE LEU LEU TYR
SEQRES 9 B 161 GLY GLU GLU MET ILE ASP LEU PRO LYS LEU SER VAL PRO
SEQRES 10 B 161 HIS PRO ARG MET ASN GLU ARG ALA PHE VAL LEU ILE PRO
SEQRES 11 B 161 LEU ASN ASP ILE ALA ALA ASN VAL VAL GLU PRO ARG SER
SEQRES 12 B 161 LYS LEU LYS VAL LYS ASP LEU VAL PHE VAL ASP ASP SER
SEQRES 13 B 161 VAL LYS ARG TYR LYS
SEQRES 1 C 161 GLY SER HIS MET ILE GLN ALA TYR LEU GLY LEU GLY SER
SEQRES 2 C 161 ASN ILE GLY ASP ARG GLU SER GLN LEU ASN ASP ALA ILE
SEQRES 3 C 161 LYS ILE LEU ASN GLU TYR ASP GLY ILE SER VAL SER ASN
SEQRES 4 C 161 ILE SER PRO ILE TYR GLU THR ALA PRO VAL GLY TYR THR
SEQRES 5 C 161 GLU GLN PRO ASN PHE LEU ASN LEU CYS VAL GLU ILE GLN
SEQRES 6 C 161 THR THR LEU THR VAL LEU GLN LEU LEU GLU CYS CYS LEU
SEQRES 7 C 161 LYS THR GLU GLU CYS LEU HIS ARG ILE ARG LYS GLU ARG
SEQRES 8 C 161 TRP GLY PRO ARG THR LEU ASP VAL ASP ILE LEU LEU TYR
SEQRES 9 C 161 GLY GLU GLU MET ILE ASP LEU PRO LYS LEU SER VAL PRO
SEQRES 10 C 161 HIS PRO ARG MET ASN GLU ARG ALA PHE VAL LEU ILE PRO
SEQRES 11 C 161 LEU ASN ASP ILE ALA ALA ASN VAL VAL GLU PRO ARG SER
SEQRES 12 C 161 LYS LEU LYS VAL LYS ASP LEU VAL PHE VAL ASP ASP SER
SEQRES 13 C 161 VAL LYS ARG TYR LYS
SEQRES 1 D 161 GLY SER HIS MET ILE GLN ALA TYR LEU GLY LEU GLY SER
SEQRES 2 D 161 ASN ILE GLY ASP ARG GLU SER GLN LEU ASN ASP ALA ILE
SEQRES 3 D 161 LYS ILE LEU ASN GLU TYR ASP GLY ILE SER VAL SER ASN
SEQRES 4 D 161 ILE SER PRO ILE TYR GLU THR ALA PRO VAL GLY TYR THR
SEQRES 5 D 161 GLU GLN PRO ASN PHE LEU ASN LEU CYS VAL GLU ILE GLN
SEQRES 6 D 161 THR THR LEU THR VAL LEU GLN LEU LEU GLU CYS CYS LEU
SEQRES 7 D 161 LYS THR GLU GLU CYS LEU HIS ARG ILE ARG LYS GLU ARG
SEQRES 8 D 161 TRP GLY PRO ARG THR LEU ASP VAL ASP ILE LEU LEU TYR
SEQRES 9 D 161 GLY GLU GLU MET ILE ASP LEU PRO LYS LEU SER VAL PRO
SEQRES 10 D 161 HIS PRO ARG MET ASN GLU ARG ALA PHE VAL LEU ILE PRO
SEQRES 11 D 161 LEU ASN ASP ILE ALA ALA ASN VAL VAL GLU PRO ARG SER
SEQRES 12 D 161 LYS LEU LYS VAL LYS ASP LEU VAL PHE VAL ASP ASP SER
SEQRES 13 D 161 VAL LYS ARG TYR LYS
HET MG A 170 1
HET MG A 171 1
HET APC A1158 31
HET TRS A1159 8
HET MG B 170 1
HET MG B 171 1
HET APC B1159 62
HET TRS B1160 8
HET MG C 170 1
HET MG C 171 1
HET APC C1158 31
HET MG D 170 1
HET MG D 171 1
HET APC D1158 62
HETNAM MG MAGNESIUM ION
HETNAM APC DIPHOSPHOMETHYLPHOSPHONIC ACID ADENOSYL ESTER
HETNAM TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL
HETSYN APC ALPHA,BETA-METHYLENEADENOSINE-5'-TRIPHOSPHATE
HETSYN TRS TRIS BUFFER
FORMUL 5 MG 8(MG 2+)
