HEADER OXIDOREDUCTASE (SUPEROXIDE ACCEPTOR) 11-FEB-92 1SOS
TITLE ATOMIC STRUCTURES OF WILD-TYPE AND THERMOSTABLE MUTANT
TITLE 2 RECOMBINANT HUMAN CU, ZN SUPEROXIDE DISMUTASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SUPEROXIDE DISMUTASE;
COMPND 3 CHAIN: A, F, B, G, C, H, D, I, E, J;
COMPND 4 EC: 1.15.1.1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606
KEYWDS OXIDOREDUCTASE (SUPEROXIDE ACCEPTOR)
EXPDTA X-RAY DIFFRACTION
AUTHOR H.E.PARGE,R.A.HALLEWELL,J.A.TAINER
REVDAT 3 24-FEB-09 1SOS 1 VERSN
REVDAT 2 31-JUL-94 1SOS 1 SHEET
REVDAT 1 15-APR-93 1SOS 0
JRNL AUTH H.E.PARGE,R.A.HALLEWELL,J.A.TAINER
JRNL TITL ATOMIC STRUCTURES OF WILD-TYPE AND THERMOSTABLE
JRNL TITL 2 MUTANT RECOMBINANT HUMAN CU,ZN SUPEROXIDE
JRNL TITL 3 DISMUTASE.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 89 6109 1992
JRNL REFN ISSN 0027-8424
JRNL PMID 1463506
JRNL DOI 10.1073/PNAS.89.13.6109
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : NULL
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : NULL
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.202
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 11120
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 30
REMARK 3 SOLVENT ATOMS : 499
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.017
REMARK 3 BOND ANGLES (DEGREES) : 3.50
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1SOS COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : NULL
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 68.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.94
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 72.75000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 72.75000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 102.60000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 83.50000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 102.60000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 83.50000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 72.75000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 102.60000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 83.50000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 72.75000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 102.60000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 83.50000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5
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: 1900 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13630 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -37.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: 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: 1990 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13750 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, G
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: 1890 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13830 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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 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: 2100 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13680 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -47.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, I
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: 5
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: 1910 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13620 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -37.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, J
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: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 HIS A 43 NE2 HIS A 43 CD2 -0.073
REMARK 500 HIS A 48 NE2 HIS A 48 CD2 -0.078
REMARK 500 HIS A 71 NE2 HIS A 71 CD2 -0.071
REMARK 500 HIS A 80 NE2 HIS A 80 CD2 -0.080
REMARK 500 HIS A 110 NE2 HIS A 110 CD2 -0.069
REMARK 500 HIS A 120 NE2 HIS A 120 CD2 -0.072
REMARK 500 HIS F 46 NE2 HIS F 46 CD2 -0.072
REMARK 500 HIS F 48 NE2 HIS F 48 CD2 -0.075
REMARK 500 HIS F 71 NE2 HIS F 71 CD2 -0.074
REMARK 500 HIS F 80 NE2 HIS F 80 CD2 -0.079
REMARK 500 HIS F 110 NE2 HIS F 110 CD2 -0.077
REMARK 500 HIS F 120 NE2 HIS F 120 CD2 -0.074
REMARK 500 HIS B 43 NE2 HIS B 43 CD2 -0.071
REMARK 500 HIS B 46 NE2 HIS B 46 CD2 -0.087
REMARK 500 HIS B 63 NE2 HIS B 63 CD2 -0.073
REMARK 500 HIS B 71 NE2 HIS B 71 CD2 -0.091
REMARK 500 HIS G 43 NE2 HIS G 43 CD2 -0.088
REMARK 500 HIS G 46 NE2 HIS G 46 CD2 -0.074
REMARK 500 HIS G 63 NE2 HIS G 63 CD2 -0.078
REMARK 500 HIS G 71 NE2 HIS G 71 CD2 -0.079
REMARK 500 HIS G 80 NE2 HIS G 80 CD2 -0.072
REMARK 500 HIS G 110 NE2 HIS G 110 CD2 -0.079
REMARK 500 HIS G 120 NE2 HIS G 120 CD2 -0.072
REMARK 500 HIS C 43 NE2 HIS C 43 CD2 -0.078
REMARK 500 HIS C 46 NE2 HIS C 46 CD2 -0.071
REMARK 500 HIS C 71 NE2 HIS C 71 CD2 -0.092
REMARK 500 HIS C 80 NE2 HIS C 80 CD2 -0.085
REMARK 500 HIS C 120 NE2 HIS C 120 CD2 -0.073
REMARK 500 HIS H 43 NE2 HIS H 43 CD2 -0.068
REMARK 500 HIS H 46 NE2 HIS H 46 CD2 -0.068
REMARK 500 HIS H 71 NE2 HIS H 71 CD2 -0.078
REMARK 500 HIS H 80 NE2 HIS H 80 CD2 -0.076
REMARK 500 HIS H 110 NE2 HIS H 110 CD2 -0.079
REMARK 500 HIS D 43 NE2 HIS D 43 CD2 -0.075
REMARK 500 HIS D 46 NE2 HIS D 46 CD2 -0.072
REMARK 500 HIS D 48 NE2 HIS D 48 CD2 -0.068
REMARK 500 HIS D 71 NE2 HIS D 71 CD2 -0.095
REMARK 500 HIS D 80 NE2 HIS D 80 CD2 -0.083
REMARK 500 HIS D 120 NE2 HIS D 120 CD2 -0.072
REMARK 500 HIS I 43 NE2 HIS I 43 CD2 -0.070
REMARK 500 HIS I 46 NE2 HIS I 46 CD2 -0.083
REMARK 500 HIS I 48 NE2 HIS I 48 CD2 -0.069
REMARK 500 HIS I 71 NE2 HIS I 71 CD2 -0.079
REMARK 500 HIS I 80 NE2 HIS I 80 CD2 -0.071
REMARK 500 HIS I 110 NE2 HIS I 110 CD2 -0.072
REMARK 500 HIS I 120 NE2 HIS I 120 CD2 -0.084
REMARK 500 HIS E 71 NE2 HIS E 71 CD2 -0.077
REMARK 500 HIS E 80 NE2 HIS E 80 CD2 -0.074
REMARK 500 HIS E 110 NE2 HIS E 110 CD2 -0.071
REMARK 500 HIS J 43 NE2 HIS J 43 CD2 -0.070
REMARK 500
REMARK 500 THIS ENTRY HAS 54 BOND DEVIATIONS.
