HEADER CHAPERONE 07-JUN-17 5XR2
TITLE SAV0551
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN/NUCLEIC ACID DEGLYCASE HCHA;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H;
COMPND 4 SYNONYM: MAILLARD DEGLYCASE,PROTEIN DEGLYCASE HCHA;
COMPND 5 EC: 3.1.2.-,3.5.1.124;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS (STRAIN MU50 / ATCC
SOURCE 3 700699);
SOURCE 4 ORGANISM_TAXID: 158878;
SOURCE 5 STRAIN: MU50 / ATCC 700699;
SOURCE 6 GENE: HCHA, SAV0551;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HSP31, CHAPERONE, GLYOXALASE III
EXPDTA X-RAY DIFFRACTION
AUTHOR H.J.KIM,A.R.KWON,B.J.LEE
REVDAT 5 22-NOV-23 5XR2 1 REMARK
REVDAT 4 15-NOV-23 5XR2 1 LINK ATOM
REVDAT 3 18-APR-18 5XR2 1 JRNL
REVDAT 2 29-NOV-17 5XR2 1 JRNL
REVDAT 1 01-NOV-17 5XR2 0
JRNL AUTH H.J.KIM,K.Y.LEE,A.R.KWON,B.J.LEE
JRNL TITL STRUCTURAL AND FUNCTIONAL STUDIES OF SAV0551
JRNL TITL 2 FROMSTAPHYLOCOCCUS AUREUSAS A CHAPERONE AND GLYOXALASE III.
JRNL REF BIOSCI. REP. V. 37 2017
JRNL REFN ISSN 1573-4935
JRNL PMID 29046369
JRNL DOI 10.1042/BSR20171106
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0158
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) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.65
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 68531
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) : 0.185
REMARK 3 R VALUE (WORKING SET) : 0.181
REMARK 3 FREE R VALUE : 0.254
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3580
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) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.67
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4667
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.43
REMARK 3 BIN R VALUE (WORKING SET) : 0.2200
REMARK 3 BIN FREE R VALUE SET COUNT : 232
REMARK 3 BIN FREE R VALUE : 0.3150
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 17891
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 13
REMARK 3 SOLVENT ATOMS : 280
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.74
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.04000
REMARK 3 B22 (A**2) : 0.01000
REMARK 3 B33 (A**2) : 0.02000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
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): 0.348
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.249
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.742
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.954
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.908
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 18289 ; 0.013 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 17109 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 24817 ; 1.629 ; 1.985
REMARK 3 BOND ANGLES OTHERS (DEGREES): 39984 ; 1.011 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2298 ; 7.134 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 785 ;39.402 ;25.873
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 3202 ;16.233 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 48 ;18.147 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2785 ; 0.086 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 20210 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 3274 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 9216 ; 2.625 ; 3.952
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 9215 ; 2.624 ; 3.952
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 11506 ; 4.070 ; 5.921
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 11507 ; 4.071 ; 5.921
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 9073 ; 3.001 ; 4.314
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 9074 ; 3.000 ; 4.314
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 13312 ; 4.835 ; 6.317
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 19403 ; 6.602 ;46.093
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 19378 ; 6.600 ;46.096
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 : 1.20
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 5XR2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-JUN-17.
REMARK 100 THE DEPOSITION ID IS D_1300003964.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-APR-15
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 : PAL/PLS
REMARK 200 BEAMLINE : 5C (4A)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 72192
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 6.500
REMARK 200 R MERGE (I) : 0.11600
REMARK 200 R SYM (I) : 0.10700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 32.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.64
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.4