FORMUL 7 APC 4(C11 H18 N5 O12 P3)
FORMUL 8 TRS 2(C4 H12 N O3 1+)
FORMUL 19 HOH *13(H2 O)
HELIX 1 1 ASP A 14 GLU A 28 1 15
HELIX 2 2 THR A 66 ILE A 84 1 19
HELIX 3 3 ARG A 117 GLU A 120 5 4
HELIX 4 4 ARG A 121 ALA A 133 1 13
HELIX 5 5 VAL A 144 VAL A 148 1 5
HELIX 6 6 ASP B 14 GLU B 28 1 15
HELIX 7 7 THR B 66 ILE B 84 1 19
HELIX 8 8 ARG B 117 GLU B 120 5 4
HELIX 9 9 ARG B 121 ALA B 133 1 13
HELIX 10 10 VAL B 144 VAL B 148 1 5
HELIX 11 11 ASP C 14 ASN C 27 1 14
HELIX 12 12 THR C 66 LYS C 86 1 21
HELIX 13 13 ARG C 117 GLU C 120 5 4
HELIX 14 14 ARG C 121 ALA C 133 1 13
HELIX 15 15 VAL C 144 VAL C 148 1 5
HELIX 16 16 ASP D 14 GLU D 28 1 15
HELIX 17 17 THR D 66 ARG D 85 1 20
HELIX 18 18 ARG D 117 GLU D 120 5 4
HELIX 19 19 ARG D 121 ALA D 133 1 13
HELIX 20 20 VAL D 144 VAL D 148 1 5
SHEET 1 AA 2 ILE A 32 ILE A 37 0
SHEET 2 AA 2 PHE A 54 THR A 63 -1 O GLU A 60 N SER A 35
SHEET 1 AB 5 ASP A 95 TYR A 101 0
SHEET 2 AB 5 ILE A 2 SER A 10 -1 O TYR A 5 N LEU A 99
SHEET 3 AB 5 PHE A 54 THR A 63 -1 O LEU A 55 N SER A 10
SHEET 4 AB 5 TYR A 41 THR A 43 -1 O TYR A 41 N ASN A 56
SHEET 5 AB 5 VAL A 154 ARG A 156 -1 O LYS A 155 N GLU A 42
SHEET 1 AC 4 ASP A 95 TYR A 101 0
SHEET 2 AC 4 ILE A 2 SER A 10 -1 O TYR A 5 N LEU A 99
SHEET 3 AC 4 PHE A 54 THR A 63 -1 O LEU A 55 N SER A 10
SHEET 4 AC 4 ILE A 32 ILE A 37 -1 O SER A 33 N GLN A 62
SHEET 1 AD 2 ILE A 106 LEU A 108 0
SHEET 2 AD 2 LEU A 111 VAL A 113 -1 O LEU A 111 N LEU A 108
SHEET 1 AE 2 VAL A 136 GLU A 137 0
SHEET 2 AE 2 LEU A 142 LYS A 143 -1 O LEU A 142 N GLU A 137
SHEET 1 BA 2 ILE B 32 ILE B 37 0
SHEET 2 BA 2 PHE B 54 THR B 63 -1 O GLU B 60 N SER B 35
SHEET 1 BB 5 ASP B 95 TYR B 101 0
SHEET 2 BB 5 ILE B 2 SER B 10 -1 O TYR B 5 N LEU B 99
SHEET 3 BB 5 PHE B 54 THR B 63 -1 O LEU B 55 N SER B 10
SHEET 4 BB 5 TYR B 41 THR B 43 -1 O TYR B 41 N ASN B 56
SHEET 5 BB 5 VAL B 154 ARG B 156 -1 O LYS B 155 N GLU B 42
SHEET 1 BC 4 ASP B 95 TYR B 101 0
SHEET 2 BC 4 ILE B 2 SER B 10 -1 O TYR B 5 N LEU B 99
SHEET 3 BC 4 PHE B 54 THR B 63 -1 O LEU B 55 N SER B 10
SHEET 4 BC 4 ILE B 32 ILE B 37 -1 O SER B 33 N GLN B 62
SHEET 1 BD 2 ILE B 106 LEU B 108 0
SHEET 2 BD 2 LEU B 111 VAL B 113 -1 O LEU B 111 N LEU B 108
SHEET 1 BE 2 VAL B 136 GLU B 137 0
SHEET 2 BE 2 LEU B 142 LYS B 143 -1 O LEU B 142 N GLU B 137
SHEET 1 CA 2 ILE C 32 ILE C 37 0
SHEET 2 CA 2 PHE C 54 THR C 63 -1 O GLU C 60 N SER C 35
SHEET 1 CB 5 ASP C 95 TYR C 101 0
SHEET 2 CB 5 ILE C 2 SER C 10 -1 O TYR C 5 N LEU C 99
SHEET 3 CB 5 PHE C 54 THR C 63 -1 O LEU C 55 N SER C 10
