HEADER OXIDOREDUCTASE 05-JAN-09 3FPC
TITLE CHIMERA OF ALCOHOL DEHYDROGENASE BY EXCHANGE OF THE COFACTOR BINDING
TITLE 2 DOMAIN RES 153-294 OF T. BROCKII ADH BY E. HISTOLYTICA ADH
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NADP-DEPENDENT ALCOHOL DEHYDROGENASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 EC: 1.1.1.2;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: CHIMERA OF ALCOHOL DEHYDROGENASE BY EXCHANGE OF
COMPND 7 COFACTOR BINDING DOMAIN RES 153-294 OF THERMOANAEROBACTER BROCKII BY
COMPND 8 ENTAMOEBA HISTOLYTICA
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOANAEROBACTER BROCKII, ENTAMOEBA
SOURCE 3 HISTOLYTICA;
SOURCE 4 ORGANISM_COMMON: THERMOANAEROBIUM BROCKII;
SOURCE 5 ORGANISM_TAXID: 29323, 5759;
SOURCE 6 GENE: ADH1, ADH1;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: TG-I;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: BS-P58
KEYWDS OXYDOREDUCTASE, BACTERIAL ALCOHOL DEHYDROGENASE, DOMAIN EXCHANGE,
KEYWDS 2 CHIMERA, METAL-BINDING, NADP, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR F.FELIX,E.GOIHBERG,L.SHIMON,Y.BURSTEIN
REVDAT 6 01-NOV-23 3FPC 1 REMARK LINK
REVDAT 5 01-NOV-17 3FPC 1 REMARK
REVDAT 4 09-AUG-17 3FPC 1 SOURCE REMARK
REVDAT 3 29-JAN-14 3FPC 1 JRNL VERSN
REVDAT 2 16-FEB-10 3FPC 1 JRNL
REVDAT 1 19-JAN-10 3FPC 0
JRNL AUTH E.GOIHBERG,M.PERETZ,S.TEL-OR,O.DYM,L.SHIMON,F.FROLOW,
JRNL AUTH 2 Y.BURSTEIN
JRNL TITL BIOCHEMICAL AND STRUCTURAL PROPERTIES OF CHIMERAS
JRNL TITL 2 CONSTRUCTED BY EXCHANGE OF COFACTOR-BINDING DOMAINS IN
JRNL TITL 3 ALCOHOL DEHYDROGENASES FROM THERMOPHILIC AND MESOPHILIC
JRNL TITL 4 MICROORGANISMS
JRNL REF BIOCHEMISTRY V. 49 1943 2010
JRNL REFN ISSN 0006-2960
JRNL PMID 20102159
JRNL DOI 10.1021/BI901730X
REMARK 2
REMARK 2 RESOLUTION. 1.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
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) : 1.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.77
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 293136
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) : 0.118
REMARK 3 R VALUE (WORKING SET) : 0.116
REMARK 3 FREE R VALUE : 0.155
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 14820
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.44
REMARK 3 REFLECTION IN BIN (WORKING SET) : 19107
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.17
REMARK 3 BIN R VALUE (WORKING SET) : 0.2210
REMARK 3 BIN FREE R VALUE SET COUNT : 940
REMARK 3 BIN FREE R VALUE : 0.2650
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 10675
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 97
REMARK 3 SOLVENT ATOMS : 1988
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 11.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.04000
REMARK 3 B22 (A**2) : -0.23000
REMARK 3 B33 (A**2) : 0.09000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.50000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.047
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.048
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.030
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.708
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.983
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.971
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 11332 ; 0.014 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 7776 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 15343 ; 1.507 ; 1.960
REMARK 3 BOND ANGLES OTHERS (DEGREES): 19046 ; 0.991 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1494 ; 6.618 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 468 ;35.021 ;23.996
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1941 ;11.914 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 59 ;15.240 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1678 ; 0.103 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 12742 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 2235 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2317 ; 0.218 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 8673 ; 0.206 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 5431 ; 0.176 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 5914 ; 0.086 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 1575 ; 0.193 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 13 ; 0.112 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 8 ; 0.229 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 69 ; 0.233 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 56 ; 0.185 ; 0.200
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): 7109 ; 2.405 ; 3.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2972 ; 1.269 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 11468 ; 3.311 ; 5.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4314 ; 4.387 ; 7.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3841 ; 6.226 ;10.000
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): 19731 ; 1.784 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 1996 ; 6.795 ; 3.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 18838 ; 3.410 ; 3.000
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 : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3FPC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 07-JAN-09.