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 TRP A 32 CD1 - CG - CD2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 TRP A 32 CE2 - CD2 - CG ANGL. DEV. = -5.4 DEGREES
REMARK 500 ARG A 69 CB - CG - CD ANGL. DEV. = -17.2 DEGREES
REMARK 500 ARG A 69 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG A 69 NE - CZ - NH2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 ARG A 79 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 GLU A 100 N - CA - C ANGL. DEV. = -18.6 DEGREES
REMARK 500 ARG A 115 NE - CZ - NH1 ANGL. DEV. = 4.8 DEGREES
REMARK 500 TRP F 32 CD1 - CG - CD2 ANGL. DEV. = 5.4 DEGREES
REMARK 500 TRP F 32 CE2 - CD2 - CG ANGL. DEV. = -5.0 DEGREES
REMARK 500 ARG F 79 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG F 79 NE - CZ - NH2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 HIS F 80 CA - CB - CG ANGL. DEV. = 11.2 DEGREES
REMARK 500 ARG F 115 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG F 143 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 CYS F 146 CA - CB - SG ANGL. DEV. = 6.6 DEGREES
REMARK 500 VAL B 14 CG1 - CB - CG2 ANGL. DEV. = -10.9 DEGREES
REMARK 500 TRP B 32 CD1 - CG - CD2 ANGL. DEV. = 6.6 DEGREES
REMARK 500 TRP B 32 CB - CG - CD1 ANGL. DEV. = -8.2 DEGREES
REMARK 500 TRP B 32 CE2 - CD2 - CG ANGL. DEV. = -5.8 DEGREES
REMARK 500 TRP B 32 CG - CD2 - CE3 ANGL. DEV. = 5.6 DEGREES
REMARK 500 LYS B 70 CA - CB - CG ANGL. DEV. = -13.4 DEGREES
REMARK 500 ARG B 79 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ASP B 83 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ARG B 143 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 TRP G 32 CD1 - CG - CD2 ANGL. DEV. = 6.5 DEGREES
REMARK 500 TRP G 32 CE2 - CD2 - CG ANGL. DEV. = -6.0 DEGREES
REMARK 500 ARG G 115 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 GLU G 133 N - CA - CB ANGL. DEV. = -11.3 DEGREES
REMARK 500 ARG G 143 NE - CZ - NH1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 ARG G 143 NE - CZ - NH2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 TRP C 32 CD1 - CG - CD2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 TRP C 32 CE2 - CD2 - CG ANGL. DEV. = -5.7 DEGREES
REMARK 500 ARG C 79 NE - CZ - NH1 ANGL. DEV. = 7.4 DEGREES
REMARK 500 ARG C 79 NE - CZ - NH2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 ASP C 83 CB - CG - OD1 ANGL. DEV. = 7.4 DEGREES
REMARK 500 ASP C 83 CB - CG - OD2 ANGL. DEV. = -6.4 DEGREES
REMARK 500 VAL C 118 CG1 - CB - CG2 ANGL. DEV. = -10.2 DEGREES
REMARK 500 TRP H 32 CD1 - CG - CD2 ANGL. DEV. = 6.8 DEGREES
REMARK 500 TRP H 32 CB - CG - CD1 ANGL. DEV. = -8.9 DEGREES
REMARK 500 TRP H 32 CE2 - CD2 - CG ANGL. DEV. = -5.9 DEGREES
REMARK 500 TRP H 32 CG - CD2 - CE3 ANGL. DEV. = 6.6 DEGREES
REMARK 500 ARG H 79 NE - CZ - NH1 ANGL. DEV. = 6.6 DEGREES
REMARK 500 ARG H 79 NE - CZ - NH2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 TRP D 32 CD1 - CG - CD2 ANGL. DEV. = 5.2 DEGREES
REMARK 500 TRP D 32 CE2 - CD2 - CG ANGL. DEV. = -5.1 DEGREES
REMARK 500 ARG D 69 NE - CZ - NH1 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ARG D 69 NE - CZ - NH2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 ARG D 115 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 LYS I 30 CA - CB - CG ANGL. DEV. = 15.0 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 70 ANGLE DEVIATIONS.
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 125 21.64 -77.18
REMARK 500 LEU A 126 27.89 43.64
REMARK 500 ASN A 131 160.58 171.47
REMARK 500 ASP F 90 -170.32 -68.51
REMARK 500 GLU B 40 129.77 -33.39
REMARK 500 ALA B 55 31.63 -86.62
REMARK 500 SER B 68 61.29 32.01
REMARK 500 ARG B 69 -169.34 -105.44
REMARK 500 LYS B 128 45.16 -96.20
REMARK 500 ALA G 55 36.94 -90.98
REMARK 500 SER G 68 58.93 39.56
REMARK 500 ARG G 69 -167.82 -105.92
REMARK 500 ASP C 90 -172.95 -64.46
REMARK 500 SER C 98 89.33 -158.02
REMARK 500 LYS C 136 -61.23 -104.64
REMARK 500 ASP H 92 4.24 -66.09
REMARK 500 ASP H 125 31.97 -87.51
REMARK 500 LEU H 126 20.09 37.92
REMARK 500 SER D 25 -36.41 -12.10
REMARK 500 ASN D 26 28.15 -153.77
REMARK 500 ALA D 55 47.76 -94.26
REMARK 500 SER D 68 70.67 29.96
REMARK 500 LYS D 91 -5.56 -59.09
REMARK 500 SER D 98 107.33 -165.27
REMARK 500 LEU D 126 19.65 48.97
REMARK 500 ASN D 131 162.38 175.47
REMARK 500 ALA I 55 50.27 -112.08
REMARK 500 ASN I 65 69.08 -150.75
REMARK 500 ASP I 90 -167.40 -73.74
REMARK 500 LYS I 136 -60.14 -107.68
REMARK 500 SER E 25 -34.85 -30.57
REMARK 500 PHE E 64 109.59 -57.16
REMARK 500 SER E 68 73.34 40.12
REMARK 500 ASP E 90 176.85 -59.97
REMARK 500 VAL E 103 -45.27 -148.87
REMARK 500 LYS E 128 36.83 -72.40
REMARK 500 LYS E 136 -76.64 -102.71
REMARK 500 GLU J 24 123.31 158.05
REMARK 500 SER J 25 -25.78 -25.33
REMARK 500 ASN J 26 44.64 -159.01
REMARK 500 ASN J 53 61.99 -105.81
REMARK 500 ALA J 55 49.21 -102.67
REMARK 500 SER J 59 6.62 -67.96
REMARK 500 ASP J 92 64.75 -103.74
REMARK 500 VAL J 103 -32.72 -148.82
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLY D 12 PRO D 13 -129.84
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH D 156 DISTANCE = 8.59 ANGSTROMS
REMARK 525 HOH G 156 DISTANCE = 5.15 ANGSTROMS
REMARK 525 HOH B 157 DISTANCE = 5.65 ANGSTROMS
REMARK 525 HOH D 159 DISTANCE = 17.57 ANGSTROMS
REMARK 525 HOH E 160 DISTANCE = 5.29 ANGSTROMS
REMARK 525 HOH F 361 DISTANCE = 6.07 ANGSTROMS
REMARK 525 HOH A 161 DISTANCE = 7.43 ANGSTROMS
REMARK 525 HOH C 162 DISTANCE = 10.21 ANGSTROMS
REMARK 525 HOH G 162 DISTANCE = 5.84 ANGSTROMS
REMARK 525 HOH J 162 DISTANCE = 6.08 ANGSTROMS