SHEET 4 CB 5 TYR C 41 THR C 43 -1 O TYR C 41 N ASN C 56
SHEET 5 CB 5 VAL C 154 ARG C 156 -1 O LYS C 155 N GLU C 42
SHEET 1 CC 4 ASP C 95 TYR C 101 0
SHEET 2 CC 4 ILE C 2 SER C 10 -1 O TYR C 5 N LEU C 99
SHEET 3 CC 4 PHE C 54 THR C 63 -1 O LEU C 55 N SER C 10
SHEET 4 CC 4 ILE C 32 ILE C 37 -1 O SER C 33 N GLN C 62
SHEET 1 CD 2 ILE C 106 LEU C 108 0
SHEET 2 CD 2 LEU C 111 VAL C 113 -1 O LEU C 111 N LEU C 108
SHEET 1 CE 2 VAL C 136 GLU C 137 0
SHEET 2 CE 2 LEU C 142 LYS C 143 -1 O LEU C 142 N GLU C 137
SHEET 1 DA 2 ILE D 32 ILE D 37 0
SHEET 2 DA 2 PHE D 54 THR D 63 -1 O GLU D 60 N SER D 35
SHEET 1 DB 5 ASP D 95 TYR D 101 0
SHEET 2 DB 5 ILE D 2 SER D 10 -1 O TYR D 5 N LEU D 99
SHEET 3 DB 5 PHE D 54 THR D 63 -1 O LEU D 55 N SER D 10
SHEET 4 DB 5 TYR D 41 THR D 43 -1 O TYR D 41 N ASN D 56
SHEET 5 DB 5 VAL D 154 ARG D 156 -1 O LYS D 155 N GLU D 42
SHEET 1 DC 4 ASP D 95 TYR D 101 0
SHEET 2 DC 4 ILE D 2 SER D 10 -1 O TYR D 5 N LEU D 99
SHEET 3 DC 4 PHE D 54 THR D 63 -1 O LEU D 55 N SER D 10
SHEET 4 DC 4 ILE D 32 ILE D 37 -1 O SER D 33 N GLN D 62
SHEET 1 DD 2 ILE D 106 LEU D 108 0
SHEET 2 DD 2 LEU D 111 VAL D 113 -1 O LEU D 111 N LEU D 108
SHEET 1 DE 2 VAL D 136 GLU D 137 0
SHEET 2 DE 2 LEU D 142 LYS D 143 -1 O LEU D 142 N GLU D 137
SSBOND 1 CYS B 80 CYS D 80 1555 2746 1.96
LINK OD1 ASP A 95 MG MG A 170 1555 1555 2.45
LINK OD2 ASP A 95 MG MG A 171 1555 1555 2.05
LINK OD1 ASP A 97 MG MG A 170 1555 1555 2.01
LINK OD2 ASP A 97 MG MG A 171 1555 1555 2.38
LINK MG MG A 170 O1A APC A1158 1555 1555 2.00
LINK MG MG A 170 O1B APC A1158 1555 1555 2.15
LINK MG MG A 170 O HOH A2002 1555 1555 2.32
LINK MG MG A 171 O1B APC A1158 1555 1555 2.45
LINK MG MG A 171 O1G APC A1158 1555 1555 2.06
LINK OE2 GLU B 78 MG MG B 170 1555 1555 2.82
LINK OD1 ASP B 95 MG MG B 170 1555 1555 2.19
LINK OD2 ASP B 95 MG MG B 171 1555 1555 2.05
LINK OD1 ASP B 97 MG MG B 170 1555 1555 2.42
LINK OD2 ASP B 97 MG MG B 171 1555 1555 2.43
LINK MG MG B 170 O1AAAPC B1159 1555 1555 2.30
LINK MG MG B 170 O1ABAPC B1159 1555 1555 2.60
LINK MG MG B 170 O HOH B2001 1555 1555 2.07
LINK MG MG B 171 O1BAAPC B1159 1555 1555 2.81
LINK MG MG B 171 O2BAAPC B1159 1555 1555 2.64
LINK MG MG B 171 O1BBAPC B1159 1555 1555 2.47
LINK MG MG B 171 O1GBAPC B1159 1555 1555 1.86
LINK OD1 ASP C 95 MG MG C 170 1555 1555 2.23
LINK OD2 ASP C 95 MG MG C 171 1555 1555 2.02
LINK OD1 ASP C 97 MG MG C 170 1555 1555 2.14
LINK OD2 ASP C 97 MG MG C 171 1555 1555 2.26
LINK MG MG C 170 O1B APC C1158 1555 1555 2.16