REMARK 100 THE DEPOSITION ID IS D_1000050874.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-JUN-03
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.933
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 294442
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.400
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 3.100
REMARK 200 R MERGE (I) : 0.07500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.1430
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.42
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.30
REMARK 200 R MERGE FOR SHELL (I) : 0.66400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.400
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 1KEV
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 8MG/ML PROTEIN [25MM TRIS-HCL, 50MM
REMARK 280 NACL, 0.1MM DTT, 50MM ZNCL2 (PH=7.5)] WAS MIXED WITH 0.001 ML OF
REMARK 280 RESERVOIR SOLUTION [16% (W/V) PEG 8000, 200MM MAGNESIUM ACETATE
REMARK 280 TETRAHYDRATE, 100MM CACODYLATE BUFFER (PH 6.5)], VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 298K
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 41.21450
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 20640 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 43380 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -178.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 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 A 439 O HOH A 2027 1.60
REMARK 500 OD2 ASP A 275 O HOH A 465 1.68
REMARK 500 O HOH A 451 O HOH A 464 1.86
REMARK 500 O HOH A 434 O HOH A 2028 1.89
REMARK 500 O HOH D 660 O HOH D 2025 1.90
REMARK 500 O HOH B 470 O HOH B 1945 1.92
REMARK 500 O HOH B 882 O HOH B 2061 1.93
REMARK 500 O HOH A 465 O HOH A 468 1.95
REMARK 500 O HOH B 483 O HOH B 527 1.97
REMARK 500 NZ LYS B 111 O HOH B 2021 1.97
REMARK 500 O HOH B 651 O HOH B 2056 1.98
REMARK 500 O HOH C 2031 O HOH C 2048 2.02
REMARK 500 OG SER A 103 O HOH A 449 2.03
REMARK 500 CB LYS C 138 O HOH C 2044 2.08
REMARK 500 O HOH D 1838 O HOH D 1958 2.09
REMARK 500 O HOH C 368 O HOH C 1948 2.12
REMARK 500 O HOH C 503 O HOH C 2082 2.12
REMARK 500 OE1 GLU D 67 O HOH D 1872 2.13
REMARK 500 O HOH C 1993 O HOH D 1453 2.13
REMARK 500 O LYS D 165 O HOH D 1890 2.15
REMARK 500 C5 IMD C 355 O HOH C 590 2.16
REMARK 500 O HOH C 626 O HOH C 1948 2.17
REMARK 500 O HOH C 1144 O HOH C 2049 2.18
REMARK 500 O HOH B 565 O HOH B 1845 2.19
REMARK 500 O HOH A 911 O HOH A 1870 2.19
REMARK 500 O HOH C 641 O HOH D 1991 2.19
REMARK 500 O HOH C 784 O HOH C 1846 2.19
REMARK 500 O HOH A 629 O HOH A 1852 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG D 278 NE - CZ - NH1 ANGL. DEV. = 3.1 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 HIS A 59 20.37 -146.57
REMARK 500 ARG A 91 68.44 -103.67
REMARK 500 LYS A 111 -60.27 -95.64
REMARK 500 ASP A 150 -55.82 -142.04
REMARK 500 ILE A 345 -70.03 -114.54
REMARK 500 HIS B 59 21.86 -145.06
REMARK 500 ARG B 91 68.29 -105.56
REMARK 500 ASP B 150 -53.37 -142.66
REMARK 500 SER B 199 -11.62 -140.71
REMARK 500 HIS C 59 19.43 -143.78
REMARK 500 ARG C 91 67.01 -102.09
REMARK 500 ASP C 150 -53.56 -142.65
REMARK 500 LYS C 340 80.97 18.79
REMARK 500 LYS C 340 80.97 30.91
REMARK 500 ILE C 345 -70.55 -112.22
REMARK 500 HIS D 59 20.86 -144.86
REMARK 500 ARG D 91 66.96 -105.31
REMARK 500 ASP D 128 70.29 56.02
REMARK 500 ASP D 150 -55.18 -140.86
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 A 353 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 37 SG
REMARK 620 2 HIS A 59 NE2 117.0
REMARK 620 3 ASP A 150 OD2 121.6 93.5
REMARK 620 4 CAC A 354 O2 108.6 104.4 110.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 353 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 37 SG
