HEADER COMPLEX (ANTIBODY/ELECTRON TRANSPORT) 26-MAR-98 1WEJ
TITLE IGG1 FAB FRAGMENT (OF E8 ANTIBODY) COMPLEXED WITH HORSE
TITLE 2 CYTOCHROME C AT 1.8 A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: E8 ANTIBODY;
COMPND 3 CHAIN: L;
COMPND 4 FRAGMENT: FAB;
COMPND 5 SYNONYM: FAB E8;
COMPND 6 OTHER_DETAILS: IGG1 KAPPA MOUSE MONOCLONAL ANTIBODY;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: E8 ANTIBODY;
COMPND 9 CHAIN: H;
COMPND 10 FRAGMENT: FAB;
COMPND 11 SYNONYM: FAB E8;
COMPND 12 OTHER_DETAILS: IGG1 KAPPA MOUSE MONOCLONAL ANTIBODY;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: CYTOCHROME C;
COMPND 15 CHAIN: F;
COMPND 16 SYNONYM: CYT C, ANTIGEN;
COMPND 17 OTHER_DETAILS: ELECTRON TRANSPORT PROTEIN WITH HEME
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 STRAIN: BALB/C;
SOURCE 6 CELL_LINE: P3-X63-AG8.653;
SOURCE 7 ORGAN: SPLEEN;
SOURCE 8 OTHER_DETAILS: E8 ANTIBODY PURIFIED FROM ASCITES;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 11 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 12 ORGANISM_TAXID: 10090;
SOURCE 13 STRAIN: BALB-C;
SOURCE 14 CELL_LINE: P3-X63-AG8.653;
SOURCE 15 ORGAN: SPLEEN;
SOURCE 16 OTHER_DETAILS: E8 ANTIBODY PURIFIED FROM ASCITES;
SOURCE 17 MOL_ID: 3;
SOURCE 18 ORGANISM_SCIENTIFIC: EQUUS CABALLUS;
SOURCE 19 ORGANISM_COMMON: HORSE;
SOURCE 20 ORGANISM_TAXID: 9796;
SOURCE 21 ORGAN: HEART;
SOURCE 22 OTHER_DETAILS: OBTAINED FROM SIGMA
KEYWDS IMMUNOGLOBULIN, IGG1 KAPPA, FAB FRAGMENT, HORSE CYTOCHROME
KEYWDS 2 C, COMPLEX (ANTIBODY/ELECTRON TRANSPORT)
EXPDTA X-RAY DIFFRACTION
AUTHOR S.E.MYLVAGANAM,Y.PATERSON,E.D.GETZOFF
REVDAT 2 24-FEB-09 1WEJ 1 VERSN
REVDAT 1 09-DEC-98 1WEJ 0
JRNL AUTH S.E.MYLVAGANAM,Y.PATERSON,E.D.GETZOFF
JRNL TITL STRUCTURAL BASIS FOR THE BINDING OF AN
JRNL TITL 2 ANTI-CYTOCHROME C ANTIBODY TO ITS ANTIGEN: CRYSTAL
JRNL TITL 3 STRUCTURES OF FABE8-CYTOCHROME C COMPLEX TO 1.8 A
JRNL TITL 4 RESOLUTION AND FABE8 TO 2.26 A RESOLUTION.
JRNL REF J.MOL.BIOL. V. 281 301 1998
JRNL REFN ISSN 0022-2836
JRNL PMID 9698550
JRNL DOI 10.1006/JMBI.1998.1942
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.E.MYLVAGANAM,Y.PATERSON,K.KAISER,K.BOWDISH,
REMARK 1 AUTH 2 E.D.GETZOFF
REMARK 1 TITL BIOCHEMICAL IMPLICATIONS FROM THE VARIABLE GENE
REMARK 1 TITL 2 SEQUENCES OF AN ANTI-CYTOCHROME C ANTIBODY AND
REMARK 1 TITL 3 CRYSTALLOGRAPHIC CHARACTERIZATION OF ITS
REMARK 1 TITL 4 ANTIGEN-BINDING FRAGMENT IN FREE AND
REMARK 1 TITL 5 ANTIGEN-COMPLEXED FORMS
REMARK 1 REF J.MOL.BIOL. V. 221 455 1991
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 2
REMARK 1 AUTH F.R.CARBONE,Y.PATERSON
REMARK 1 TITL MONOCLONAL ANTIBODIES TO HORSE CYTOCHROME C
REMARK 1 TITL 2 EXPRESSING FOUR DISTINCT IDIOTYPES DISTRIBUTE
REMARK 1 TITL 3 AMONG TWO SITES ON THE NATIVE PROTEIN
REMARK 1 REF J.IMMUNOL. V. 135 2609 1985
REMARK 1 REFN ISSN 0022-1767
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.8
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 94.1
REMARK 3 NUMBER OF REFLECTIONS : 47993
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) : 0.200
REMARK 3 FREE R VALUE : 0.256
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
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 : 8
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.88
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.30
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 5745
REMARK 3 BIN R VALUE (WORKING SET) : 0.3160
REMARK 3 BIN FREE R VALUE : 8.0000
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.10
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 : 4166
REMARK 3 NUCLEIC ACID ATOMS : NULL
REMARK 3 HETEROGEN ATOMS : 43
REMARK 3 SOLVENT ATOMS : 637
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 18.06