REMARK 200 DATA REDUNDANCY IN SHELL : 3.20
REMARK 200 R MERGE FOR SHELL (I) : 0.47500
REMARK 200 R SYM FOR SHELL (I) : 0.43700
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP 11.4.06
REMARK 200 STARTING MODEL: 4I4N
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.51
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 23% (W/V) PEG 3350, 100MM BISTRIS, PH
REMARK 280 6.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 297K
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 48.14200
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 93.92650
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 64.72700
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 93.92650
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 48.14200
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 64.72700
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2240 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22880 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2270 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23190 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2210 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22420 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2350 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24240 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H
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 SER A 2
REMARK 465 GLN A 3
REMARK 465 ASP A 4
REMARK 465 VAL A 5
REMARK 465 ASN A 6
REMARK 465 GLU A 294
REMARK 465 HIS A 295
REMARK 465 HIS A 296
REMARK 465 HIS A 297
REMARK 465 HIS A 298
REMARK 465 HIS A 299
REMARK 465 HIS A 300
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 GLN B 3
REMARK 465 ASP B 4
REMARK 465 ASN B 291
REMARK 465 LYS B 292
REMARK 465 LEU B 293
REMARK 465 GLU B 294
REMARK 465 HIS B 295
REMARK 465 HIS B 296
REMARK 465 HIS B 297
REMARK 465 HIS B 298
REMARK 465 HIS B 299
REMARK 465 HIS B 300
REMARK 465 MET C 1
REMARK 465 SER C 2
REMARK 465 GLN C 3
REMARK 465 ASP C 4
REMARK 465 VAL C 5
REMARK 465 MET D 1
REMARK 465 SER D 2
REMARK 465 GLN D 3
REMARK 465 ASP D 4
REMARK 465 VAL D 5
REMARK 465 GLN D 290
REMARK 465 ASN D 291
REMARK 465 LYS D 292
REMARK 465 LEU D 293
REMARK 465 GLU D 294
REMARK 465 HIS D 295
REMARK 465 HIS D 296
REMARK 465 HIS D 297
REMARK 465 HIS D 298
REMARK 465 HIS D 299
REMARK 465 HIS D 300
REMARK 465 MET E 1
REMARK 465 SER E 2
REMARK 465 GLN E 3
REMARK 465 ASP E 4
REMARK 465 VAL E 5
REMARK 465 LEU E 293
REMARK 465 GLU E 294
REMARK 465 HIS E 295
REMARK 465 HIS E 296
REMARK 465 HIS E 297
REMARK 465 HIS E 298
REMARK 465 HIS E 299
REMARK 465 HIS E 300
REMARK 465 MET F 1
REMARK 465 SER F 2
REMARK 465 GLN F 3
REMARK 465 ASP F 4
REMARK 465 VAL F 5
REMARK 465 ASN F 6
REMARK 465 GLU F 7
REMARK 465 ASN F 291
REMARK 465 LYS F 292
REMARK 465 LEU F 293
REMARK 465 GLU F 294
REMARK 465 HIS F 295
REMARK 465 HIS F 296
REMARK 465 HIS F 297
REMARK 465 HIS F 298
REMARK 465 HIS F 299
REMARK 465 HIS F 300
REMARK 465 MET G 1
REMARK 465 SER G 2
REMARK 465 GLN G 3
REMARK 465 ASP G 4
REMARK 465 VAL G 5
REMARK 465 MET H 1
REMARK 465 SER H 2
REMARK 465 LYS H 292
REMARK 465 LEU H 293
REMARK 465 GLU H 294
REMARK 465 HIS H 295
REMARK 465 HIS H 296
REMARK 465 HIS H 297
REMARK 465 HIS H 298
REMARK 465 HIS H 299
REMARK 465 HIS H 300
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 CYS D 190 CA - CB - SG ANGL. DEV. = 8.3 DEGREES
REMARK 500 CYS E 190 CA - CB - SG ANGL. DEV. = 8.3 DEGREES
REMARK 500 CYS F 190 CA - CB - SG ANGL. DEV. = 8.0 DEGREES
REMARK 500 CYS H 190 CA - CB - SG ANGL. DEV. = 8.3 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP A 40 36.24 -140.94
REMARK 500 HIS A 44 50.35 -145.11
REMARK 500 THR A 75 -122.77 -131.09
REMARK 500 LEU A 145 -136.34 -99.64
REMARK 500 GLU A 168 52.13 -146.16
REMARK 500 CYS A 190 -136.02 63.39
REMARK 500 ARG A 263 -118.95 49.91
REMARK 500 SER A 270 176.74 179.36
REMARK 500 LYS A 292 32.00 -91.61
REMARK 500 LYS B 45 100.14 -44.26
REMARK 500 THR B 75 -135.74 -119.42
REMARK 500 LEU B 145 -132.39 -101.72
REMARK 500 GLU B 168 47.71 -154.56
REMARK 500 CYS B 190 -123.62 69.31
REMARK 500 GLU B 209 123.46 -35.26
REMARK 500 ARG B 263 -123.23 51.53
REMARK 500 GLU C 7 7.43 -64.67
REMARK 500 ASP C 40 47.09 -147.28
REMARK 500 HIS C 44 45.55 -149.13
REMARK 500 THR C 75 -125.89 -126.81
REMARK 500 THR C 115 -39.62 -38.31
REMARK 500 LEU C 145 -129.03 -98.04
REMARK 500 GLU C 168 53.04 -142.96
REMARK 500 CYS C 190 -119.73 56.31
REMARK 500 ARG C 263 -122.67 52.80
REMARK 500 HIS C 297 -92.38 -106.01
REMARK 500 GLU D 7 46.10 -84.57
REMARK 500 ASP D 38 25.76 -75.55
REMARK 500 HIS D 44 45.76 -103.84