REMARK 620 2 HIS B 59 NE2 117.7
REMARK 620 3 ASP B 150 OD2 118.6 95.6
REMARK 620 4 CAC B 354 O1 108.4 103.3 111.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 353 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 37 SG
REMARK 620 2 HIS C 59 NE2 116.7
REMARK 620 3 ASP C 150 OD2 120.8 96.0
REMARK 620 4 CAC C 354 O2 108.3 102.9 110.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA C 361 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER C 103 O
REMARK 620 2 SER C 103 O 2.6
REMARK 620 3 SER C 103 OG 63.0 65.3
REMARK 620 4 ALA C 108 O 87.2 87.1 112.0
REMARK 620 5 LYS C 111 NZ 123.5 121.3 172.7 66.8
REMARK 620 6 HOH C 754 O 64.7 62.2 117.7 96.5 69.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 353 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 37 SG
REMARK 620 2 HIS D 59 NE2 116.7
REMARK 620 3 ASP D 150 OD2 119.9 95.7
REMARK 620 4 CAC D 354 O2 108.7 103.7 110.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA D 361 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 89 N
REMARK 620 2 SER D 103 O 127.6
REMARK 620 3 SER D 103 O 130.6 3.3
REMARK 620 4 SER D 103 OG 78.3 62.9 65.9
REMARK 620 5 ALA D 108 O 141.4 87.2 84.8 110.6
REMARK 620 6 LYS D 111 NZ 97.5 123.8 120.7 173.0 69.2
REMARK 620 7 HOH D2019 O 112.9 67.1 65.1 121.6 94.6 65.1
REMARK 620 N 1 2 3 4 5 6
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 353
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAC A 354
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OXY A 355
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 353
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAC B 354
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 355
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 356
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 B 357
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 358
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 359
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 353
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAC C 354
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD C 355
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 356
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 357
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 358
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 359
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 360
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA C 361
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 353
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAC D 354
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 355
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 356
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 357
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 358
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 D 359
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 360
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA D 361
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3FPL RELATED DB: PDB
DBREF 3FPC A 1 152 UNP P14941 ADH_THEBR 1 152
DBREF 3FPC A 153 294 UNP P35630 ADH1_ENTHI 153 294
DBREF 3FPC A 295 352 UNP P14941 ADH_THEBR 295 352
DBREF 3FPC B 1 152 UNP P14941 ADH_THEBR 1 152
DBREF 3FPC B 153 294 UNP P35630 ADH1_ENTHI 153 294
DBREF 3FPC B 295 352 UNP P14941 ADH_THEBR 295 352
DBREF 3FPC C 1 152 UNP P14941 ADH_THEBR 1 152
DBREF 3FPC C 153 294 UNP P35630 ADH1_ENTHI 153 294
DBREF 3FPC C 295 352 UNP P14941 ADH_THEBR 295 352
DBREF 3FPC D 1 152 UNP P14941 ADH_THEBR 1 152
DBREF 3FPC D 153 294 UNP P35630 ADH1_ENTHI 153 294
DBREF 3FPC D 295 352 UNP P14941 ADH_THEBR 295 352