REMARK 525 HOH C 164 DISTANCE = 5.42 ANGSTROMS
REMARK 525 HOH C 166 DISTANCE = 6.06 ANGSTROMS
REMARK 525 HOH H 167 DISTANCE = 5.12 ANGSTROMS
REMARK 525 HOH E 168 DISTANCE = 5.27 ANGSTROMS
REMARK 525 HOH F 369 DISTANCE = 5.71 ANGSTROMS
REMARK 525 HOH A 169 DISTANCE = 8.41 ANGSTROMS
REMARK 525 HOH C 170 DISTANCE = 7.01 ANGSTROMS
REMARK 525 HOH D 170 DISTANCE = 6.43 ANGSTROMS
REMARK 525 HOH I 372 DISTANCE = 5.75 ANGSTROMS
REMARK 525 HOH D 172 DISTANCE = 6.27 ANGSTROMS
REMARK 525 HOH H 172 DISTANCE = 5.27 ANGSTROMS
REMARK 525 HOH D 173 DISTANCE = 6.21 ANGSTROMS
REMARK 525 HOH I 375 DISTANCE = 5.69 ANGSTROMS
REMARK 525 HOH B 174 DISTANCE = 5.22 ANGSTROMS
REMARK 525 HOH C 174 DISTANCE = 5.92 ANGSTROMS
REMARK 525 HOH H 175 DISTANCE = 5.07 ANGSTROMS
REMARK 525 HOH B 176 DISTANCE = 7.44 ANGSTROMS
REMARK 525 HOH H 177 DISTANCE = 5.83 ANGSTROMS
REMARK 525 HOH E 179 DISTANCE = 6.15 ANGSTROMS
REMARK 525 HOH H 179 DISTANCE = 5.34 ANGSTROMS
REMARK 525 HOH D 180 DISTANCE = 5.90 ANGSTROMS
REMARK 525 HOH G 180 DISTANCE = 5.50 ANGSTROMS
REMARK 525 HOH F 383 DISTANCE = 7.45 ANGSTROMS
REMARK 525 HOH D 183 DISTANCE = 6.88 ANGSTROMS
REMARK 525 HOH C 184 DISTANCE = 5.54 ANGSTROMS
REMARK 525 HOH C 186 DISTANCE = 5.96 ANGSTROMS
REMARK 525 HOH G 188 DISTANCE = 7.23 ANGSTROMS
REMARK 525 HOH E 190 DISTANCE = 5.81 ANGSTROMS
REMARK 525 HOH H 191 DISTANCE = 7.37 ANGSTROMS
REMARK 525 HOH G 193 DISTANCE = 5.53 ANGSTROMS
REMARK 525 HOH H 193 DISTANCE = 6.11 ANGSTROMS
REMARK 525 HOH B 194 DISTANCE = 7.24 ANGSTROMS
REMARK 525 HOH D 195 DISTANCE = 5.09 ANGSTROMS
REMARK 525 HOH G 195 DISTANCE = 5.86 ANGSTROMS
REMARK 525 HOH A 196 DISTANCE = 6.04 ANGSTROMS
REMARK 525 HOH B 202 DISTANCE = 7.33 ANGSTROMS
REMARK 525 HOH B 208 DISTANCE = 5.31 ANGSTROMS
REMARK 525 HOH B 209 DISTANCE = 6.15 ANGSTROMS
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 CU A 154 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 48 NE2
REMARK 620 2 HIS A 63 NE2 100.5
REMARK 620 3 HIS A 120 NE2 108.1 151.2
REMARK 620 4 HIS A 46 ND1 131.9 72.9 85.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 155 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 71 ND1
REMARK 620 2 ASP A 83 OD1 84.8
REMARK 620 3 HIS A 63 ND1 105.0 116.8
REMARK 620 4 HIS A 80 ND1 112.4 111.4 120.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU B 154 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 63 NE2
REMARK 620 2 HIS B 120 NE2 152.4
REMARK 620 3 HIS B 48 NE2 102.0 102.3
REMARK 620 4 HIS B 46 ND1 84.1 89.0 132.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 155 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 80 ND1
REMARK 620 2 ASP B 83 OD1 100.8
REMARK 620 3 HIS B 63 ND1 109.7 106.0
REMARK 620 4 HIS B 71 ND1 132.4 106.3 99.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU C 154 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 48 NE2
REMARK 620 2 HIS C 120 NE2 110.9
REMARK 620 3 HIS C 46 ND1 142.6 94.7
REMARK 620 4 HIS C 63 NE2 96.6 144.9 74.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 155 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 71 ND1
REMARK 620 2 ASP C 83 OD1 89.6
REMARK 620 3 HIS C 80 ND1 111.0 98.4
REMARK 620 4 HIS C 63 ND1 106.8 132.7 115.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU D 154 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 46 ND1
REMARK 620 2 HIS D 48 NE2 142.6
REMARK 620 3 HIS D 63 NE2 75.3 97.7
REMARK 620 4 HIS D 120 NE2 95.4 105.4 151.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 155 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 63 ND1
REMARK 620 2 HIS D 71 ND1 107.9
REMARK 620 3 HIS D 80 ND1 112.4 116.4
REMARK 620 4 ASP D 83 OD1 117.2 91.1 110.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU E 154 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS E 48 NE2
REMARK 620 2 HIS E 46 ND1 135.1
REMARK 620 3 HIS E 120 NE2 105.6 92.2
REMARK 620 4 HIS E 63 NE2 95.6 86.3 151.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN E 155 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS E 80 ND1
REMARK 620 2 HIS E 71 ND1 112.0
REMARK 620 3 ASP E 83 OD2 76.3 68.6
REMARK 620 4 HIS E 63 ND1 117.0 118.4 156.1
REMARK 620 5 ASP E 83 OD1 101.3 102.9 54.7 101.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU F 154 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS F 48 NE2
REMARK 620 2 HIS F 63 NE2 89.8
REMARK 620 3 HIS F 120 NE2 108.7 157.7
REMARK 620 4 HIS F 46 ND1 132.0 83.2 92.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN F 155 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP F 83 OD1
REMARK 620 2 HIS F 71 ND1 103.1
REMARK 620 3 HIS F 63 ND1 114.6 111.2
REMARK 620 4 HIS F 80 ND1 101.9 112.9 112.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU G 154 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS G 48 NE2
REMARK 620 2 HIS G 120 NE2 99.4
REMARK 620 3 HIS G 63 NE2 94.6 165.2
REMARK 620 4 HIS G 46 ND1 132.7 96.1 77.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN G 155 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP G 83 OD1
REMARK 620 2 HIS G 63 ND1 102.8
REMARK 620 3 ASP G 83 OD2 52.2 155.0
REMARK 620 4 HIS G 80 ND1 107.3 109.4 81.3
REMARK 620 5 HIS G 71 ND1 101.9 112.4 78.1 121.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU H 154 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS H 46 ND1
REMARK 620 2 HIS H 48 NE2 137.4
REMARK 620 3 HIS H 120 NE2 93.1 105.8
REMARK 620 4 HIS H 63 NE2 75.1 94.8 158.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN H 155 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS H 71 ND1