REMARK 500 THR D 75 -133.29 -129.32
REMARK 500 LEU D 145 -135.81 -90.61
REMARK 500 GLU D 168 47.71 -146.01
REMARK 500 CYS D 190 -111.81 72.16
REMARK 500 ASP D 253 17.59 -141.76
REMARK 500 THR D 259 -168.05 -110.09
REMARK 500 LEU D 260 122.85 176.06
REMARK 500 ARG D 263 -119.11 55.61
REMARK 500 SER D 270 -178.31 -178.89
REMARK 500 ALA D 288 21.77 -67.48
REMARK 500 HIS E 44 44.72 -142.92
REMARK 500 LYS E 52 -63.84 -104.22
REMARK 500 THR E 75 -134.10 -133.05
REMARK 500 LEU E 145 -136.68 -103.85
REMARK 500 GLU E 168 48.47 -155.82
REMARK 500 CYS E 190 -108.60 72.72
REMARK 500 ARG E 263 -117.85 49.55
REMARK 500 SER E 270 174.21 178.94
REMARK 500 ASP F 40 78.28 -156.10
REMARK 500 THR F 75 -136.91 -133.47
REMARK 500 PRO F 114 94.26 -66.84
REMARK 500
REMARK 500 THIS ENTRY HAS 71 RAMACHANDRAN OUTLIERS.
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 ZN C 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 295 NE2
REMARK 620 2 HIS G 296 NE2 90.2
REMARK 620 3 HIS G 298 NE2 91.8 1.9
REMARK 620 4 HIS G 300 NE2 91.7 1.7 1.7
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LAC A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LAC E 401
DBREF 5XR2 A 1 292 UNP P64312 HCHA_STAAM 1 292
DBREF 5XR2 B 1 292 UNP P64312 HCHA_STAAM 1 292
DBREF 5XR2 C 1 292 UNP P64312 HCHA_STAAM 1 292
DBREF 5XR2 D 1 292 UNP P64312 HCHA_STAAM 1 292
DBREF 5XR2 E 1 292 UNP P64312 HCHA_STAAM 1 292
DBREF 5XR2 F 1 292 UNP P64312 HCHA_STAAM 1 292
DBREF 5XR2 G 1 292 UNP P64312 HCHA_STAAM 1 292
DBREF 5XR2 H 1 292 UNP P64312 HCHA_STAAM 1 292
SEQADV 5XR2 LEU A 293 UNP P64312 EXPRESSION TAG
SEQADV 5XR2 GLU A 294 UNP P64312 EXPRESSION TAG
SEQADV 5XR2 HIS A 295 UNP P64312 EXPRESSION TAG
SEQADV 5XR2 HIS A 296 UNP P64312 EXPRESSION TAG
SEQADV 5XR2 HIS A 297 UNP P64312 EXPRESSION TAG
SEQADV 5XR2 HIS A 298 UNP P64312 EXPRESSION TAG
SEQADV 5XR2 HIS A 299 UNP P64312 EXPRESSION TAG
SEQADV 5XR2 HIS A 300 UNP P64312 EXPRESSION TAG
SEQADV 5XR2 LEU B 293 UNP P64312 EXPRESSION TAG
SEQADV 5XR2 GLU B 294 UNP P64312 EXPRESSION TAG
SEQADV 5XR2 HIS B 295 UNP P64312 EXPRESSION TAG
SEQADV 5XR2 HIS B 296 UNP P64312 EXPRESSION TAG
SEQADV 5XR2 HIS B 297 UNP P64312 EXPRESSION TAG
SEQADV 5XR2 HIS B 298 UNP P64312 EXPRESSION TAG
SEQADV 5XR2 HIS B 299 UNP P64312 EXPRESSION TAG
SEQADV 5XR2 HIS B 300 UNP P64312 EXPRESSION TAG
SEQADV 5XR2 LEU C 293 UNP P64312 EXPRESSION TAG
SEQADV 5XR2 GLU C 294 UNP P64312 EXPRESSION TAG
SEQADV 5XR2 HIS C 295 UNP P64312 EXPRESSION TAG
SEQADV 5XR2 HIS C 296 UNP P64312 EXPRESSION TAG
SEQADV 5XR2 HIS C 297 UNP P64312 EXPRESSION TAG
SEQADV 5XR2 HIS C 298 UNP P64312 EXPRESSION TAG
SEQADV 5XR2 HIS C 299 UNP P64312 EXPRESSION TAG
SEQADV 5XR2 HIS C 300 UNP P64312 EXPRESSION TAG
SEQADV 5XR2 LEU D 293 UNP P64312 EXPRESSION TAG
SEQADV 5XR2 GLU D 294 UNP P64312 EXPRESSION TAG
SEQADV 5XR2 HIS D 295 UNP P64312 EXPRESSION TAG
SEQADV 5XR2 HIS D 296 UNP P64312 EXPRESSION TAG
SEQADV 5XR2 HIS D 297 UNP P64312 EXPRESSION TAG
SEQADV 5XR2 HIS D 298 UNP P64312 EXPRESSION TAG
SEQADV 5XR2 HIS D 299 UNP P64312 EXPRESSION TAG
SEQADV 5XR2 HIS D 300 UNP P64312 EXPRESSION TAG
SEQADV 5XR2 LEU E 293 UNP P64312 EXPRESSION TAG
SEQADV 5XR2 GLU E 294 UNP P64312 EXPRESSION TAG
SEQADV 5XR2 HIS E 295 UNP P64312 EXPRESSION TAG
SEQADV 5XR2 HIS E 296 UNP P64312 EXPRESSION TAG
SEQADV 5XR2 HIS E 297 UNP P64312 EXPRESSION TAG
SEQADV 5XR2 HIS E 298 UNP P64312 EXPRESSION TAG
SEQADV 5XR2 HIS E 299 UNP P64312 EXPRESSION TAG
SEQADV 5XR2 HIS E 300 UNP P64312 EXPRESSION TAG
SEQADV 5XR2 LEU F 293 UNP P64312 EXPRESSION TAG
SEQADV 5XR2 GLU F 294 UNP P64312 EXPRESSION TAG
SEQADV 5XR2 HIS F 295 UNP P64312 EXPRESSION TAG
SEQADV 5XR2 HIS F 296 UNP P64312 EXPRESSION TAG
SEQADV 5XR2 HIS F 297 UNP P64312 EXPRESSION TAG
SEQADV 5XR2 HIS F 298 UNP P64312 EXPRESSION TAG
SEQADV 5XR2 HIS F 299 UNP P64312 EXPRESSION TAG
SEQADV 5XR2 HIS F 300 UNP P64312 EXPRESSION TAG
SEQADV 5XR2 LEU G 293 UNP P64312 EXPRESSION TAG
SEQADV 5XR2 GLU G 294 UNP P64312 EXPRESSION TAG
SEQADV 5XR2 HIS G 295 UNP P64312 EXPRESSION TAG
SEQADV 5XR2 HIS G 296 UNP P64312 EXPRESSION TAG
SEQADV 5XR2 HIS G 297 UNP P64312 EXPRESSION TAG
SEQADV 5XR2 HIS G 298 UNP P64312 EXPRESSION TAG
SEQADV 5XR2 HIS G 299 UNP P64312 EXPRESSION TAG
SEQADV 5XR2 HIS G 300 UNP P64312 EXPRESSION TAG
SEQADV 5XR2 LEU H 293 UNP P64312 EXPRESSION TAG
SEQADV 5XR2 GLU H 294 UNP P64312 EXPRESSION TAG
SEQADV 5XR2 HIS H 295 UNP P64312 EXPRESSION TAG
SEQADV 5XR2 HIS H 296 UNP P64312 EXPRESSION TAG
SEQADV 5XR2 HIS H 297 UNP P64312 EXPRESSION TAG
SEQADV 5XR2 HIS H 298 UNP P64312 EXPRESSION TAG
SEQADV 5XR2 HIS H 299 UNP P64312 EXPRESSION TAG