SEQRES 1 A 352 MET LYS GLY PHE ALA MET LEU SER ILE GLY LYS VAL GLY
SEQRES 2 A 352 TRP ILE GLU LYS GLU LYS PRO ALA PRO GLY PRO PHE ASP
SEQRES 3 A 352 ALA ILE VAL ARG PRO LEU ALA VAL ALA PRO CYS THR SER
SEQRES 4 A 352 ASP ILE HIS THR VAL PHE GLU GLY ALA ILE GLY GLU ARG
SEQRES 5 A 352 HIS ASN MET ILE LEU GLY HIS GLU ALA VAL GLY GLU VAL
SEQRES 6 A 352 VAL GLU VAL GLY SER GLU VAL LYS ASP PHE LYS PRO GLY
SEQRES 7 A 352 ASP ARG VAL VAL VAL PRO ALA ILE THR PRO ASP TRP ARG
SEQRES 8 A 352 THR SER GLU VAL GLN ARG GLY TYR HIS GLN HIS SER GLY
SEQRES 9 A 352 GLY MET LEU ALA GLY TRP LYS PHE SER ASN VAL LYS ASP
SEQRES 10 A 352 GLY VAL PHE GLY GLU PHE PHE HIS VAL ASN ASP ALA ASP
SEQRES 11 A 352 MET ASN LEU ALA HIS LEU PRO LYS GLU ILE PRO LEU GLU
SEQRES 12 A 352 ALA ALA VAL MET ILE PRO ASP MET MET THR THR GLY PHE
SEQRES 13 A 352 HIS GLY ALA GLU LEU ALA ASN ILE LYS LEU GLY ASP THR
SEQRES 14 A 352 VAL CYS VAL ILE GLY ILE GLY PRO VAL GLY LEU MET SER
SEQRES 15 A 352 VAL ALA GLY ALA ASN HIS LEU GLY ALA GLY ARG ILE PHE
SEQRES 16 A 352 ALA VAL GLY SER ARG LYS HIS CYS CYS ASP ILE ALA LEU
SEQRES 17 A 352 GLU TYR GLY ALA THR ASP ILE ILE ASN TYR LYS ASN GLY
SEQRES 18 A 352 ASP ILE VAL GLU GLN ILE LEU LYS ALA THR ASP GLY LYS
SEQRES 19 A 352 GLY VAL ASP LYS VAL VAL ILE ALA GLY GLY ASP VAL HIS
SEQRES 20 A 352 THR PHE ALA GLN ALA VAL LYS MET ILE LYS PRO GLY SER
SEQRES 21 A 352 ASP ILE GLY ASN VAL ASN TYR LEU GLY GLU GLY ASP ASN
SEQRES 22 A 352 ILE ASP ILE PRO ARG SER GLU TRP GLY VAL GLY MET GLY
SEQRES 23 A 352 HIS LYS HIS ILE HIS GLY GLY LEU CYS PRO GLY GLY ARG
SEQRES 24 A 352 LEU ARG MET GLU ARG LEU ILE ASP LEU VAL PHE TYR LYS
SEQRES 25 A 352 ARG VAL ASP PRO SER LYS LEU VAL THR HIS VAL PHE ARG
SEQRES 26 A 352 GLY PHE ASP ASN ILE GLU LYS ALA PHE MET LEU MET LYS
SEQRES 27 A 352 ASP LYS PRO LYS ASP LEU ILE LYS PRO VAL VAL ILE LEU
SEQRES 28 A 352 ALA
SEQRES 1 B 352 MET LYS GLY PHE ALA MET LEU SER ILE GLY LYS VAL GLY
SEQRES 2 B 352 TRP ILE GLU LYS GLU LYS PRO ALA PRO GLY PRO PHE ASP
SEQRES 3 B 352 ALA ILE VAL ARG PRO LEU ALA VAL ALA PRO CYS THR SER
SEQRES 4 B 352 ASP ILE HIS THR VAL PHE GLU GLY ALA ILE GLY GLU ARG
SEQRES 5 B 352 HIS ASN MET ILE LEU GLY HIS GLU ALA VAL GLY GLU VAL
SEQRES 6 B 352 VAL GLU VAL GLY SER GLU VAL LYS ASP PHE LYS PRO GLY
SEQRES 7 B 352 ASP ARG VAL VAL VAL PRO ALA ILE THR PRO ASP TRP ARG
SEQRES 8 B 352 THR SER GLU VAL GLN ARG GLY TYR HIS GLN HIS SER GLY
SEQRES 9 B 352 GLY MET LEU ALA GLY TRP LYS PHE SER ASN VAL LYS ASP
SEQRES 10 B 352 GLY VAL PHE GLY GLU PHE PHE HIS VAL ASN ASP ALA ASP
SEQRES 11 B 352 MET ASN LEU ALA HIS LEU PRO LYS GLU ILE PRO LEU GLU
SEQRES 12 B 352 ALA ALA VAL MET ILE PRO ASP MET MET THR THR GLY PHE
SEQRES 13 B 352 HIS GLY ALA GLU LEU ALA ASN ILE LYS LEU GLY ASP THR
SEQRES 14 B 352 VAL CYS VAL ILE GLY ILE GLY PRO VAL GLY LEU MET SER
SEQRES 15 B 352 VAL ALA GLY ALA ASN HIS LEU GLY ALA GLY ARG ILE PHE
SEQRES 16 B 352 ALA VAL GLY SER ARG LYS HIS CYS CYS ASP ILE ALA LEU
SEQRES 17 B 352 GLU TYR GLY ALA THR ASP ILE ILE ASN TYR LYS ASN GLY
SEQRES 18 B 352 ASP ILE VAL GLU GLN ILE LEU LYS ALA THR ASP GLY LYS
SEQRES 19 B 352 GLY VAL ASP LYS VAL VAL ILE ALA GLY GLY ASP VAL HIS
SEQRES 20 B 352 THR PHE ALA GLN ALA VAL LYS MET ILE LYS PRO GLY SER
SEQRES 21 B 352 ASP ILE GLY ASN VAL ASN TYR LEU GLY GLU GLY ASP ASN
SEQRES 22 B 352 ILE ASP ILE PRO ARG SER GLU TRP GLY VAL GLY MET GLY
SEQRES 23 B 352 HIS LYS HIS ILE HIS GLY GLY LEU CYS PRO GLY GLY ARG
SEQRES 24 B 352 LEU ARG MET GLU ARG LEU ILE ASP LEU VAL PHE TYR LYS
SEQRES 25 B 352 ARG VAL ASP PRO SER LYS LEU VAL THR HIS VAL PHE ARG
SEQRES 26 B 352 GLY PHE ASP ASN ILE GLU LYS ALA PHE MET LEU MET LYS
SEQRES 27 B 352 ASP LYS PRO LYS ASP LEU ILE LYS PRO VAL VAL ILE LEU
SEQRES 28 B 352 ALA