REMARK 620 2 HIS H 63 ND1 104.5
REMARK 620 3 HIS H 80 ND1 119.9 106.9
REMARK 620 4 ASP H 83 OD1 108.1 121.6 96.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU I 154 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS I 120 NE2
REMARK 620 2 HIS I 63 NE2 143.4
REMARK 620 3 HIS I 46 ND1 81.8 78.5
REMARK 620 4 HIS I 48 NE2 109.5 106.5 133.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN I 155 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS I 63 ND1
REMARK 620 2 HIS I 80 ND1 115.8
REMARK 620 3 HIS I 71 ND1 103.4 129.3
REMARK 620 4 ASP I 83 OD1 107.6 97.4 100.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU J 154 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS J 46 ND1
REMARK 620 2 HIS J 63 NE2 74.7
REMARK 620 3 HIS J 120 NE2 87.1 143.2
REMARK 620 4 HIS J 48 NE2 145.5 110.1 103.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN J 155 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP J 83 OD1
REMARK 620 2 HIS J 80 ND1 107.9
REMARK 620 3 HIS J 71 ND1 101.8 103.3
REMARK 620 4 HIS J 63 ND1 118.7 110.3 113.6
REMARK 620 N 1 2 3
REMARK 700
REMARK 700 SHEET
REMARK 700 THE SHEETS PRESENTED ON SHEET RECORDS BELOW ARE ACTUALLY
REMARK 700 EIGHT-STRANDED BETA-BARRELS. EACH ONE IS REPRESENTED BY A
REMARK 700 NINE-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE
REMARK 700 IDENTICAL.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CUA
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800 SITE_IDENTIFIER: ZNA
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800 SITE_IDENTIFIER: CUF
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800 SITE_IDENTIFIER: ZNF
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800 SITE_IDENTIFIER: CUB
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800 SITE_IDENTIFIER: ZNB
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800 SITE_IDENTIFIER: CUG
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800 SITE_IDENTIFIER: ZNG
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800 SITE_IDENTIFIER: CUC
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800 SITE_IDENTIFIER: ZNC
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800 SITE_IDENTIFIER: CUH
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800 SITE_IDENTIFIER: ZNH
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800 SITE_IDENTIFIER: CUD
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800 SITE_IDENTIFIER: ZND
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800 SITE_IDENTIFIER: CUI
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800 SITE_IDENTIFIER: ZNI
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800 SITE_IDENTIFIER: CUE
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800 SITE_IDENTIFIER: ZNE
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800 SITE_IDENTIFIER: CUJ
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800 SITE_IDENTIFIER: ZNJ
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU A 154
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 155
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU F 154
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN F 155
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU B 154
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 155
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU G 154
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN G 155
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU C 154
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 155
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU H 154
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN H 155
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU D 154
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 155
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU I 154
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN I 155
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU E 154
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN E 155
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU J 154
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN J 155
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 F 356
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 I 357
DBREF 1SOS A 1 153 UNP P00441 SODC_HUMAN 1 153
DBREF 1SOS F 1 153 UNP P00441 SODC_HUMAN 1 153
DBREF 1SOS B 1 153 UNP P00441 SODC_HUMAN 1 153
DBREF 1SOS G 1 153 UNP P00441 SODC_HUMAN 1 153
DBREF 1SOS C 1 153 UNP P00441 SODC_HUMAN 1 153
DBREF 1SOS H 1 153 UNP P00441 SODC_HUMAN 1 153
DBREF 1SOS D 1 153 UNP P00441 SODC_HUMAN 1 153
DBREF 1SOS I 1 153 UNP P00441 SODC_HUMAN 1 153
DBREF 1SOS E 1 153 UNP P00441 SODC_HUMAN 1 153
DBREF 1SOS J 1 153 UNP P00441 SODC_HUMAN 1 153
SEQRES 1 A 154 ACE ALA THR LYS ALA VAL ALA VAL LEU LYS GLY ASP GLY
SEQRES 2 A 154 PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER
SEQRES 3 A 154 ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU
SEQRES 4 A 154 THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY
SEQRES 5 A 154 ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE
SEQRES 6 A 154 ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU
SEQRES 7 A 154 GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP
SEQRES 8 A 154 LYS ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL
SEQRES 9 A 154 ILE SER LEU SER GLY ASP HIS SER ILE ILE GLY ARG THR
SEQRES 10 A 154 LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY
SEQRES 11 A 154 GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER
SEQRES 12 A 154 ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN
SEQRES 1 F 154 ACE ALA THR LYS ALA VAL ALA VAL LEU LYS GLY ASP GLY
SEQRES 2 F 154 PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER
SEQRES 3 F 154 ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU
SEQRES 4 F 154 THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY
SEQRES 5 F 154 ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE
SEQRES 6 F 154 ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU
SEQRES 7 F 154 GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP
SEQRES 8 F 154 LYS ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL
SEQRES 9 F 154 ILE SER LEU SER GLY ASP HIS SER ILE ILE GLY ARG THR
SEQRES 10 F 154 LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY
SEQRES 11 F 154 GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER
SEQRES 12 F 154 ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN
SEQRES 1 B 154 ACE ALA THR LYS ALA VAL ALA VAL LEU LYS GLY ASP GLY
SEQRES 2 B 154 PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER
SEQRES 3 B 154 ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU
SEQRES 4 B 154 THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY
SEQRES 5 B 154 ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE
SEQRES 6 B 154 ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU
SEQRES 7 B 154 GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP
SEQRES 8 B 154 LYS ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL
SEQRES 9 B 154 ILE SER LEU SER GLY ASP HIS SER ILE ILE GLY ARG THR
SEQRES 10 B 154 LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY
SEQRES 11 B 154 GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER
SEQRES 12 B 154 ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN
SEQRES 1 G 154 ACE ALA THR LYS ALA VAL ALA VAL LEU LYS GLY ASP GLY
SEQRES 2 G 154 PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER
SEQRES 3 G 154 ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU
SEQRES 4 G 154 THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY
SEQRES 5 G 154 ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE
SEQRES 6 G 154 ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU
SEQRES 7 G 154 GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP
SEQRES 8 G 154 LYS ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL
SEQRES 9 G 154 ILE SER LEU SER GLY ASP HIS SER ILE ILE GLY ARG THR
SEQRES 10 G 154 LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY
SEQRES 11 G 154 GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER
SEQRES 12 G 154 ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN
SEQRES 1 C 154 ACE ALA THR LYS ALA VAL ALA VAL LEU LYS GLY ASP GLY
SEQRES 2 C 154 PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER
SEQRES 3 C 154 ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU
SEQRES 4 C 154 THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY
SEQRES 5 C 154 ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE
SEQRES 6 C 154 ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU
SEQRES 7 C 154 GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP
SEQRES 8 C 154 LYS ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL
SEQRES 9 C 154 ILE SER LEU SER GLY ASP HIS SER ILE ILE GLY ARG THR
SEQRES 10 C 154 LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY
SEQRES 11 C 154 GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER
SEQRES 12 C 154 ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN
SEQRES 1 H 154 ACE ALA THR LYS ALA VAL ALA VAL LEU LYS GLY ASP GLY
SEQRES 2 H 154 PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER
SEQRES 3 H 154 ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU
SEQRES 4 H 154 THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY
SEQRES 5 H 154 ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE
SEQRES 6 H 154 ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU
SEQRES 7 H 154 GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP
SEQRES 8 H 154 LYS ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL
SEQRES 9 H 154 ILE SER LEU SER GLY ASP HIS SER ILE ILE GLY ARG THR
SEQRES 10 H 154 LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY
SEQRES 11 H 154 GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER
SEQRES 12 H 154 ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN
SEQRES 1 D 154 ACE ALA THR LYS ALA VAL ALA VAL LEU LYS GLY ASP GLY
SEQRES 2 D 154 PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER
SEQRES 3 D 154 ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU
SEQRES 4 D 154 THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY
SEQRES 5 D 154 ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE
SEQRES 6 D 154 ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU
SEQRES 7 D 154 GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP
SEQRES 8 D 154 LYS ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL
SEQRES 9 D 154 ILE SER LEU SER GLY ASP HIS SER ILE ILE GLY ARG THR
SEQRES 10 D 154 LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY
SEQRES 11 D 154 GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER
SEQRES 12 D 154 ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN
SEQRES 1 I 154 ACE ALA THR LYS ALA VAL ALA VAL LEU LYS GLY ASP GLY
SEQRES 2 I 154 PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER
SEQRES 3 I 154 ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU
SEQRES 4 I 154 THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY
SEQRES 5 I 154 ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE
SEQRES 6 I 154 ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU
SEQRES 7 I 154 GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP
SEQRES 8 I 154 LYS ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL
SEQRES 9 I 154 ILE SER LEU SER GLY ASP HIS SER ILE ILE GLY ARG THR
SEQRES 10 I 154 LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY
SEQRES 11 I 154 GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER
SEQRES 12 I 154 ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN
SEQRES 1 E 154 ACE ALA THR LYS ALA VAL ALA VAL LEU LYS GLY ASP GLY
SEQRES 2 E 154 PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER
SEQRES 3 E 154 ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU
SEQRES 4 E 154 THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY
SEQRES 5 E 154 ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE
SEQRES 6 E 154 ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU
SEQRES 7 E 154 GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP
SEQRES 8 E 154 LYS ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL
SEQRES 9 E 154 ILE SER LEU SER GLY ASP HIS SER ILE ILE GLY ARG THR
SEQRES 10 E 154 LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY
SEQRES 11 E 154 GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER
SEQRES 12 E 154 ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN
SEQRES 1 J 154 ACE ALA THR LYS ALA VAL ALA VAL LEU LYS GLY ASP GLY
SEQRES 2 J 154 PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER
SEQRES 3 J 154 ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU
SEQRES 4 J 154 THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY
SEQRES 5 J 154 ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE
SEQRES 6 J 154 ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU
SEQRES 7 J 154 GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP
SEQRES 8 J 154 LYS ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL
SEQRES 9 J 154 ILE SER LEU SER GLY ASP HIS SER ILE ILE GLY ARG THR
SEQRES 10 J 154 LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY
SEQRES 11 J 154 GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER
SEQRES 12 J 154 ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN
HET ACE A 0 3
HET ACE F 0 3
HET ACE B 0 3
HET ACE G 0 3
HET ACE C 0 3
HET ACE H 0 3
HET ACE D 0 3
HET ACE I 0 3
HET ACE E 0 3
HET ACE J 0 3
HET CU A 154 1
HET ZN A 155 1
HET CU F 154 1
HET ZN F 155 1
HET CU B 154 1
HET ZN B 155 1
HET CU G 154 1
HET ZN G 155 1
HET CU C 154 1
HET ZN C 155 1
HET CU H 154 1
HET ZN H 155 1
HET CU D 154 1
HET ZN D 155 1
HET CU I 154 1
HET ZN I 155 1
HET CU E 154 1
HET ZN E 155 1
HET CU J 154 1
HET ZN J 155 1
HET SO4 F 356 5
HET SO4 I 357 5
HETNAM ACE ACETYL GROUP
HETNAM CU COPPER (II) ION
HETNAM ZN ZINC ION
HETNAM SO4 SULFATE ION
FORMUL 1 ACE 10(C2 H4 O)
FORMUL 11 CU 10(CU 2+)
FORMUL 12 ZN 10(ZN 2+)
FORMUL 31 SO4 2(O4 S 2-)
FORMUL 33 HOH *499(H2 O)
HELIX 1 HA GLU A 133 THR A 137 1SINGLE-LOOP ALPHA-HELIX 5
HELIX 2 HF GLU F 133 THR F 137 1SINGLE-LOOP ALPHA-HELIX 5
HELIX 3 HB GLU B 133 THR B 137 1SINGLE-LOOP ALPHA-HELIX 5
HELIX 4 HG GLU G 133 THR G 137 1SINGLE-LOOP ALPHA-HELIX 5
HELIX 5 HC GLU C 133 THR C 137 1SINGLE-LOOP ALPHA-HELIX 5
HELIX 6 HH GLU H 133 THR H 137 1SINGLE-LOOP ALPHA-HELIX 5
HELIX 7 HD GLU D 133 THR D 137 1SINGLE-LOOP ALPHA-HELIX 5
HELIX 8 HI GLU I 133 THR I 137 1SINGLE-LOOP ALPHA-HELIX 5
HELIX 9 HE GLU E 133 THR E 137 1SINGLE-LOOP ALPHA-HELIX 5
HELIX 10 HJ GLU J 133 THR J 137 1SINGLE-LOOP ALPHA-HELIX 5
SHEET 1 SA 9 ALA A 4 LYS A 9 0
SHEET 2 SA 9 GLN A 15 GLU A 21 -1 N PHE A 20 O ALA A 4
SHEET 3 SA 9 VAL A 29 LYS A 30 1 N LYS A 30 O GLU A 21
SHEET 4 SA 9 VAL A 94 ASP A 101 -1 N ILE A 99 O VAL A 31
SHEET 5 SA 9 GLY A 85 ALA A 89 1
SHEET 6 SA 9 GLY A 41 HIS A 48 -1 N HIS A 43 O VAL A 87
SHEET 7 SA 9 ARG A 115 HIS A 120 1 N VAL A 118 O HIS A 46
SHEET 8 SA 9 CYS A 146 GLY A 150 -1 N GLY A 147 O LEU A 117
SHEET 9 SA 9 ALA A 4 LYS A 9 -1 N VAL A 7 O VAL A 148
SHEET 1 SF 9 ALA F 4 LYS F 9 0
SHEET 2 SF 9 GLN F 15 GLU F 21 -1 N PHE F 20 O ALA F 4
SHEET 3 SF 9 VAL F 29 LYS F 30 1 N LYS F 30 O GLU F 21
SHEET 4 SF 9 VAL F 94 ASP F 101 -1 N ILE F 99 O VAL F 31
SHEET 5 SF 9 GLY F 85 ALA F 89 1
SHEET 6 SF 9 GLY F 41 HIS F 48 -1 N HIS F 43 O VAL F 87
SHEET 7 SF 9 ARG F 115 HIS F 120 1 N VAL F 118 O HIS F 46
SHEET 8 SF 9 CYS F 146 GLY F 150 -1 N GLY F 147 O LEU F 117
SHEET 9 SF 9 ALA F 4 LYS F 9 -1 N VAL F 7 O VAL F 148
SHEET 1 SB 9 ALA B 4 LYS B 9 0
SHEET 2 SB 9 GLN B 15 GLU B 21 -1 N PHE B 20 O ALA B 4
SHEET 3 SB 9 VAL B 29 LYS B 30 1 N LYS B 30 O GLU B 21
SHEET 4 SB 9 VAL B 94 ASP B 101 -1 N ILE B 99 O VAL B 31
SHEET 5 SB 9 GLY B 85 ALA B 89 1
SHEET 6 SB 9 GLY B 41 HIS B 48 -1 N HIS B 43 O VAL B 87
SHEET 7 SB 9 ARG B 115 HIS B 120 1 N VAL B 118 O HIS B 46
SHEET 8 SB 9 CYS B 146 GLY B 150 -1 N GLY B 147 O LEU B 117
SHEET 9 SB 9 ALA B 4 LYS B 9 -1 N VAL B 7 O VAL B 148
SHEET 1 SG 9 ALA G 4 LYS G 9 0
SHEET 2 SG 9 GLN G 15 GLU G 21 -1 N PHE G 20 O ALA G 4
SHEET 3 SG 9 VAL G 29 LYS G 30 1 N LYS G 30 O GLU G 21
SHEET 4 SG 9 VAL G 94 ASP G 101 -1 N ILE G 99 O VAL G 31
SHEET 5 SG 9 GLY G 85 ALA G 89 1
SHEET 6 SG 9 GLY G 41 HIS G 48 -1 N HIS G 43 O VAL G 87
SHEET 7 SG 9 ARG G 115 HIS G 120 1 N VAL G 118 O HIS G 46
SHEET 8 SG 9 CYS G 146 GLY G 150 -1 N GLY G 147 O LEU G 117
SHEET 9 SG 9 ALA G 4 LYS G 9 -1 N VAL G 7 O VAL G 148
SHEET 1 SC 9 ALA C 4 LYS C 9 0
SHEET 2 SC 9 GLN C 15 GLU C 21 -1 N PHE C 20 O ALA C 4
SHEET 3 SC 9 VAL C 29 LYS C 30 1 N LYS C 30 O GLU C 21
SHEET 4 SC 9 VAL C 94 ASP C 101 -1 N ILE C 99 O VAL C 31