SEQADV 5XR2 HIS H 300 UNP P64312 EXPRESSION TAG
SEQRES 1 A 300 MET SER GLN ASP VAL ASN GLU LEU SER LYS GLN PRO THR
SEQRES 2 A 300 PRO ASP LYS ALA GLU ASP ASN ALA PHE PHE PRO SER PRO
SEQRES 3 A 300 TYR SER LEU SER GLN TYR THR ALA PRO LYS THR ASP PHE
SEQRES 4 A 300 ASP GLY VAL GLU HIS LYS GLY ALA TYR LYS ASP GLY LYS
SEQRES 5 A 300 TRP LYS VAL LEU MET ILE ALA ALA GLU GLU ARG TYR VAL
SEQRES 6 A 300 LEU LEU GLU ASN GLY LYS MET PHE SER THR GLY ASN HIS
SEQRES 7 A 300 PRO VAL GLU MET LEU LEU PRO LEU HIS HIS LEU MET GLU
SEQRES 8 A 300 ALA GLY PHE ASP VAL ASP VAL ALA THR LEU SER GLY TYR
SEQRES 9 A 300 PRO VAL LYS LEU GLU LEU TRP ALA MET PRO THR GLU ASP
SEQRES 10 A 300 GLU ALA VAL ILE SER THR TYR ASN LYS LEU LYS GLU LYS
SEQRES 11 A 300 LEU LYS GLN PRO LYS LYS LEU ALA ASP VAL ILE LYS ASN
SEQRES 12 A 300 GLU LEU GLY PRO ASP SER ASP TYR LEU SER VAL PHE ILE
SEQRES 13 A 300 PRO GLY GLY HIS ALA ALA VAL VAL GLY ILE SER GLU SER
SEQRES 14 A 300 GLU ASP VAL GLN GLN THR LEU ASP TRP ALA LEU ASP ASN
SEQRES 15 A 300 ASP ARG PHE ILE VAL THR LEU CYS HIS GLY PRO ALA ALA
SEQRES 16 A 300 LEU LEU SER ALA GLY LEU ASN ARG GLU LYS SER PRO LEU
SEQRES 17 A 300 GLU GLY TYR SER VAL CYS VAL PHE PRO ASP SER LEU ASP
SEQRES 18 A 300 GLU GLY ALA ASN ILE GLU ILE GLY TYR LEU PRO GLY ARG
SEQRES 19 A 300 LEU LYS TRP LEU VAL ALA ASP LEU LEU THR LYS GLN GLY
SEQRES 20 A 300 LEU LYS VAL VAL ASN ASP ASP MET THR GLY ARG THR LEU
SEQRES 21 A 300 LYS ASP ARG LYS LEU LEU THR GLY ASP SER PRO LEU ALA
SEQRES 22 A 300 SER ASN GLU LEU GLY LYS LEU ALA VAL ASN GLU MET LEU
SEQRES 23 A 300 ASN ALA ILE GLN ASN LYS LEU GLU HIS HIS HIS HIS HIS
SEQRES 24 A 300 HIS
SEQRES 1 B 300 MET SER GLN ASP VAL ASN GLU LEU SER LYS GLN PRO THR
SEQRES 2 B 300 PRO ASP LYS ALA GLU ASP ASN ALA PHE PHE PRO SER PRO
SEQRES 3 B 300 TYR SER LEU SER GLN TYR THR ALA PRO LYS THR ASP PHE
SEQRES 4 B 300 ASP GLY VAL GLU HIS LYS GLY ALA TYR LYS ASP GLY LYS
SEQRES 5 B 300 TRP LYS VAL LEU MET ILE ALA ALA GLU GLU ARG TYR VAL
SEQRES 6 B 300 LEU LEU GLU ASN GLY LYS MET PHE SER THR GLY ASN HIS
SEQRES 7 B 300 PRO VAL GLU MET LEU LEU PRO LEU HIS HIS LEU MET GLU
SEQRES 8 B 300 ALA GLY PHE ASP VAL ASP VAL ALA THR LEU SER GLY TYR
SEQRES 9 B 300 PRO VAL LYS LEU GLU LEU TRP ALA MET PRO THR GLU ASP
SEQRES 10 B 300 GLU ALA VAL ILE SER THR TYR ASN LYS LEU LYS GLU LYS
SEQRES 11 B 300 LEU LYS GLN PRO LYS LYS LEU ALA ASP VAL ILE LYS ASN
SEQRES 12 B 300 GLU LEU GLY PRO ASP SER ASP TYR LEU SER VAL PHE ILE
SEQRES 13 B 300 PRO GLY GLY HIS ALA ALA VAL VAL GLY ILE SER GLU SER
SEQRES 14 B 300 GLU ASP VAL GLN GLN THR LEU ASP TRP ALA LEU ASP ASN
SEQRES 15 B 300 ASP ARG PHE ILE VAL THR LEU CYS HIS GLY PRO ALA ALA
SEQRES 16 B 300 LEU LEU SER ALA GLY LEU ASN ARG GLU LYS SER PRO LEU
SEQRES 17 B 300 GLU GLY TYR SER VAL CYS VAL PHE PRO ASP SER LEU ASP
SEQRES 18 B 300 GLU GLY ALA ASN ILE GLU ILE GLY TYR LEU PRO GLY ARG
SEQRES 19 B 300 LEU LYS TRP LEU VAL ALA ASP LEU LEU THR LYS GLN GLY
SEQRES 20 B 300 LEU LYS VAL VAL ASN ASP ASP MET THR GLY ARG THR LEU
SEQRES 21 B 300 LYS ASP ARG LYS LEU LEU THR GLY ASP SER PRO LEU ALA
SEQRES 22 B 300 SER ASN GLU LEU GLY LYS LEU ALA VAL ASN GLU MET LEU
SEQRES 23 B 300 ASN ALA ILE GLN ASN LYS LEU GLU HIS HIS HIS HIS HIS
SEQRES 24 B 300 HIS
SEQRES 1 C 300 MET SER GLN ASP VAL ASN GLU LEU SER LYS GLN PRO THR
SEQRES 2 C 300 PRO ASP LYS ALA GLU ASP ASN ALA PHE PHE PRO SER PRO
SEQRES 3 C 300 TYR SER LEU SER GLN TYR THR ALA PRO LYS THR ASP PHE
SEQRES 4 C 300 ASP GLY VAL GLU HIS LYS GLY ALA TYR LYS ASP GLY LYS
SEQRES 5 C 300 TRP LYS VAL LEU MET ILE ALA ALA GLU GLU ARG TYR VAL
SEQRES 6 C 300 LEU LEU GLU ASN GLY LYS MET PHE SER THR GLY ASN HIS
SEQRES 7 C 300 PRO VAL GLU MET LEU LEU PRO LEU HIS HIS LEU MET GLU
SEQRES 8 C 300 ALA GLY PHE ASP VAL ASP VAL ALA THR LEU SER GLY TYR
SEQRES 9 C 300 PRO VAL LYS LEU GLU LEU TRP ALA MET PRO THR GLU ASP
SEQRES 10 C 300 GLU ALA VAL ILE SER THR TYR ASN LYS LEU LYS GLU LYS
SEQRES 11 C 300 LEU LYS GLN PRO LYS LYS LEU ALA ASP VAL ILE LYS ASN
SEQRES 12 C 300 GLU LEU GLY PRO ASP SER ASP TYR LEU SER VAL PHE ILE
SEQRES 13 C 300 PRO GLY GLY HIS ALA ALA VAL VAL GLY ILE SER GLU SER
SEQRES 14 C 300 GLU ASP VAL GLN GLN THR LEU ASP TRP ALA LEU ASP ASN
SEQRES 15 C 300 ASP ARG PHE ILE VAL THR LEU CYS HIS GLY PRO ALA ALA
SEQRES 16 C 300 LEU LEU SER ALA GLY LEU ASN ARG GLU LYS SER PRO LEU
SEQRES 17 C 300 GLU GLY TYR SER VAL CYS VAL PHE PRO ASP SER LEU ASP
SEQRES 18 C 300 GLU GLY ALA ASN ILE GLU ILE GLY TYR LEU PRO GLY ARG
SEQRES 19 C 300 LEU LYS TRP LEU VAL ALA ASP LEU LEU THR LYS GLN GLY
SEQRES 20 C 300 LEU LYS VAL VAL ASN ASP ASP MET THR GLY ARG THR LEU
SEQRES 21 C 300 LYS ASP ARG LYS LEU LEU THR GLY ASP SER PRO LEU ALA