SEQRES 1 C 352 MET LYS GLY PHE ALA MET LEU SER ILE GLY LYS VAL GLY
SEQRES 2 C 352 TRP ILE GLU LYS GLU LYS PRO ALA PRO GLY PRO PHE ASP
SEQRES 3 C 352 ALA ILE VAL ARG PRO LEU ALA VAL ALA PRO CYS THR SER
SEQRES 4 C 352 ASP ILE HIS THR VAL PHE GLU GLY ALA ILE GLY GLU ARG
SEQRES 5 C 352 HIS ASN MET ILE LEU GLY HIS GLU ALA VAL GLY GLU VAL
SEQRES 6 C 352 VAL GLU VAL GLY SER GLU VAL LYS ASP PHE LYS PRO GLY
SEQRES 7 C 352 ASP ARG VAL VAL VAL PRO ALA ILE THR PRO ASP TRP ARG
SEQRES 8 C 352 THR SER GLU VAL GLN ARG GLY TYR HIS GLN HIS SER GLY
SEQRES 9 C 352 GLY MET LEU ALA GLY TRP LYS PHE SER ASN VAL LYS ASP
SEQRES 10 C 352 GLY VAL PHE GLY GLU PHE PHE HIS VAL ASN ASP ALA ASP
SEQRES 11 C 352 MET ASN LEU ALA HIS LEU PRO LYS GLU ILE PRO LEU GLU
SEQRES 12 C 352 ALA ALA VAL MET ILE PRO ASP MET MET THR THR GLY PHE
SEQRES 13 C 352 HIS GLY ALA GLU LEU ALA ASN ILE LYS LEU GLY ASP THR
SEQRES 14 C 352 VAL CYS VAL ILE GLY ILE GLY PRO VAL GLY LEU MET SER
SEQRES 15 C 352 VAL ALA GLY ALA ASN HIS LEU GLY ALA GLY ARG ILE PHE
SEQRES 16 C 352 ALA VAL GLY SER ARG LYS HIS CYS CYS ASP ILE ALA LEU
SEQRES 17 C 352 GLU TYR GLY ALA THR ASP ILE ILE ASN TYR LYS ASN GLY
SEQRES 18 C 352 ASP ILE VAL GLU GLN ILE LEU LYS ALA THR ASP GLY LYS
SEQRES 19 C 352 GLY VAL ASP LYS VAL VAL ILE ALA GLY GLY ASP VAL HIS
SEQRES 20 C 352 THR PHE ALA GLN ALA VAL LYS MET ILE LYS PRO GLY SER
SEQRES 21 C 352 ASP ILE GLY ASN VAL ASN TYR LEU GLY GLU GLY ASP ASN
SEQRES 22 C 352 ILE ASP ILE PRO ARG SER GLU TRP GLY VAL GLY MET GLY
SEQRES 23 C 352 HIS LYS HIS ILE HIS GLY GLY LEU CYS PRO GLY GLY ARG
SEQRES 24 C 352 LEU ARG MET GLU ARG LEU ILE ASP LEU VAL PHE TYR LYS
SEQRES 25 C 352 ARG VAL ASP PRO SER LYS LEU VAL THR HIS VAL PHE ARG
SEQRES 26 C 352 GLY PHE ASP ASN ILE GLU LYS ALA PHE MET LEU MET LYS
SEQRES 27 C 352 ASP LYS PRO LYS ASP LEU ILE LYS PRO VAL VAL ILE LEU
SEQRES 28 C 352 ALA
SEQRES 1 D 352 MET LYS GLY PHE ALA MET LEU SER ILE GLY LYS VAL GLY
SEQRES 2 D 352 TRP ILE GLU LYS GLU LYS PRO ALA PRO GLY PRO PHE ASP
SEQRES 3 D 352 ALA ILE VAL ARG PRO LEU ALA VAL ALA PRO CYS THR SER
SEQRES 4 D 352 ASP ILE HIS THR VAL PHE GLU GLY ALA ILE GLY GLU ARG
SEQRES 5 D 352 HIS ASN MET ILE LEU GLY HIS GLU ALA VAL GLY GLU VAL
SEQRES 6 D 352 VAL GLU VAL GLY SER GLU VAL LYS ASP PHE LYS PRO GLY
SEQRES 7 D 352 ASP ARG VAL VAL VAL PRO ALA ILE THR PRO ASP TRP ARG
SEQRES 8 D 352 THR SER GLU VAL GLN ARG GLY TYR HIS GLN HIS SER GLY
SEQRES 9 D 352 GLY MET LEU ALA GLY TRP LYS PHE SER ASN VAL LYS ASP
SEQRES 10 D 352 GLY VAL PHE GLY GLU PHE PHE HIS VAL ASN ASP ALA ASP
SEQRES 11 D 352 MET ASN LEU ALA HIS LEU PRO LYS GLU ILE PRO LEU GLU
SEQRES 12 D 352 ALA ALA VAL MET ILE PRO ASP MET MET THR THR GLY PHE
SEQRES 13 D 352 HIS GLY ALA GLU LEU ALA ASN ILE LYS LEU GLY ASP THR
SEQRES 14 D 352 VAL CYS VAL ILE GLY ILE GLY PRO VAL GLY LEU MET SER
SEQRES 15 D 352 VAL ALA GLY ALA ASN HIS LEU GLY ALA GLY ARG ILE PHE
SEQRES 16 D 352 ALA VAL GLY SER ARG LYS HIS CYS CYS ASP ILE ALA LEU
SEQRES 17 D 352 GLU TYR GLY ALA THR ASP ILE ILE ASN TYR LYS ASN GLY
SEQRES 18 D 352 ASP ILE VAL GLU GLN ILE LEU LYS ALA THR ASP GLY LYS
SEQRES 19 D 352 GLY VAL ASP LYS VAL VAL ILE ALA GLY GLY ASP VAL HIS
SEQRES 20 D 352 THR PHE ALA GLN ALA VAL LYS MET ILE LYS PRO GLY SER
SEQRES 21 D 352 ASP ILE GLY ASN VAL ASN TYR LEU GLY GLU GLY ASP ASN
SEQRES 22 D 352 ILE ASP ILE PRO ARG SER GLU TRP GLY VAL GLY MET GLY
SEQRES 23 D 352 HIS LYS HIS ILE HIS GLY GLY LEU CYS PRO GLY GLY ARG
SEQRES 24 D 352 LEU ARG MET GLU ARG LEU ILE ASP LEU VAL PHE TYR LYS
SEQRES 25 D 352 ARG VAL ASP PRO SER LYS LEU VAL THR HIS VAL PHE ARG
SEQRES 26 D 352 GLY PHE ASP ASN ILE GLU LYS ALA PHE MET LEU MET LYS
SEQRES 27 D 352 ASP LYS PRO LYS ASP LEU ILE LYS PRO VAL VAL ILE LEU
SEQRES 28 D 352 ALA