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.96
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.94200
REMARK 3 B22 (A**2) : -2.04200
REMARK 3 B33 (A**2) : 2.07000
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) : 0.33
REMARK 3 LOW RESOLUTION CUTOFF (A) : 20.00
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) : 0.30
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.47
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 27.40
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.54
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 : PARAM19X.HEME
REMARK 3 PARAMETER FILE 2 : PARHCSDXB.PRO
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPH19X.HEM
REMARK 3 TOPOLOGY FILE 2 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1WEJ 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 : JAN-95
REMARK 200 TEMPERATURE (KELVIN) : 90
REMARK 200 PH : 6.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL7-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.08
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 48348
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.1
REMARK 200 DATA REDUNDANCY : 5.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 36.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.86
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.5
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.28200
REMARK 200 <I/SIGMA(I)> FOR SHELL : 12.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR 3.8
REMARK 200 STARTING MODEL: 2.26 A RESOLUTION FABE8 X-RAY STRUCTURE (FREE
REMARK 200 FAB E8) (MYLVAGANAM ET AL., 1998, JMB, 281, 301-32; PDB ENTRY
REMARK 200 1QBL) AND HORSE CYTOCHROME C 1.9 A X-RAY STRUCTURE (BUSHNELL
REMARK 200 ET. AL., 1990; PDB ENTRY 1HRC).
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50MM ZINC ACETATE BUFFER, PH 6.4,
REMARK 280 25% (W/V) PEG 4000.
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 39.79000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 47.19000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.27000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 47.19000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 39.79000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 36.27000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6420 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24230 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -80.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, H, 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6040 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24610 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -87.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 -94.38000
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, H
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 CYS H 223 CA - CB - SG ANGL. DEV. = 6.6 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 ALA L 51 -39.27 68.18
REMARK 500 SER H 76 -0.02 -144.14
REMARK 500 ALA H 92 -178.23 -177.80
REMARK 500 ASP H 100 -124.93 -133.29
REMARK 500 LYS H 136 58.30 -109.21
REMARK 500 PRO H 151 -164.82 -102.67
REMARK 500 CYS H 219 29.09 80.06
REMARK 500 ASP H 222 148.55 153.64
REMARK 500 LYS F 27 -129.04 -113.20
REMARK 500 ASN F 70 85.73 -162.19
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 F 666 DISTANCE = 5.11 ANGSTROMS
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 HEM F 105
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 L 215 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP L 151 OD2
REMARK 620 2 HIS L 189 ND1 118.3
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN L 215
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM F 105
DBREF 1WEJ L 1 214 GB 2072141 AAB53778 15 228