SEQRES 22 C 300 SER ASN GLU LEU GLY LYS LEU ALA VAL ASN GLU MET LEU
SEQRES 23 C 300 ASN ALA ILE GLN ASN LYS LEU GLU HIS HIS HIS HIS HIS
SEQRES 24 C 300 HIS
SEQRES 1 D 300 MET SER GLN ASP VAL ASN GLU LEU SER LYS GLN PRO THR
SEQRES 2 D 300 PRO ASP LYS ALA GLU ASP ASN ALA PHE PHE PRO SER PRO
SEQRES 3 D 300 TYR SER LEU SER GLN TYR THR ALA PRO LYS THR ASP PHE
SEQRES 4 D 300 ASP GLY VAL GLU HIS LYS GLY ALA TYR LYS ASP GLY LYS
SEQRES 5 D 300 TRP LYS VAL LEU MET ILE ALA ALA GLU GLU ARG TYR VAL
SEQRES 6 D 300 LEU LEU GLU ASN GLY LYS MET PHE SER THR GLY ASN HIS
SEQRES 7 D 300 PRO VAL GLU MET LEU LEU PRO LEU HIS HIS LEU MET GLU
SEQRES 8 D 300 ALA GLY PHE ASP VAL ASP VAL ALA THR LEU SER GLY TYR
SEQRES 9 D 300 PRO VAL LYS LEU GLU LEU TRP ALA MET PRO THR GLU ASP
SEQRES 10 D 300 GLU ALA VAL ILE SER THR TYR ASN LYS LEU LYS GLU LYS
SEQRES 11 D 300 LEU LYS GLN PRO LYS LYS LEU ALA ASP VAL ILE LYS ASN
SEQRES 12 D 300 GLU LEU GLY PRO ASP SER ASP TYR LEU SER VAL PHE ILE
SEQRES 13 D 300 PRO GLY GLY HIS ALA ALA VAL VAL GLY ILE SER GLU SER
SEQRES 14 D 300 GLU ASP VAL GLN GLN THR LEU ASP TRP ALA LEU ASP ASN
SEQRES 15 D 300 ASP ARG PHE ILE VAL THR LEU CYS HIS GLY PRO ALA ALA
SEQRES 16 D 300 LEU LEU SER ALA GLY LEU ASN ARG GLU LYS SER PRO LEU
SEQRES 17 D 300 GLU GLY TYR SER VAL CYS VAL PHE PRO ASP SER LEU ASP
SEQRES 18 D 300 GLU GLY ALA ASN ILE GLU ILE GLY TYR LEU PRO GLY ARG
SEQRES 19 D 300 LEU LYS TRP LEU VAL ALA ASP LEU LEU THR LYS GLN GLY
SEQRES 20 D 300 LEU LYS VAL VAL ASN ASP ASP MET THR GLY ARG THR LEU
SEQRES 21 D 300 LYS ASP ARG LYS LEU LEU THR GLY ASP SER PRO LEU ALA
SEQRES 22 D 300 SER ASN GLU LEU GLY LYS LEU ALA VAL ASN GLU MET LEU
SEQRES 23 D 300 ASN ALA ILE GLN ASN LYS LEU GLU HIS HIS HIS HIS HIS
SEQRES 24 D 300 HIS
SEQRES 1 E 300 MET SER GLN ASP VAL ASN GLU LEU SER LYS GLN PRO THR
SEQRES 2 E 300 PRO ASP LYS ALA GLU ASP ASN ALA PHE PHE PRO SER PRO
SEQRES 3 E 300 TYR SER LEU SER GLN TYR THR ALA PRO LYS THR ASP PHE
SEQRES 4 E 300 ASP GLY VAL GLU HIS LYS GLY ALA TYR LYS ASP GLY LYS
SEQRES 5 E 300 TRP LYS VAL LEU MET ILE ALA ALA GLU GLU ARG TYR VAL
SEQRES 6 E 300 LEU LEU GLU ASN GLY LYS MET PHE SER THR GLY ASN HIS
SEQRES 7 E 300 PRO VAL GLU MET LEU LEU PRO LEU HIS HIS LEU MET GLU
SEQRES 8 E 300 ALA GLY PHE ASP VAL ASP VAL ALA THR LEU SER GLY TYR
SEQRES 9 E 300 PRO VAL LYS LEU GLU LEU TRP ALA MET PRO THR GLU ASP
SEQRES 10 E 300 GLU ALA VAL ILE SER THR TYR ASN LYS LEU LYS GLU LYS
SEQRES 11 E 300 LEU LYS GLN PRO LYS LYS LEU ALA ASP VAL ILE LYS ASN
SEQRES 12 E 300 GLU LEU GLY PRO ASP SER ASP TYR LEU SER VAL PHE ILE
SEQRES 13 E 300 PRO GLY GLY HIS ALA ALA VAL VAL GLY ILE SER GLU SER
SEQRES 14 E 300 GLU ASP VAL GLN GLN THR LEU ASP TRP ALA LEU ASP ASN
SEQRES 15 E 300 ASP ARG PHE ILE VAL THR LEU CYS HIS GLY PRO ALA ALA
SEQRES 16 E 300 LEU LEU SER ALA GLY LEU ASN ARG GLU LYS SER PRO LEU
SEQRES 17 E 300 GLU GLY TYR SER VAL CYS VAL PHE PRO ASP SER LEU ASP
SEQRES 18 E 300 GLU GLY ALA ASN ILE GLU ILE GLY TYR LEU PRO GLY ARG
SEQRES 19 E 300 LEU LYS TRP LEU VAL ALA ASP LEU LEU THR LYS GLN GLY
SEQRES 20 E 300 LEU LYS VAL VAL ASN ASP ASP MET THR GLY ARG THR LEU
SEQRES 21 E 300 LYS ASP ARG LYS LEU LEU THR GLY ASP SER PRO LEU ALA
SEQRES 22 E 300 SER ASN GLU LEU GLY LYS LEU ALA VAL ASN GLU MET LEU
SEQRES 23 E 300 ASN ALA ILE GLN ASN LYS LEU GLU HIS HIS HIS HIS HIS
SEQRES 24 E 300 HIS
SEQRES 1 F 300 MET SER GLN ASP VAL ASN GLU LEU SER LYS GLN PRO THR
SEQRES 2 F 300 PRO ASP LYS ALA GLU ASP ASN ALA PHE PHE PRO SER PRO
SEQRES 3 F 300 TYR SER LEU SER GLN TYR THR ALA PRO LYS THR ASP PHE
SEQRES 4 F 300 ASP GLY VAL GLU HIS LYS GLY ALA TYR LYS ASP GLY LYS
SEQRES 5 F 300 TRP LYS VAL LEU MET ILE ALA ALA GLU GLU ARG TYR VAL
SEQRES 6 F 300 LEU LEU GLU ASN GLY LYS MET PHE SER THR GLY ASN HIS
SEQRES 7 F 300 PRO VAL GLU MET LEU LEU PRO LEU HIS HIS LEU MET GLU
SEQRES 8 F 300 ALA GLY PHE ASP VAL ASP VAL ALA THR LEU SER GLY TYR
SEQRES 9 F 300 PRO VAL LYS LEU GLU LEU TRP ALA MET PRO THR GLU ASP
SEQRES 10 F 300 GLU ALA VAL ILE SER THR TYR ASN LYS LEU LYS GLU LYS
SEQRES 11 F 300 LEU LYS GLN PRO LYS LYS LEU ALA ASP VAL ILE LYS ASN
SEQRES 12 F 300 GLU LEU GLY PRO ASP SER ASP TYR LEU SER VAL PHE ILE
SEQRES 13 F 300 PRO GLY GLY HIS ALA ALA VAL VAL GLY ILE SER GLU SER
SEQRES 14 F 300 GLU ASP VAL GLN GLN THR LEU ASP TRP ALA LEU ASP ASN
SEQRES 15 F 300 ASP ARG PHE ILE VAL THR LEU CYS HIS GLY PRO ALA ALA
SEQRES 16 F 300 LEU LEU SER ALA GLY LEU ASN ARG GLU LYS SER PRO LEU
SEQRES 17 F 300 GLU GLY TYR SER VAL CYS VAL PHE PRO ASP SER LEU ASP
SEQRES 18 F 300 GLU GLY ALA ASN ILE GLU ILE GLY TYR LEU PRO GLY ARG
SEQRES 19 F 300 LEU LYS TRP LEU VAL ALA ASP LEU LEU THR LYS GLN GLY