HET ZN A 353 1
HET CAC A 354 5
HET OXY A 355 2
HET ZN B 353 1
HET CAC B 354 5
HET EDO B 355 4
HET EDO B 356 4
HET NO3 B 357 4
HET EDO B 358 4
HET EDO B 359 8
HET ZN C 353 1
HET CAC C 354 5
HET IMD C 355 5
HET EDO C 356 4
HET EDO C 357 8
HET EDO C 358 4
HET EDO C 359 4
HET EDO C 360 4
HET NA C 361 1
HET ZN D 353 1
HET CAC D 354 5
HET EDO D 355 4
HET EDO D 356 4
HET EDO D 357 4
HET EDO D 358 4
HET NO3 D 359 4
HET EDO D 360 8
HET NA D 361 1
HETNAM ZN ZINC ION
HETNAM CAC CACODYLATE ION
HETNAM OXY OXYGEN MOLECULE
HETNAM EDO 1,2-ETHANEDIOL
HETNAM NO3 NITRATE ION
HETNAM IMD IMIDAZOLE
HETNAM NA SODIUM ION
HETSYN CAC DIMETHYLARSINATE
HETSYN EDO ETHYLENE GLYCOL
FORMUL 5 ZN 4(ZN 2+)
FORMUL 6 CAC 4(C2 H6 AS O2 1-)
FORMUL 7 OXY O2
FORMUL 10 EDO 14(C2 H6 O2)
FORMUL 12 NO3 2(N O3 1-)
FORMUL 17 IMD C3 H5 N2 1+
FORMUL 23 NA 2(NA 1+)
FORMUL 33 HOH *1988(H2 O)
HELIX 1 1 CYS A 37 GLU A 46 1 10
HELIX 2 2 THR A 92 ARG A 97 1 6
HELIX 3 3 TYR A 99 SER A 103 5 5
HELIX 4 4 ASP A 128 LEU A 133 1 6
HELIX 5 5 PRO A 141 VAL A 146 1 6
HELIX 6 6 ASP A 150 ALA A 162 1 13
HELIX 7 7 GLY A 176 HIS A 188 1 13
HELIX 8 8 ARG A 200 GLY A 211 1 12
HELIX 9 9 ASN A 217 GLY A 221 5 5
HELIX 10 10 ASP A 222 THR A 231 1 10
HELIX 11 11 HIS A 247 MET A 255 1 9
HELIX 12 12 TRP A 281 MET A 285 5 5
HELIX 13 13 GLY A 297 TYR A 311 1 15
HELIX 14 14 ASP A 315 LYS A 318 5 4
HELIX 15 15 ASP A 328 ASP A 339 1 12
HELIX 16 16 CYS B 37 GLU B 46 1 10
HELIX 17 17 THR B 92 ARG B 97 1 6
HELIX 18 18 TYR B 99 SER B 103 5 5
HELIX 19 19 ASP B 128 LEU B 133 1 6
HELIX 20 20 PRO B 141 VAL B 146 1 6
HELIX 21 21 ASP B 150 ALA B 162 1 13
HELIX 22 22 GLY B 176 HIS B 188 1 13
HELIX 23 23 ARG B 200 GLY B 211 1 12
HELIX 24 24 ASN B 217 GLY B 221 5 5
HELIX 25 25 ASP B 222 THR B 231 1 10
HELIX 26 26 HIS B 247 MET B 255 1 9
HELIX 27 27 TRP B 281 MET B 285 5 5
HELIX 28 28 GLY B 297 TYR B 311 1 15
HELIX 29 29 ASP B 315 LYS B 318 5 4
HELIX 30 30 ASN B 329 ASP B 339 1 11
HELIX 31 31 CYS C 37 GLU C 46 1 10
HELIX 32 32 THR C 92 ARG C 97 1 6
HELIX 33 33 TYR C 99 SER C 103 5 5
HELIX 34 34 ASP C 128 LEU C 133 1 6
HELIX 35 35 PRO C 141 VAL C 146 1 6
HELIX 36 36 ASP C 150 ALA C 162 1 13
HELIX 37 37 GLY C 176 LEU C 189 1 14
HELIX 38 38 ARG C 200 TYR C 210 1 11
HELIX 39 39 ASN C 217 GLY C 221 5 5
HELIX 40 40 ASP C 222 THR C 231 1 10
HELIX 41 41 HIS C 247 MET C 255 1 9
HELIX 42 42 TRP C 281 MET C 285 5 5
HELIX 43 43 GLY C 297 TYR C 311 1 15
HELIX 44 44 ASP C 315 LYS C 318 5 4
HELIX 45 45 ASN C 329 LYS C 340 1 12
HELIX 46 46 CYS D 37 GLU D 46 1 10
HELIX 47 47 THR D 92 ARG D 97 1 6
HELIX 48 48 TYR D 99 SER D 103 5 5
HELIX 49 49 ASP D 128 LEU D 133 1 6
HELIX 50 50 PRO D 141 VAL D 146 1 6
HELIX 51 51 ASP D 150 ALA D 162 1 13
HELIX 52 52 GLY D 176 LEU D 189 1 14
HELIX 53 53 ARG D 200 GLY D 211 1 12
HELIX 54 54 ASN D 217 GLY D 221 5 5
HELIX 55 55 ASP D 222 THR D 231 1 10
HELIX 56 56 HIS D 247 MET D 255 1 9
HELIX 57 57 TRP D 281 MET D 285 5 5
HELIX 58 58 GLY D 297 TYR D 311 1 15
HELIX 59 59 ASP D 315 LYS D 318 5 4
HELIX 60 60 ASN D 329 ASP D 339 1 11
SHEET 1 A 3 LYS A 11 GLU A 16 0
SHEET 2 A 3 LYS A 2 SER A 8 -1 N ALA A 5 O GLY A 13
SHEET 3 A 3 MET A 55 ILE A 56 -1 O MET A 55 N MET A 6
SHEET 1 B 5 PHE A 124 VAL A 126 0
SHEET 2 B 5 ALA A 27 ALA A 35 -1 N ALA A 27 O VAL A 126
SHEET 3 B 5 GLU A 60 VAL A 68 -1 O VAL A 62 N LEU A 32
SHEET 4 B 5 ARG A 80 VAL A 83 -1 O VAL A 81 N GLY A 63
SHEET 5 B 5 ALA A 134 HIS A 135 -1 O ALA A 134 N VAL A 82
SHEET 1 C 4 PHE A 124 VAL A 126 0
SHEET 2 C 4 ALA A 27 ALA A 35 -1 N ALA A 27 O VAL A 126
SHEET 3 C 4 LYS A 346 ILE A 350 -1 O VAL A 349 N VAL A 34
SHEET 4 C 4 VAL A 320 ARG A 325 1 N PHE A 324 O ILE A 350
SHEET 1 D 6 ASP A 214 ILE A 216 0
SHEET 2 D 6 ILE A 194 VAL A 197 1 N ALA A 196 O ILE A 216