LINK MG MG C 170 O1A APC C1158 1555 1555 1.93
LINK MG MG C 170 O HOH C2001 1555 1555 2.15
LINK MG MG C 170 O HOH C2002 1555 1555 2.10
LINK MG MG C 171 O1G APC C1158 1555 1555 2.01
LINK MG MG C 171 O1B APC C1158 1555 1555 2.54
LINK OD1 ASP D 95 MG MG D 170 1555 1555 2.49
LINK OD2 ASP D 95 MG MG D 171 1555 1555 2.10
LINK OD1 ASP D 97 MG MG D 170 1555 1555 1.97
LINK OD2 ASP D 97 MG MG D 171 1555 1555 2.27
LINK MG MG D 170 O1BBAPC D1158 1555 1555 2.21
LINK MG MG D 170 O1ABAPC D1158 1555 1555 2.07
LINK MG MG D 170 O2BAAPC D1158 1555 1555 2.44
LINK MG MG D 170 O1AAAPC D1158 1555 1555 1.88
LINK MG MG D 170 O HOH D2002 1555 1555 2.06
LINK MG MG D 171 O1GBAPC D1158 1555 1555 1.84
LINK MG MG D 171 O1BBAPC D1158 1555 1555 2.42
LINK MG MG D 171 O2BAAPC D1158 1555 1555 2.39
LINK MG MG D 171 O1BAAPC D1158 1555 1555 2.85
CISPEP 1 VAL A 113 PRO A 114 0 -0.48
CISPEP 2 VAL B 113 PRO B 114 0 -1.87
CISPEP 3 VAL C 113 PRO C 114 0 -1.08
CISPEP 4 VAL D 113 PRO D 114 0 -1.86
SITE 1 AC1 4 ASP A 95 ASP A 97 APC A1158 HOH A2002
SITE 1 AC2 3 ASP A 95 ASP A 97 APC A1158
SITE 1 AC3 6 GLU B 78 ASP B 95 VAL B 96 ASP B 97
SITE 2 AC3 6 APC B1159 HOH B2001
SITE 1 AC4 3 ASP B 95 ASP B 97 APC B1159
SITE 1 AC5 5 ASP C 95 ASP C 97 APC C1158 HOH C2001
SITE 2 AC5 5 HOH C2002
SITE 1 AC6 3 ASP C 95 ASP C 97 APC C1158
SITE 1 AC7 4 ASP D 95 ASP D 97 APC D1158 HOH D2002
SITE 1 AC8 3 ASP D 95 ASP D 97 APC D1158
SITE 1 AC9 14 ARG A 92 ASP A 95 ASP A 97 ILE A 98
SITE 2 AC9 14 LYS A 110 LEU A 111 SER A 112 HIS A 115
SITE 3 AC9 14 ARG A 117 ARG A 121 MG A 170 MG A 171
SITE 4 AC9 14 HOH A2002 HOH A2005
SITE 1 BC1 11 GLN A 3 ARG B 92 ASP B 95 ASP B 97
SITE 2 BC1 11 ILE B 98 LYS B 110 LEU B 111 SER B 112
SITE 3 BC1 11 MG B 170 MG B 171 HOH B2001
SITE 1 BC2 14 LEU C 71 ARG C 92 ASP C 95 ASP C 97
SITE 2 BC2 14 ILE C 98 LYS C 110 LEU C 111 SER C 112
SITE 3 BC2 14 HIS C 115 ARG C 117 ARG C 121 MG C 170
SITE 4 BC2 14 MG C 171 HOH C2002
SITE 1 BC3 11 GLN C 3 LEU D 71 ARG D 92 ASP D 95
SITE 2 BC3 11 ASP D 97 ILE D 98 LYS D 110 LEU D 111
SITE 3 BC3 11 SER D 112 MG D 170 MG D 171
SITE 1 BC4 4 ASN B 27 GLU B 28 TYR B 29 ASP B 30
SITE 1 BC5 5 ASN A 27 GLU A 28 TYR A 29 ASP A 30
SITE 2 BC5 5 ILE A 32
CRYST1 62.002 94.263 62.989 90.00 112.44 90.00 P 1 21 1 6
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 0.016129 0.000000 0.006661 0.00000
SCALE2 0.000000 0.010609 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017176 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