SEQRES 20 F 300 LEU LYS VAL VAL ASN ASP ASP MET THR GLY ARG THR LEU
SEQRES 21 F 300 LYS ASP ARG LYS LEU LEU THR GLY ASP SER PRO LEU ALA
SEQRES 22 F 300 SER ASN GLU LEU GLY LYS LEU ALA VAL ASN GLU MET LEU
SEQRES 23 F 300 ASN ALA ILE GLN ASN LYS LEU GLU HIS HIS HIS HIS HIS
SEQRES 24 F 300 HIS
SEQRES 1 G 300 MET SER GLN ASP VAL ASN GLU LEU SER LYS GLN PRO THR
SEQRES 2 G 300 PRO ASP LYS ALA GLU ASP ASN ALA PHE PHE PRO SER PRO
SEQRES 3 G 300 TYR SER LEU SER GLN TYR THR ALA PRO LYS THR ASP PHE
SEQRES 4 G 300 ASP GLY VAL GLU HIS LYS GLY ALA TYR LYS ASP GLY LYS
SEQRES 5 G 300 TRP LYS VAL LEU MET ILE ALA ALA GLU GLU ARG TYR VAL
SEQRES 6 G 300 LEU LEU GLU ASN GLY LYS MET PHE SER THR GLY ASN HIS
SEQRES 7 G 300 PRO VAL GLU MET LEU LEU PRO LEU HIS HIS LEU MET GLU
SEQRES 8 G 300 ALA GLY PHE ASP VAL ASP VAL ALA THR LEU SER GLY TYR
SEQRES 9 G 300 PRO VAL LYS LEU GLU LEU TRP ALA MET PRO THR GLU ASP
SEQRES 10 G 300 GLU ALA VAL ILE SER THR TYR ASN LYS LEU LYS GLU LYS
SEQRES 11 G 300 LEU LYS GLN PRO LYS LYS LEU ALA ASP VAL ILE LYS ASN
SEQRES 12 G 300 GLU LEU GLY PRO ASP SER ASP TYR LEU SER VAL PHE ILE
SEQRES 13 G 300 PRO GLY GLY HIS ALA ALA VAL VAL GLY ILE SER GLU SER
SEQRES 14 G 300 GLU ASP VAL GLN GLN THR LEU ASP TRP ALA LEU ASP ASN
SEQRES 15 G 300 ASP ARG PHE ILE VAL THR LEU CYS HIS GLY PRO ALA ALA
SEQRES 16 G 300 LEU LEU SER ALA GLY LEU ASN ARG GLU LYS SER PRO LEU
SEQRES 17 G 300 GLU GLY TYR SER VAL CYS VAL PHE PRO ASP SER LEU ASP
SEQRES 18 G 300 GLU GLY ALA ASN ILE GLU ILE GLY TYR LEU PRO GLY ARG
SEQRES 19 G 300 LEU LYS TRP LEU VAL ALA ASP LEU LEU THR LYS GLN GLY
SEQRES 20 G 300 LEU LYS VAL VAL ASN ASP ASP MET THR GLY ARG THR LEU
SEQRES 21 G 300 LYS ASP ARG LYS LEU LEU THR GLY ASP SER PRO LEU ALA
SEQRES 22 G 300 SER ASN GLU LEU GLY LYS LEU ALA VAL ASN GLU MET LEU
SEQRES 23 G 300 ASN ALA ILE GLN ASN LYS LEU GLU HIS HIS HIS HIS HIS
SEQRES 24 G 300 HIS
SEQRES 1 H 300 MET SER GLN ASP VAL ASN GLU LEU SER LYS GLN PRO THR
SEQRES 2 H 300 PRO ASP LYS ALA GLU ASP ASN ALA PHE PHE PRO SER PRO
SEQRES 3 H 300 TYR SER LEU SER GLN TYR THR ALA PRO LYS THR ASP PHE
SEQRES 4 H 300 ASP GLY VAL GLU HIS LYS GLY ALA TYR LYS ASP GLY LYS
SEQRES 5 H 300 TRP LYS VAL LEU MET ILE ALA ALA GLU GLU ARG TYR VAL
SEQRES 6 H 300 LEU LEU GLU ASN GLY LYS MET PHE SER THR GLY ASN HIS
SEQRES 7 H 300 PRO VAL GLU MET LEU LEU PRO LEU HIS HIS LEU MET GLU
SEQRES 8 H 300 ALA GLY PHE ASP VAL ASP VAL ALA THR LEU SER GLY TYR
SEQRES 9 H 300 PRO VAL LYS LEU GLU LEU TRP ALA MET PRO THR GLU ASP
SEQRES 10 H 300 GLU ALA VAL ILE SER THR TYR ASN LYS LEU LYS GLU LYS
SEQRES 11 H 300 LEU LYS GLN PRO LYS LYS LEU ALA ASP VAL ILE LYS ASN
SEQRES 12 H 300 GLU LEU GLY PRO ASP SER ASP TYR LEU SER VAL PHE ILE
SEQRES 13 H 300 PRO GLY GLY HIS ALA ALA VAL VAL GLY ILE SER GLU SER
SEQRES 14 H 300 GLU ASP VAL GLN GLN THR LEU ASP TRP ALA LEU ASP ASN
SEQRES 15 H 300 ASP ARG PHE ILE VAL THR LEU CYS HIS GLY PRO ALA ALA
SEQRES 16 H 300 LEU LEU SER ALA GLY LEU ASN ARG GLU LYS SER PRO LEU
SEQRES 17 H 300 GLU GLY TYR SER VAL CYS VAL PHE PRO ASP SER LEU ASP
SEQRES 18 H 300 GLU GLY ALA ASN ILE GLU ILE GLY TYR LEU PRO GLY ARG
SEQRES 19 H 300 LEU LYS TRP LEU VAL ALA ASP LEU LEU THR LYS GLN GLY
SEQRES 20 H 300 LEU LYS VAL VAL ASN ASP ASP MET THR GLY ARG THR LEU
SEQRES 21 H 300 LYS ASP ARG LYS LEU LEU THR GLY ASP SER PRO LEU ALA
SEQRES 22 H 300 SER ASN GLU LEU GLY LYS LEU ALA VAL ASN GLU MET LEU
SEQRES 23 H 300 ASN ALA ILE GLN ASN LYS LEU GLU HIS HIS HIS HIS HIS
SEQRES 24 H 300 HIS
HET LAC A 401 6
HET ZN C 401 1
HET LAC E 401 6
HETNAM LAC LACTIC ACID
HETNAM ZN ZINC ION
FORMUL 9 LAC 2(C3 H6 O3)
FORMUL 10 ZN ZN 2+
FORMUL 12 HOH *280(H2 O)
HELIX 1 AA1 SER A 25 THR A 33 1 9
HELIX 2 AA2 HIS A 78 ALA A 92 1 15
HELIX 3 AA3 GLU A 109 MET A 113 5 5
HELIX 4 AA4 ASP A 117 GLN A 133 1 17
HELIX 5 AA5 LEU A 137 GLU A 144 1 8
HELIX 6 AA6 GLY A 159 VAL A 164 5 6
HELIX 7 AA7 GLY A 165 GLU A 168 5 4
HELIX 8 AA8 SER A 169 ASN A 182 1 14
HELIX 9 AA9 HIS A 191 LEU A 201 5 11
HELIX 10 AB1 PRO A 217 GLY A 223 1 7
HELIX 11 AB2 GLY A 223 ILE A 228 1 6
HELIX 12 AB3 LEU A 238 GLN A 246 1 9
HELIX 13 AB4 SER A 270 LEU A 272 5 3
HELIX 14 AB5 ALA A 273 LYS A 292 1 20
HELIX 15 AB6 SER B 25 THR B 33 1 9
HELIX 16 AB7 HIS B 78 ALA B 92 1 15
HELIX 17 AB8 GLU B 109 MET B 113 5 5
HELIX 18 AB9 ASP B 117 GLN B 133 1 17
HELIX 19 AC1 LEU B 137 GLU B 144 1 8
HELIX 20 AC2 GLY B 159 VAL B 164 5 6
HELIX 21 AC3 SER B 169 ASN B 182 1 14
HELIX 22 AC4 HIS B 191 LEU B 201 5 11
HELIX 23 AC5 PRO B 217 GLY B 223 1 7
HELIX 24 AC6 GLY B 223 ILE B 228 1 6
HELIX 25 AC7 LEU B 238 LYS B 245 1 8
HELIX 26 AC8 SER B 270 LEU B 272 5 3
HELIX 27 AC9 ALA B 273 ILE B 289 1 17