SHEET 3 D 6 VAL A 170 ILE A 173 1 N VAL A 170 O PHE A 195
SHEET 4 D 6 VAL A 236 ILE A 241 1 O VAL A 240 N ILE A 173
SHEET 5 D 6 ILE A 256 ASN A 264 1 O GLY A 263 N VAL A 239
SHEET 6 D 6 LYS A 288 GLY A 292 1 O HIS A 291 N ASN A 264
SHEET 1 E 2 ASN A 273 PRO A 277 0
SHEET 2 E 2 ASN C 273 PRO C 277 -1 O ILE C 276 N ILE A 274
SHEET 1 F 3 LYS B 11 GLU B 16 0
SHEET 2 F 3 LYS B 2 SER B 8 -1 N ALA B 5 O GLY B 13
SHEET 3 F 3 MET B 55 ILE B 56 -1 O MET B 55 N MET B 6
SHEET 1 G 5 PHE B 124 VAL B 126 0
SHEET 2 G 5 ALA B 27 ALA B 35 -1 N ALA B 27 O VAL B 126
SHEET 3 G 5 GLU B 60 VAL B 68 -1 O VAL B 62 N LEU B 32
SHEET 4 G 5 ARG B 80 VAL B 83 -1 O VAL B 81 N GLY B 63
SHEET 5 G 5 ALA B 134 HIS B 135 -1 O ALA B 134 N VAL B 82
SHEET 1 H 4 PHE B 124 VAL B 126 0
SHEET 2 H 4 ALA B 27 ALA B 35 -1 N ALA B 27 O VAL B 126
SHEET 3 H 4 LYS B 346 ILE B 350 -1 O VAL B 349 N VAL B 34
SHEET 4 H 4 VAL B 320 ARG B 325 1 N PHE B 324 O ILE B 350
SHEET 1 I 6 ASP B 214 ILE B 216 0
SHEET 2 I 6 ILE B 194 VAL B 197 1 N ALA B 196 O ILE B 216
SHEET 3 I 6 VAL B 170 ILE B 173 1 N VAL B 172 O VAL B 197
SHEET 4 I 6 VAL B 236 ILE B 241 1 O VAL B 240 N ILE B 173
SHEET 5 I 6 ILE B 256 ASN B 264 1 O GLY B 263 N VAL B 239
SHEET 6 I 6 LYS B 288 GLY B 292 1 O HIS B 291 N ASN B 264
SHEET 1 J 2 ASN B 273 PRO B 277 0
SHEET 2 J 2 ASN D 273 PRO D 277 -1 O ILE D 276 N ILE B 274
SHEET 1 K 3 LYS C 11 GLU C 16 0
SHEET 2 K 3 LYS C 2 SER C 8 -1 N ALA C 5 O GLY C 13
SHEET 3 K 3 MET C 55 ILE C 56 -1 O MET C 55 N MET C 6
SHEET 1 L 5 PHE C 124 VAL C 126 0
SHEET 2 L 5 ALA C 27 ALA C 35 -1 N ALA C 27 O VAL C 126
SHEET 3 L 5 GLU C 60 VAL C 68 -1 O VAL C 62 N LEU C 32
SHEET 4 L 5 ARG C 80 VAL C 83 -1 O VAL C 81 N GLY C 63
SHEET 5 L 5 ALA C 134 HIS C 135 -1 O ALA C 134 N VAL C 82
SHEET 1 M 4 PHE C 124 VAL C 126 0
SHEET 2 M 4 ALA C 27 ALA C 35 -1 N ALA C 27 O VAL C 126
SHEET 3 M 4 LYS C 346 ILE C 350 -1 O VAL C 349 N VAL C 34
SHEET 4 M 4 VAL C 320 ARG C 325 1 N PHE C 324 O ILE C 350
SHEET 1 N 6 ASP C 214 ILE C 216 0
SHEET 2 N 6 ILE C 194 VAL C 197 1 N ALA C 196 O ILE C 216
SHEET 3 N 6 VAL C 170 ILE C 173 1 N VAL C 170 O PHE C 195
SHEET 4 N 6 VAL C 236 ILE C 241 1 O VAL C 240 N ILE C 173
SHEET 5 N 6 ILE C 256 ASN C 264 1 O GLY C 263 N VAL C 239
SHEET 6 N 6 LYS C 288 GLY C 292 1 O HIS C 291 N ASN C 264
SHEET 1 O 3 LYS D 11 GLU D 16 0
SHEET 2 O 3 LYS D 2 SER D 8 -1 N GLY D 3 O ILE D 15
SHEET 3 O 3 MET D 55 ILE D 56 -1 O MET D 55 N MET D 6
SHEET 1 P 5 PHE D 124 VAL D 126 0
SHEET 2 P 5 ALA D 27 ALA D 35 -1 N ALA D 27 O VAL D 126
SHEET 3 P 5 GLU D 60 VAL D 68 -1 O VAL D 62 N LEU D 32
SHEET 4 P 5 ARG D 80 VAL D 83 -1 O VAL D 81 N GLY D 63
SHEET 5 P 5 ALA D 134 HIS D 135 -1 O ALA D 134 N VAL D 82
SHEET 1 Q 4 PHE D 124 VAL D 126 0
SHEET 2 Q 4 ALA D 27 ALA D 35 -1 N ALA D 27 O VAL D 126
SHEET 3 Q 4 LYS D 346 ILE D 350 -1 O VAL D 349 N VAL D 34
SHEET 4 Q 4 VAL D 320 ARG D 325 1 N PHE D 324 O ILE D 350
SHEET 1 R 6 ASP D 214 ILE D 216 0
SHEET 2 R 6 ILE D 194 VAL D 197 1 N ALA D 196 O ILE D 216
SHEET 3 R 6 VAL D 170 ILE D 173 1 N VAL D 170 O PHE D 195
SHEET 4 R 6 VAL D 236 ILE D 241 1 O VAL D 240 N ILE D 173
SHEET 5 R 6 ILE D 256 ASN D 264 1 O GLY D 263 N VAL D 239
SHEET 6 R 6 LYS D 288 GLY D 292 1 O HIS D 291 N ASN D 264
LINK SG CYS A 37 ZN ZN A 353 1555 1555 2.25
LINK NE2 HIS A 59 ZN ZN A 353 1555 1555 2.04
LINK OD2 ASP A 150 ZN ZN A 353 1555 1555 1.96
LINK ZN ZN A 353 O2 CAC A 354 1555 1555 1.95
LINK SG CYS B 37 ZN ZN B 353 1555 1555 2.26
LINK NE2 HIS B 59 ZN ZN B 353 1555 1555 2.02
LINK OD2 ASP B 150 ZN ZN B 353 1555 1555 1.97
LINK ZN ZN B 353 O1 CAC B 354 1555 1555 1.96
LINK SG CYS C 37 ZN ZN C 353 1555 1555 2.26
LINK NE2 HIS C 59 ZN ZN C 353 1555 1555 2.02