SHEET 5 SC 9 GLY C 85 ALA C 89 1
SHEET 6 SC 9 GLY C 41 HIS C 48 -1 N HIS C 43 O VAL C 87
SHEET 7 SC 9 ARG C 115 HIS C 120 1 N VAL C 118 O HIS C 46
SHEET 8 SC 9 CYS C 146 GLY C 150 -1 N GLY C 147 O LEU C 117
SHEET 9 SC 9 ALA C 4 LYS C 9 -1 N VAL C 7 O VAL C 148
SHEET 1 SH 9 ALA H 4 LYS H 9 0
SHEET 2 SH 9 GLN H 15 GLU H 21 -1 N PHE H 20 O ALA H 4
SHEET 3 SH 9 VAL H 29 LYS H 30 1 N LYS H 30 O GLU H 21
SHEET 4 SH 9 VAL H 94 ASP H 101 -1 N ILE H 99 O VAL H 31
SHEET 5 SH 9 GLY H 85 ALA H 89 1
SHEET 6 SH 9 GLY H 41 HIS H 48 -1 N HIS H 43 O VAL H 87
SHEET 7 SH 9 ARG H 115 HIS H 120 1 N VAL H 118 O HIS H 46
SHEET 8 SH 9 CYS H 146 GLY H 150 -1 N GLY H 147 O LEU H 117
SHEET 9 SH 9 ALA H 4 LYS H 9 -1 N VAL H 7 O VAL H 148
SHEET 1 SD 9 ALA D 4 LYS D 9 0
SHEET 2 SD 9 GLN D 15 GLU D 21 -1 N PHE D 20 O ALA D 4
SHEET 3 SD 9 VAL D 29 LYS D 30 1 N LYS D 30 O GLU D 21
SHEET 4 SD 9 VAL D 94 ASP D 101 -1 N ILE D 99 O VAL D 31
SHEET 5 SD 9 GLY D 85 ALA D 89 1
SHEET 6 SD 9 GLY D 41 HIS D 48 -1 N HIS D 43 O VAL D 87
SHEET 7 SD 9 ARG D 115 HIS D 120 1 N VAL D 118 O HIS D 46
SHEET 8 SD 9 CYS D 146 GLY D 150 -1 N GLY D 147 O LEU D 117
SHEET 9 SD 9 ALA D 4 LYS D 9 -1 N VAL D 7 O VAL D 148
SHEET 1 SI 9 ALA I 4 LYS I 9 0
SHEET 2 SI 9 GLN I 15 GLU I 21 -1 N PHE I 20 O ALA I 4
SHEET 3 SI 9 VAL I 29 LYS I 30 1 N LYS I 30 O GLU I 21
SHEET 4 SI 9 VAL I 94 ASP I 101 -1 N ILE I 99 O VAL I 31
SHEET 5 SI 9 GLY I 85 ALA I 89 1
SHEET 6 SI 9 GLY I 41 HIS I 48 -1 N HIS I 43 O VAL I 87
SHEET 7 SI 9 ARG I 115 HIS I 120 1 N VAL I 118 O HIS I 46
SHEET 8 SI 9 CYS I 146 GLY I 150 -1 N GLY I 147 O LEU I 117
SHEET 9 SI 9 ALA I 4 LYS I 9 -1 N VAL I 7 O VAL I 148
SHEET 1 SE 9 ALA E 4 LYS E 9 0
SHEET 2 SE 9 GLN E 15 GLU E 21 -1 N PHE E 20 O ALA E 4
SHEET 3 SE 9 VAL E 29 LYS E 30 1 N LYS E 30 O GLU E 21
SHEET 4 SE 9 VAL E 94 ASP E 101 -1 N ILE E 99 O VAL E 31
SHEET 5 SE 9 GLY E 85 ALA E 89 1
SHEET 6 SE 9 GLY E 41 HIS E 48 -1 N HIS E 43 O VAL E 87
SHEET 7 SE 9 ARG E 115 HIS E 120 1 N VAL E 118 O HIS E 46
SHEET 8 SE 9 CYS E 146 GLY E 150 -1 N GLY E 147 O LEU E 117
SHEET 9 SE 9 ALA E 4 LYS E 9 -1 N VAL E 7 O VAL E 148
SHEET 1 SJ 9 ALA J 4 LYS J 9 0
SHEET 2 SJ 9 GLN J 15 GLU J 21 -1 N PHE J 20 O ALA J 4
SHEET 3 SJ 9 VAL J 29 LYS J 30 1 N LYS J 30 O GLU J 21
SHEET 4 SJ 9 VAL J 94 ASP J 101 -1 N ILE J 99 O VAL J 31
SHEET 5 SJ 9 GLY J 85 ALA J 89 1
SHEET 6 SJ 9 GLY J 41 HIS J 48 -1 N HIS J 43 O VAL J 87
SHEET 7 SJ 9 ARG J 115 HIS J 120 1 N VAL J 118 O HIS J 46
SHEET 8 SJ 9 CYS J 146 GLY J 150 -1 N GLY J 147 O LEU J 117
SHEET 9 SJ 9 ALA J 4 LYS J 9 -1 N VAL J 7 O VAL J 148
SSBOND 1 CYS A 57 CYS A 146 1555 1555 2.01
SSBOND 2 CYS F 57 CYS F 146 1555 1555 2.02
SSBOND 3 CYS B 57 CYS B 146 1555 1555 2.03
SSBOND 4 CYS G 57 CYS G 146 1555 1555 2.02
SSBOND 5 CYS C 57 CYS C 146 1555 1555 2.00
SSBOND 6 CYS H 57 CYS H 146 1555 1555 2.00
SSBOND 7 CYS D 57 CYS D 146 1555 1555 2.00
SSBOND 8 CYS I 57 CYS I 146 1555 1555 2.02
SSBOND 9 CYS E 57 CYS E 146 1555 1555 2.03
SSBOND 10 CYS J 57 CYS J 146 1555 1555 2.02
LINK C ACE A 0 N ALA A 1 1555 1555 1.34
LINK C ACE F 0 N ALA F 1 1555 1555 1.36
LINK C ACE B 0 N ALA B 1 1555 1555 1.34
LINK C ACE G 0 N ALA G 1 1555 1555 1.34
LINK C ACE C 0 N ALA C 1 1555 1555 1.35
LINK C ACE H 0 N ALA H 1 1555 1555 1.34
LINK C ACE D 0 N ALA D 1 1555 1555 1.36
LINK C ACE I 0 N ALA I 1 1555 1555 1.35
LINK C ACE E 0 N ALA E 1 1555 1555 1.34
LINK C ACE J 0 N ALA J 1 1555 1555 1.34
LINK CU CU A 154 NE2 HIS A 48 1555 1555 2.06
LINK CU CU A 154 NE2 HIS A 63 1555 1555 2.12
LINK CU CU A 154 NE2 HIS A 120 1555 1555 2.07
LINK CU CU A 154 ND1 HIS A 46 1555 1555 2.07
LINK ZN ZN A 155 ND1 HIS A 71 1555 1555 2.06
LINK ZN ZN A 155 OD1 ASP A 83 1555 1555 1.92
LINK ZN ZN A 155 ND1 HIS A 63 1555 1555 2.10
LINK ZN ZN A 155 ND1 HIS A 80 1555 1555 2.04
LINK CU CU B 154 NE2 HIS B 63 1555 1555 2.12
LINK CU CU B 154 NE2 HIS B 120 1555 1555 2.04
LINK CU CU B 154 NE2 HIS B 48 1555 1555 2.08
LINK CU CU B 154 ND1 HIS B 46 1555 1555 2.03
LINK ZN ZN B 155 ND1 HIS B 80 1555 1555 2.06
LINK ZN ZN B 155 OD1 ASP B 83 1555 1555 1.97
LINK ZN ZN B 155 ND1 HIS B 63 1555 1555 2.12
LINK ZN ZN B 155 ND1 HIS B 71 1555 1555 2.08
LINK CU CU C 154 NE2 HIS C 48 1555 1555 2.09
LINK CU CU C 154 NE2 HIS C 120 1555 1555 2.04
LINK CU CU C 154 ND1 HIS C 46 1555 1555 2.07
LINK CU CU C 154 NE2 HIS C 63 1555 1555 2.08
LINK ZN ZN C 155 ND1 HIS C 71 1555 1555 2.06
LINK ZN ZN C 155 OD1 ASP C 83 1555 1555 1.94
LINK ZN ZN C 155 ND1 HIS C 80 1555 1555 2.05
LINK ZN ZN C 155 ND1 HIS C 63 1555 1555 2.08
LINK CU CU D 154 ND1 HIS D 46 1555 1555 2.04
LINK CU CU D 154 NE2 HIS D 48 1555 1555 2.09
LINK CU CU D 154 NE2 HIS D 63 1555 1555 2.11
LINK CU CU D 154 NE2 HIS D 120 1555 1555 2.05
LINK ZN ZN D 155 ND1 HIS D 63 1555 1555 2.13
LINK ZN ZN D 155 ND1 HIS D 71 1555 1555 2.08
LINK ZN ZN D 155 ND1 HIS D 80 1555 1555 2.09
LINK ZN ZN D 155 OD1 ASP D 83 1555 1555 1.96
LINK CU CU E 154 NE2 HIS E 48 1555 1555 2.08
LINK CU CU E 154 ND1 HIS E 46 1555 1555 2.04
LINK CU CU E 154 NE2 HIS E 120 1555 1555 2.05
LINK CU CU E 154 NE2 HIS E 63 1555 1555 2.12
LINK ZN ZN E 155 ND1 HIS E 80 1555 1555 2.08
LINK ZN ZN E 155 ND1 HIS E 71 1555 1555 2.10
LINK ZN ZN E 155 OD2 ASP E 83 1555 1555 2.51
LINK ZN ZN E 155 ND1 HIS E 63 1555 1555 2.12
LINK ZN ZN E 155 OD1 ASP E 83 1555 1555 1.96
LINK CU CU F 154 NE2 HIS F 48 1555 1555 2.09
LINK CU CU F 154 NE2 HIS F 63 1555 1555 2.12
LINK CU CU F 154 NE2 HIS F 120 1555 1555 2.06
LINK CU CU F 154 ND1 HIS F 46 1555 1555 2.03
LINK ZN ZN F 155 OD1 ASP F 83 1555 1555 1.95