HELIX 28 AD1 SER C 25 THR C 33 1 9
HELIX 29 AD2 HIS C 78 ALA C 92 1 15
HELIX 30 AD3 GLU C 109 MET C 113 5 5
HELIX 31 AD4 ASP C 117 GLN C 133 1 17
HELIX 32 AD5 LEU C 137 GLU C 144 1 8
HELIX 33 AD6 GLY C 159 VAL C 164 5 6
HELIX 34 AD7 GLY C 165 GLU C 168 5 4
HELIX 35 AD8 SER C 169 ASN C 182 1 14
HELIX 36 AD9 HIS C 191 LEU C 201 5 11
HELIX 37 AE1 PRO C 217 GLY C 223 1 7
HELIX 38 AE2 GLY C 223 ILE C 228 1 6
HELIX 39 AE3 LEU C 238 GLN C 246 1 9
HELIX 40 AE4 SER C 270 LEU C 272 5 3
HELIX 41 AE5 ALA C 273 HIS C 297 1 25
HELIX 42 AE6 SER D 25 THR D 33 1 9
HELIX 43 AE7 HIS D 78 ALA D 92 1 15
HELIX 44 AE8 GLU D 109 MET D 113 5 5
HELIX 45 AE9 ASP D 117 GLN D 133 1 17
HELIX 46 AF1 LEU D 137 GLU D 144 1 8
HELIX 47 AF2 GLY D 159 VAL D 164 5 6
HELIX 48 AF3 SER D 169 ASP D 181 1 13
HELIX 49 AF4 HIS D 191 LEU D 201 5 11
HELIX 50 AF5 PRO D 217 GLY D 223 1 7
HELIX 51 AF6 GLY D 223 ILE D 228 1 6
HELIX 52 AF7 LEU D 238 GLN D 246 1 9
HELIX 53 AF8 SER D 270 LEU D 272 5 3
HELIX 54 AF9 ALA D 273 ALA D 288 1 16
HELIX 55 AG1 SER E 25 THR E 33 1 9
HELIX 56 AG2 HIS E 78 ALA E 92 1 15
HELIX 57 AG3 GLU E 109 MET E 113 5 5
HELIX 58 AG4 ASP E 117 GLN E 133 1 17
HELIX 59 AG5 LEU E 137 LEU E 145 1 9
HELIX 60 AG6 GLY E 159 VAL E 164 5 6
HELIX 61 AG7 SER E 169 ASN E 182 1 14
HELIX 62 AG8 HIS E 191 LEU E 201 5 11
HELIX 63 AG9 PRO E 217 GLY E 223 1 7
HELIX 64 AH1 GLY E 223 ILE E 228 1 6
HELIX 65 AH2 LEU E 238 GLN E 246 1 9
HELIX 66 AH3 SER E 270 LEU E 272 5 3
HELIX 67 AH4 ALA E 273 LYS E 292 1 20
HELIX 68 AH5 SER F 25 THR F 33 1 9
HELIX 69 AH6 HIS F 78 ALA F 92 1 15
HELIX 70 AH7 GLU F 109 MET F 113 5 5
HELIX 71 AH8 ASP F 117 GLN F 133 1 17
HELIX 72 AH9 LEU F 137 GLU F 144 1 8
HELIX 73 AI1 GLY F 159 VAL F 164 5 6
HELIX 74 AI2 SER F 169 ASN F 182 1 14
HELIX 75 AI3 HIS F 191 LEU F 201 5 11
HELIX 76 AI4 PRO F 217 GLY F 223 1 7
HELIX 77 AI5 GLY F 223 ILE F 228 1 6
HELIX 78 AI6 LEU F 238 GLN F 246 1 9
HELIX 79 AI7 SER F 270 LEU F 272 5 3
HELIX 80 AI8 ALA F 273 ASN F 287 1 15
HELIX 81 AI9 SER G 25 THR G 33 1 9
HELIX 82 AJ1 HIS G 78 ALA G 92 1 15
HELIX 83 AJ2 GLU G 109 MET G 113 5 5
HELIX 84 AJ3 ASP G 117 GLN G 133 1 17
HELIX 85 AJ4 LEU G 137 GLU G 144 1 8
HELIX 86 AJ5 GLY G 159 VAL G 164 5 6
HELIX 87 AJ6 GLY G 165 GLU G 168 5 4
HELIX 88 AJ7 SER G 169 ASN G 182 1 14
HELIX 89 AJ8 HIS G 191 LEU G 201 5 11
HELIX 90 AJ9 PRO G 217 GLY G 223 1 7
HELIX 91 AK1 GLY G 223 ILE G 228 1 6
HELIX 92 AK2 LEU G 238 GLN G 246 1 9
HELIX 93 AK3 SER G 270 LEU G 272 5 3
HELIX 94 AK4 ALA G 273 GLU G 294 1 22
HELIX 95 AK5 SER H 25 THR H 33 1 9
HELIX 96 AK6 HIS H 78 ALA H 92 1 15
HELIX 97 AK7 GLU H 109 MET H 113 5 5
HELIX 98 AK8 ASP H 117 GLN H 133 1 17
HELIX 99 AK9 LEU H 137 GLU H 144 1 8
HELIX 100 AL1 GLY H 159 VAL H 164 5 6
HELIX 101 AL2 GLY H 165 GLU H 168 5 4
HELIX 102 AL3 SER H 169 ASN H 182 1 14
HELIX 103 AL4 HIS H 191 LEU H 201 5 11
HELIX 104 AL5 PRO H 217 GLY H 223 1 7
HELIX 105 AL6 GLY H 223 ILE H 228 1 6
HELIX 106 AL7 LEU H 238 LYS H 245 1 8
HELIX 107 AL8 SER H 270 LEU H 272 5 3
HELIX 108 AL9 ALA H 273 ASN H 291 1 19
SHEET 1 AA1 4 THR A 13 PRO A 14 0
SHEET 2 AA1 4 ALA A 21 PHE A 23 -1 O PHE A 23 N THR A 13
SHEET 3 AA1 4 MET A 72 SER A 74 1 O SER A 74 N PHE A 22
SHEET 4 AA1 4 TYR A 64 LEU A 66 -1 N VAL A 65 O PHE A 73
SHEET 1 AA2 7 LYS A 135 LYS A 136 0
SHEET 2 AA2 7 ASP A 95 THR A 100 1 N VAL A 98 O LYS A 135
SHEET 3 AA2 7 LYS A 54 ILE A 58 1 N MET A 57 O ASP A 97
SHEET 4 AA2 7 TYR A 151 ILE A 156 1 O PHE A 155 N LEU A 56
SHEET 5 AA2 7 PHE A 185 LEU A 189 1 O VAL A 187 N ILE A 156
SHEET 6 AA2 7 LEU A 265 GLY A 268 1 O LEU A 266 N ILE A 186
SHEET 7 AA2 7 THR A 259 ASP A 262 -1 N LEU A 260 O THR A 267
SHEET 1 AA3 2 SER A 212 VAL A 213 0
SHEET 2 AA3 2 LYS A 249 VAL A 250 1 O LYS A 249 N VAL A 213
SHEET 1 AA4 4 THR B 13 PRO B 14 0
SHEET 2 AA4 4 ALA B 21 PHE B 23 -1 O PHE B 23 N THR B 13
SHEET 3 AA4 4 MET B 72 SER B 74 1 O MET B 72 N PHE B 22
SHEET 4 AA4 4 TYR B 64 LEU B 66 -1 N VAL B 65 O PHE B 73
SHEET 1 AA5 7 LYS B 135 LYS B 136 0
SHEET 2 AA5 7 ASP B 95 THR B 100 1 N VAL B 98 O LYS B 135
SHEET 3 AA5 7 LYS B 54 ILE B 58 1 N MET B 57 O ASP B 97
SHEET 4 AA5 7 TYR B 151 ILE B 156 1 O LEU B 152 N LYS B 54
SHEET 5 AA5 7 PHE B 185 LEU B 189 1 O VAL B 187 N VAL B 154
SHEET 6 AA5 7 LEU B 265 GLY B 268 1 O LEU B 266 N THR B 188
SHEET 7 AA5 7 THR B 259 ASP B 262 -1 N LEU B 260 O THR B 267
SHEET 1 AA6 2 SER B 212 VAL B 213 0
SHEET 2 AA6 2 LYS B 249 VAL B 250 1 O LYS B 249 N VAL B 213
SHEET 1 AA7 4 THR C 13 PRO C 14 0
SHEET 2 AA7 4 ALA C 21 PHE C 23 -1 O PHE C 23 N THR C 13
SHEET 3 AA7 4 MET C 72 SER C 74 1 O SER C 74 N PHE C 22
SHEET 4 AA7 4 TYR C 64 LEU C 66 -1 N VAL C 65 O PHE C 73