LINK O ASER C 103 NA NA C 361 1555 1555 2.75
LINK O BSER C 103 NA NA C 361 1555 1555 2.74
LINK OG BSER C 103 NA NA C 361 1555 1555 2.16
LINK O ALA C 108 NA NA C 361 1555 1555 2.96
LINK NZ LYS C 111 NA NA C 361 1555 1555 2.76
LINK OD2 ASP C 150 ZN ZN C 353 1555 1555 1.97
LINK ZN ZN C 353 O2 CAC C 354 1555 1555 1.96
LINK NA NA C 361 O HOH C 754 1555 1555 2.60
LINK SG CYS D 37 ZN ZN D 353 1555 1555 2.26
LINK NE2 HIS D 59 ZN ZN D 353 1555 1555 2.07
LINK N ASP D 89 NA NA D 361 1555 1555 2.98
LINK O ASER D 103 NA NA D 361 1555 1555 2.70
LINK O BSER D 103 NA NA D 361 1555 1555 2.77
LINK OG BSER D 103 NA NA D 361 1555 1555 2.17
LINK O ALA D 108 NA NA D 361 1555 1555 2.98
LINK NZ LYS D 111 NA NA D 361 1555 1555 2.99
LINK OD2 ASP D 150 ZN ZN D 353 1555 1555 1.93
LINK ZN ZN D 353 O2 CAC D 354 1555 1555 1.92
LINK NA NA D 361 O HOH D2019 1555 1555 2.75
SITE 1 AC1 4 CYS A 37 HIS A 59 ASP A 150 CAC A 354
SITE 1 AC2 10 CYS A 37 SER A 39 HIS A 59 ILE A 86
SITE 2 AC2 10 ASP A 150 THR A 154 ZN A 353 HOH A 366
SITE 3 AC2 10 HOH A2038 MET C 285
SITE 1 AC3 4 LYS A 238 HOH A 417 HOH A 764 HOH A1853
SITE 1 AC4 4 CYS B 37 HIS B 59 ASP B 150 CAC B 354
SITE 1 AC5 9 CYS B 37 SER B 39 HIS B 59 ILE B 86
SITE 2 AC5 9 ASP B 150 THR B 154 ZN B 353 HOH B 371
SITE 3 AC5 9 MET D 285
SITE 1 AC6 8 GLY B 98 TYR B 99 GLN B 101 HIS B 157
SITE 2 AC6 8 HOH B 466 HOH B 832 HOH B1180 HOH B1526
SITE 1 AC7 5 PRO B 137 ASP B 307 PHE B 310 HOH B 663
SITE 2 AC7 5 HOH B1756
SITE 1 AC8 5 PHE B 25 ARG B 91 HOH B 392 HOH B1019
SITE 2 AC8 5 HOH B1059
SITE 1 AC9 8 THR B 169 ARG B 193 EDO B 359 HOH B 708
SITE 2 AC9 8 HOH B1069 ASP C 307 EDO C 356 HOH C 478
SITE 1 BC1 10 THR B 169 THR B 231 LYS B 234 GLY B 235
SITE 2 BC1 10 VAL B 236 ASP B 237 LYS B 257 EDO B 358
SITE 3 BC1 10 HOH B1069 ARG C 304
SITE 1 BC2 4 CYS C 37 HIS C 59 ASP C 150 CAC C 354
SITE 1 BC3 10 MET A 285 CYS C 37 SER C 39 HIS C 59
SITE 2 BC3 10 ILE C 86 ASP C 150 THR C 154 ZN C 353
SITE 3 BC3 10 EDO C 357 HOH C 372
SITE 1 BC4 8 PHE C 25 ARG C 91 ASP C 128 HOH C 384
SITE 2 BC4 8 HOH C 590 HOH C1222 HOH C1495 ARG D 91
SITE 1 BC5 5 EDO B 358 ASP C 307 PHE C 310 HOH C 478
SITE 2 BC5 5 HOH C1107
SITE 1 BC6 9 THR C 38 SER C 39 VAL C 265 ASN C 266
SITE 2 BC6 9 TYR C 267 CAC C 354 HOH C 626 HOH C 691
SITE 3 BC6 9 HOH C 997
SITE 1 BC7 5 ASP C 272 ASN C 273 HOH C 516 HOH C 943
SITE 2 BC7 5 HOH C1471
SITE 1 BC8 6 TYR C 99 GLN C 101 HIS C 157 HOH C 458
SITE 2 BC8 6 HOH C 487 HOH C 546
SITE 1 BC9 5 LEU B 166 ARG C 301 ARG C 304 HOH C 678
SITE 2 BC9 5 HOH C2058
SITE 1 CC1 6 ASP C 89 SER C 103 ALA C 108 GLY C 109
SITE 2 CC1 6 LYS C 111 HOH C 754
SITE 1 CC2 5 CYS D 37 SER D 39 HIS D 59 ASP D 150
SITE 2 CC2 5 CAC D 354
SITE 1 CC3 8 MET B 285 CYS D 37 SER D 39 HIS D 59
SITE 2 CC3 8 ASP D 150 THR D 154 ZN D 353 HOH D 377
SITE 1 CC4 6 GLY D 98 GLN D 101 HIS D 157 HOH D 398
SITE 2 CC4 6 HOH D 959 HOH D1626
SITE 1 CC5 9 GLY A 167 LYS A 234 HOH A1792 LEU D 300
SITE 2 CC5 9 GLU D 303 ARG D 304 ASP D 307 HOH D 506
SITE 3 CC5 9 HOH D 822
SITE 1 CC6 4 ASP D 307 PHE D 310 HOH D 511 HOH D1577
SITE 1 CC7 5 LEU A 166 ARG D 301 ARG D 304 HOH D 918
SITE 2 CC7 5 HOH D1116
SITE 1 CC8 6 ARG C 91 PHE D 25 ARG D 91 HOH D 376
SITE 2 CC8 6 HOH D 634 HOH D1200
SITE 1 CC9 10 THR D 38 SER D 39 HIS D 42 VAL D 178
SITE 2 CC9 10 VAL D 265 ASN D 266 TYR D 267 HOH D 817
SITE 3 CC9 10 HOH D 973 HOH D1209
SITE 1 DC1 7 PRO D 88 ASP D 89 SER D 103 ALA D 108
SITE 2 DC1 7 GLY D 109 LYS D 111 HOH D2019
CRYST1 79.742 82.429 118.249 90.00 99.89 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 0.012540 0.000000 0.002186 0.00000
SCALE2 0.000000 0.012132 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008584 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