LINK ZN ZN F 155 ND1 HIS F 71 1555 1555 2.05
LINK ZN ZN F 155 ND1 HIS F 63 1555 1555 2.09
LINK ZN ZN F 155 ND1 HIS F 80 1555 1555 2.06
LINK CU CU G 154 NE2 HIS G 48 1555 1555 2.08
LINK CU CU G 154 NE2 HIS G 120 1555 1555 2.06
LINK CU CU G 154 NE2 HIS G 63 1555 1555 2.07
LINK CU CU G 154 ND1 HIS G 46 1555 1555 2.05
LINK ZN ZN G 155 OD1 ASP G 83 1555 1555 1.95
LINK ZN ZN G 155 ND1 HIS G 63 1555 1555 2.07
LINK ZN ZN G 155 OD2 ASP G 83 1555 1555 2.69
LINK ZN ZN G 155 ND1 HIS G 80 1555 1555 2.05
LINK ZN ZN G 155 ND1 HIS G 71 1555 1555 2.07
LINK CU CU H 154 ND1 HIS H 46 1555 1555 2.04
LINK CU CU H 154 NE2 HIS H 48 1555 1555 2.08
LINK CU CU H 154 NE2 HIS H 120 1555 1555 2.05
LINK CU CU H 154 NE2 HIS H 63 1555 1555 2.09
LINK ZN ZN H 155 ND1 HIS H 71 1555 1555 2.05
LINK ZN ZN H 155 ND1 HIS H 63 1555 1555 2.11
LINK ZN ZN H 155 ND1 HIS H 80 1555 1555 2.09
LINK ZN ZN H 155 OD1 ASP H 83 1555 1555 1.92
LINK CU CU I 154 NE2 HIS I 120 1555 1555 2.05
LINK CU CU I 154 NE2 HIS I 63 1555 1555 2.12
LINK CU CU I 154 ND1 HIS I 46 1555 1555 2.03
LINK CU CU I 154 NE2 HIS I 48 1555 1555 2.06
LINK ZN ZN I 155 ND1 HIS I 63 1555 1555 2.11
LINK ZN ZN I 155 ND1 HIS I 80 1555 1555 2.04
LINK ZN ZN I 155 ND1 HIS I 71 1555 1555 2.05
LINK ZN ZN I 155 OD1 ASP I 83 1555 1555 1.95
LINK CU CU J 154 ND1 HIS J 46 1555 1555 2.04
LINK CU CU J 154 NE2 HIS J 63 1555 1555 2.09
LINK CU CU J 154 NE2 HIS J 120 1555 1555 2.07
LINK CU CU J 154 NE2 HIS J 48 1555 1555 2.07
LINK ZN ZN J 155 OD1 ASP J 83 1555 1555 1.93
LINK ZN ZN J 155 ND1 HIS J 80 1555 1555 2.06
LINK ZN ZN J 155 ND1 HIS J 71 1555 1555 2.07
LINK ZN ZN J 155 ND1 HIS J 63 1555 1555 2.08
SITE 1 CUA 4 HIS A 46 HIS A 48 HIS A 63 HIS A 120
SITE 1 ZNA 4 HIS A 63 HIS A 71 HIS A 80 ASP A 83
SITE 1 CUF 4 HIS F 46 HIS F 48 HIS F 63 HIS F 120
SITE 1 ZNF 4 HIS F 63 HIS F 71 HIS F 80 ASP F 83
SITE 1 CUB 4 HIS B 46 HIS B 48 HIS B 63 HIS B 120
SITE 1 ZNB 4 HIS B 63 HIS B 71 HIS B 80 ASP B 83
SITE 1 CUG 4 HIS G 46 HIS G 48 HIS G 63 HIS G 120
SITE 1 ZNG 4 HIS G 63 HIS G 71 HIS G 80 ASP G 83
SITE 1 CUC 4 HIS C 46 HIS C 48 HIS C 63 HIS C 120
SITE 1 ZNC 4 HIS C 63 HIS C 71 HIS C 80 ASP C 83
SITE 1 CUH 4 HIS H 46 HIS H 48 HIS H 63 HIS H 120
SITE 1 ZNH 4 HIS H 63 HIS H 71 HIS H 80 ASP H 83
SITE 1 CUD 4 HIS D 46 HIS D 48 HIS D 63 HIS D 120
SITE 1 ZND 4 HIS D 63 HIS D 71 HIS D 80 ASP D 83
SITE 1 CUI 4 HIS I 46 HIS I 48 HIS I 63 HIS I 120
SITE 1 ZNI 4 HIS I 63 HIS I 71 HIS I 80 ASP I 83
SITE 1 CUE 4 HIS E 46 HIS E 48 HIS E 63 HIS E 120
SITE 1 ZNE 4 HIS E 63 HIS E 71 HIS E 80 ASP E 83
SITE 1 CUJ 4 HIS J 46 HIS J 48 HIS J 63 HIS J 120
SITE 1 ZNJ 4 HIS J 63 HIS J 71 HIS J 80 ASP J 83
SITE 1 AC1 4 HIS A 46 HIS A 48 HIS A 63 HIS A 120
SITE 1 AC2 4 HIS A 63 HIS A 71 HIS A 80 ASP A 83
SITE 1 AC3 4 HIS F 46 HIS F 48 HIS F 63 HIS F 120
SITE 1 AC4 4 HIS F 63 HIS F 71 HIS F 80 ASP F 83
SITE 1 AC5 4 HIS B 46 HIS B 48 HIS B 63 HIS B 120
SITE 1 AC6 4 HIS B 63 HIS B 71 HIS B 80 ASP B 83
SITE 1 AC7 4 HIS G 46 HIS G 48 HIS G 63 HIS G 120
SITE 1 AC8 4 HIS G 63 HIS G 71 HIS G 80 ASP G 83
SITE 1 AC9 4 HIS C 46 HIS C 48 HIS C 63 HIS C 120
SITE 1 BC1 4 HIS C 63 HIS C 71 HIS C 80 ASP C 83
SITE 1 BC2 4 HIS H 46 HIS H 48 HIS H 63 HIS H 120
SITE 1 BC3 4 HIS H 63 HIS H 71 HIS H 80 ASP H 83
SITE 1 BC4 4 HIS D 46 HIS D 48 HIS D 63 HIS D 120
SITE 1 BC5 4 HIS D 63 HIS D 71 HIS D 80 ASP D 83
SITE 1 BC6 4 HIS I 46 HIS I 48 HIS I 63 HIS I 120
SITE 1 BC7 4 HIS I 63 HIS I 71 HIS I 80 ASP I 83
SITE 1 BC8 4 HIS E 46 HIS E 48 HIS E 63 HIS E 120
SITE 1 BC9 5 HIS E 63 HIS E 71 HIS E 80 ASP E 83
SITE 2 BC9 5 LYS E 136
SITE 1 CC1 4 HIS J 46 HIS J 48 HIS J 63 HIS J 120
SITE 1 CC2 4 HIS J 63 HIS J 71 HIS J 80 ASP J 83
SITE 1 CC3 3 LYS F 75 LYS F 128 LYS G 128
SITE 1 CC4 5 LYS C 128 LYS I 75 LYS I 128 HOH I 358
SITE 2 CC4 5 LYS J 128
CRYST1 205.200 167.000 145.500 90.00 90.00 90.00 C 2 2 21 80
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 0.004873 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005988 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006873 0.00000
MTRIX1 1 -0.982700 0.008000 0.185000 120.63000 1
MTRIX2 1 0.018200 -0.990100 0.139400 56.45800 1
MTRIX3 1 0.184300 0.140300 0.972800 -15.30400 1
MTRIX1 2 -0.463700 -0.885800 0.015100 106.40600 1
MTRIX2 2 0.886000 -0.463700 0.008200 -66.09600 1
MTRIX3 2 -0.000200 0.017200 0.999900 0.01700 1
MTRIX1 3 0.467000 0.867400 0.171900 15.10400 1
MTRIX2 3 -0.883700 0.450900 0.125700 123.62500 1
MTRIX3 3 0.031500 -0.210600 0.977100 -4.28600 1
MTRIX1 4 -0.534900 0.842700 0.060800 111.29400 1
MTRIX2 4 -0.844400 -0.535700 -0.003200 61.00000 1
MTRIX3 4 0.029900 -0.053000 0.998100 -3.26200 1
MTRIX1 5 0.522700 -0.838500 0.154100 10.87600 1
MTRIX2 5 0.832900 0.540800 0.117600 -2.13100 1
MTRIX3 5 -0.181900 0.066900 0.981000 11.15100 1
MTRIX1 6 -0.981000 -0.026900 -0.192300 208.83600 1
MTRIX2 6 0.028200 -0.999600 -0.004000 28.44200 1
MTRIX3 6 -0.192200 -0.009400 0.981300 29.48700 1
MTRIX1 7 0.936100 0.007600 0.351500 -79.86000 1
MTRIX2 7 -0.056900 0.989900 0.130100 33.91200 1
MTRIX3 7 -0.347000 -0.141900 0.927100 53.15700 1
MTRIX1 8 0.476600 0.879000 0.010300 -19.71400 1
MTRIX2 8 -0.877900 0.476600 -0.046600 102.41300 1
MTRIX3 8 -0.045800 0.013200 0.998900 9.15900 1
MTRIX1 9 -0.475300 -0.865900 0.155600 142.20700 1
MTRIX2 9 0.876000 -0.449400 0.175200 -44.74400 1
MTRIX3 9 -0.081800 0.219600 0.972200 5.36500 1
HETATM 1 C ACE A 0 53.275 28.140 5.578 1.00 34.09 C
HETATM 2 O ACE A 0 52.151 27.619 5.540 1.00 34.04 O
HETATM 3 CH3 ACE A 0 54.133 28.277 4.327 1.00 33.82 C
(ATOM LINES ARE NOT SHOWN.)
END