SHEET 1 AA8 7 LYS C 135 LYS C 136 0
SHEET 2 AA8 7 ASP C 95 THR C 100 1 N THR C 100 O LYS C 135
SHEET 3 AA8 7 LYS C 54 ILE C 58 1 N MET C 57 O ASP C 97
SHEET 4 AA8 7 TYR C 151 ILE C 156 1 O PHE C 155 N LEU C 56
SHEET 5 AA8 7 PHE C 185 LEU C 189 1 O VAL C 187 N ILE C 156
SHEET 6 AA8 7 LEU C 265 GLY C 268 1 O LEU C 266 N THR C 188
SHEET 7 AA8 7 THR C 259 ASP C 262 -1 N LEU C 260 O THR C 267
SHEET 1 AA9 2 SER C 212 VAL C 213 0
SHEET 2 AA9 2 LYS C 249 VAL C 250 1 O LYS C 249 N VAL C 213
SHEET 1 AB1 4 THR D 13 PRO D 14 0
SHEET 2 AB1 4 ALA D 21 PHE D 23 -1 O PHE D 23 N THR D 13
SHEET 3 AB1 4 MET D 72 SER D 74 1 O MET D 72 N PHE D 22
SHEET 4 AB1 4 TYR D 64 LEU D 66 -1 N VAL D 65 O PHE D 73
SHEET 1 AB2 7 LYS D 135 LYS D 136 0
SHEET 2 AB2 7 ASP D 95 THR D 100 1 N VAL D 98 O LYS D 135
SHEET 3 AB2 7 LYS D 54 ILE D 58 1 N MET D 57 O ASP D 97
SHEET 4 AB2 7 TYR D 151 ILE D 156 1 O SER D 153 N LEU D 56
SHEET 5 AB2 7 PHE D 185 THR D 188 1 O VAL D 187 N VAL D 154
SHEET 6 AB2 7 LEU D 265 GLY D 268 1 O LEU D 266 N ILE D 186
SHEET 7 AB2 7 THR D 259 ASP D 262 -1 N ASP D 262 O LEU D 265
SHEET 1 AB3 2 SER D 212 VAL D 213 0
SHEET 2 AB3 2 LYS D 249 VAL D 250 1 O LYS D 249 N VAL D 213
SHEET 1 AB4 4 THR E 13 PRO E 14 0
SHEET 2 AB4 4 ALA E 21 PHE E 23 -1 O PHE E 23 N THR E 13
SHEET 3 AB4 4 MET E 72 SER E 74 1 O SER E 74 N PHE E 22
SHEET 4 AB4 4 TYR E 64 LEU E 66 -1 N VAL E 65 O PHE E 73
SHEET 1 AB5 7 LYS E 135 LYS E 136 0
SHEET 2 AB5 7 ASP E 95 THR E 100 1 N VAL E 98 O LYS E 135
SHEET 3 AB5 7 LYS E 54 ILE E 58 1 N VAL E 55 O ASP E 95
SHEET 4 AB5 7 TYR E 151 ILE E 156 1 O SER E 153 N LEU E 56
SHEET 5 AB5 7 PHE E 185 LEU E 189 1 O VAL E 187 N VAL E 154
SHEET 6 AB5 7 LEU E 265 GLY E 268 1 O LEU E 266 N THR E 188
SHEET 7 AB5 7 THR E 259 ASP E 262 -1 N ASP E 262 O LEU E 265
SHEET 1 AB6 2 SER E 212 VAL E 213 0
SHEET 2 AB6 2 LYS E 249 VAL E 250 1 O LYS E 249 N VAL E 213
SHEET 1 AB7 4 THR F 13 PRO F 14 0
SHEET 2 AB7 4 ALA F 21 PHE F 23 -1 O PHE F 23 N THR F 13
SHEET 3 AB7 4 MET F 72 SER F 74 1 O SER F 74 N PHE F 22
SHEET 4 AB7 4 TYR F 64 LEU F 66 -1 N VAL F 65 O PHE F 73
SHEET 1 AB8 7 LYS F 135 LYS F 136 0
SHEET 2 AB8 7 ASP F 95 THR F 100 1 N VAL F 98 O LYS F 135
SHEET 3 AB8 7 LYS F 54 ILE F 58 1 N VAL F 55 O ASP F 97
SHEET 4 AB8 7 TYR F 151 ILE F 156 1 O LEU F 152 N LYS F 54
SHEET 5 AB8 7 PHE F 185 LEU F 189 1 O VAL F 187 N VAL F 154
SHEET 6 AB8 7 LEU F 265 GLY F 268 1 O LEU F 266 N ILE F 186
SHEET 7 AB8 7 THR F 259 ASP F 262 -1 N ASP F 262 O LEU F 265
SHEET 1 AB9 2 SER F 212 VAL F 213 0
SHEET 2 AB9 2 LYS F 249 VAL F 250 1 O LYS F 249 N VAL F 213
SHEET 1 AC1 4 THR G 13 PRO G 14 0
SHEET 2 AC1 4 ALA G 21 PHE G 23 -1 O PHE G 23 N THR G 13
SHEET 3 AC1 4 MET G 72 SER G 74 1 O SER G 74 N PHE G 22
SHEET 4 AC1 4 TYR G 64 LEU G 66 -1 N VAL G 65 O PHE G 73
SHEET 1 AC2 7 LYS G 135 LYS G 136 0
SHEET 2 AC2 7 ASP G 95 THR G 100 1 N VAL G 98 O LYS G 135
SHEET 3 AC2 7 LYS G 54 ILE G 58 1 N VAL G 55 O ASP G 95
SHEET 4 AC2 7 TYR G 151 ILE G 156 1 O SER G 153 N LEU G 56
SHEET 5 AC2 7 PHE G 185 LEU G 189 1 O VAL G 187 N ILE G 156
SHEET 6 AC2 7 LEU G 265 GLY G 268 1 O LEU G 266 N ILE G 186
SHEET 7 AC2 7 THR G 259 ASP G 262 -1 N LEU G 260 O THR G 267
SHEET 1 AC3 2 SER G 212 VAL G 213 0
SHEET 2 AC3 2 LYS G 249 VAL G 250 1 O LYS G 249 N VAL G 213
SHEET 1 AC4 4 THR H 13 PRO H 14 0
SHEET 2 AC4 4 ALA H 21 PHE H 23 -1 O PHE H 23 N THR H 13
SHEET 3 AC4 4 MET H 72 SER H 74 1 O SER H 74 N PHE H 22
SHEET 4 AC4 4 TYR H 64 LEU H 66 -1 N VAL H 65 O PHE H 73
SHEET 1 AC5 7 LYS H 135 LYS H 136 0
SHEET 2 AC5 7 ASP H 95 THR H 100 1 N VAL H 98 O LYS H 135
SHEET 3 AC5 7 LYS H 54 ILE H 58 1 N MET H 57 O ASP H 97
SHEET 4 AC5 7 TYR H 151 ILE H 156 1 O PHE H 155 N LEU H 56
SHEET 5 AC5 7 PHE H 185 LEU H 189 1 O VAL H 187 N VAL H 154
SHEET 6 AC5 7 LEU H 265 GLY H 268 1 O LEU H 266 N THR H 188
SHEET 7 AC5 7 THR H 259 LEU H 260 -1 N LEU H 260 O THR H 267
SHEET 1 AC6 2 SER H 212 VAL H 213 0
SHEET 2 AC6 2 LYS H 249 VAL H 250 1 O LYS H 249 N VAL H 213
LINK NE2 HIS C 295 ZN ZN C 401 1555 1555 2.51
LINK ZN ZN C 401 NE2 HIS G 296 2655 1555 2.45
LINK ZN ZN C 401 NE2 HIS G 298 2655 1555 2.50
LINK ZN ZN C 401 NE2 HIS G 300 2655 1555 2.31
SITE 1 AC1 2 ASP A 181 ASP G 181
SITE 1 AC2 5 HIS C 295 HIS C 299 HIS G 296 HIS G 298
SITE 2 AC2 5 HIS G 300
SITE 1 AC3 3 ASP C 181 ARG C 203 ASP E 181
CRYST1 96.284 129.454 187.853 90.00 90.00 90.00 P 21 21 21 32
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 0.010386 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007725 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005323 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