DBREF 1WEJ H 2 217 PIR S49220 S49220 2 219
DBREF 1WEJ F 1 104 UNP P00004 CYC_HORSE 1 104
SEQADV 1WEJ SER L 85 GB 2072141 THR 99 CONFLICT
SEQADV 1WEJ GLN L 89 GB 2072141 HIS 103 CONFLICT
SEQADV 1WEJ ILE L 106 GB 2072141 VAL 120 CONFLICT
SEQADV 1WEJ PHE L 118 GB 2072141 LEU 132 CONFLICT
SEQADV 1WEJ GLN H 3 PIR S49220 LYS 3 CONFLICT
SEQADV 1WEJ GLN H 5 PIR S49220 LEU 5 CONFLICT
SEQADV 1WEJ GLN H 6 PIR S49220 GLU 6 CONFLICT
SEQADV 1WEJ PRO H 14 PIR S49220 SER 14 CONFLICT
SEQADV 1WEJ LYS H 43 PIR S49220 GLN 43 CONFLICT
SEQADV 1WEJ SER H 55 PIR S49220 ASN 55 CONFLICT
SEQADV 1WEJ ASN H 57 PIR S49220 GLU 57 CONFLICT
SEQADV 1WEJ THR H 58 PIR S49220 ILE 58 CONFLICT
SEQADV 1WEJ ASP H 66 PIR S49220 GLY 66 CONFLICT
SEQADV 1WEJ LYS H 67 PIR S49220 THR 67 CONFLICT
SEQADV 1WEJ SER H 76 PIR S49220 THR 76 CONFLICT
SEQADV 1WEJ H PIR S49220 VAL 97 DELETION
SEQADV 1WEJ H PIR S49220 ARG 98 DELETION
SEQADV 1WEJ ALA H 97 PIR S49220 ARG 99 CONFLICT
SEQADV 1WEJ ASP H 100 PIR S49220 GLY 102 CONFLICT
SEQADV 1WEJ TYR H 101 PIR S49220 SER 103 CONFLICT
SEQADV 1WEJ GLY H 102 PIR S49220 SER 104 CONFLICT
SEQADV 1WEJ ASN H 103 PIR S49220 GLN 105 CONFLICT
SEQADV 1WEJ PHE H 104 PIR S49220 GLU 106 CONFLICT
SEQADV 1WEJ ASP H 105 PIR S49220 PRO 107 CONFLICT
SEQADV 1WEJ GLU H 119 PIR S49220 LYS 121 CONFLICT
SEQADV 1WEJ THR H 132 PIR S49220 SER 134 CONFLICT
SEQADV 1WEJ LEU H 135 PIR S49220 GLN 137 CONFLICT
SEQADV 1WEJ LYS H 136 PIR S49220 THR 138 CONFLICT
SEQADV 1WEJ SER H 137 PIR S49220 ASN 139 CONFLICT
SEQADV 1WEJ THR H 182 PIR S49220 SER 184 CONFLICT
SEQADV 1WEJ GLN H 195 PIR S49220 GLU 197 CONFLICT
SEQRES 1 L 214 ASP ILE GLN MET THR GLN SER PRO ALA SER LEU SER ALA
SEQRES 2 L 214 SER VAL GLY GLU THR VAL THR ILE THR CYS ARG ALA SER
SEQRES 3 L 214 GLY ASN ILE HIS ASN TYR LEU ALA TRP TYR GLN GLN LYS
SEQRES 4 L 214 GLN GLY LYS SER PRO GLN LEU LEU VAL TYR ASN ALA LYS
SEQRES 5 L 214 THR LEU ALA ASP GLY VAL PRO SER ARG PHE SER GLY SER
SEQRES 6 L 214 GLY SER GLY THR GLN TYR SER LEU LYS ILE ASN SER LEU
SEQRES 7 L 214 GLN PRO GLU ASP PHE GLY SER TYR TYR CYS GLN HIS PHE
SEQRES 8 L 214 TRP SER THR PRO TRP THR PHE GLY GLY GLY THR LYS LEU
SEQRES 9 L 214 GLU ILE LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE
SEQRES 10 L 214 PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA
SEQRES 11 L 214 SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP
SEQRES 12 L 214 ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN
SEQRES 13 L 214 ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS
SEQRES 14 L 214 ASP SER THR TYR SER MET SER SER THR LEU THR LEU THR
SEQRES 15 L 214 LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU
SEQRES 16 L 214 ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER
SEQRES 17 L 214 PHE ASN ARG ASN GLU CYS
SEQRES 1 H 223 GLU VAL GLN LEU GLN GLN SER GLY ALA GLU LEU VAL LYS
SEQRES 2 H 223 PRO GLY ALA SER VAL LYS LEU SER CYS THR ALA SER GLY
SEQRES 3 H 223 PHE ASN ILE LYS ASP THR TYR MET HIS TRP VAL LYS GLN
SEQRES 4 H 223 ARG PRO GLU LYS GLY LEU GLU TRP ILE GLY ARG ILE ASP
SEQRES 5 H 223 PRO ALA SER GLY ASN THR LYS TYR ASP PRO LYS PHE GLN
SEQRES 6 H 223 ASP LYS ALA THR ILE THR ALA ASP THR SER SER ASN THR
SEQRES 7 H 223 ALA TYR LEU GLN LEU SER SER LEU THR SER GLU ASP THR
SEQRES 8 H 223 ALA VAL TYR TYR CYS ALA GLY TYR ASP TYR GLY ASN PHE
SEQRES 9 H 223 ASP TYR TRP GLY GLN GLY THR THR LEU THR VAL SER SER
SEQRES 10 H 223 ALA GLU THR THR PRO PRO SER VAL TYR PRO LEU ALA PRO
SEQRES 11 H 223 GLY THR ALA ALA LEU LYS SER SER MET VAL THR LEU GLY
SEQRES 12 H 223 CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL THR VAL
SEQRES 13 H 223 THR TRP ASN SER GLY SER LEU SER SER GLY VAL HIS THR
SEQRES 14 H 223 PHE PRO ALA VAL LEU GLN SER ASP LEU TYR THR LEU THR
SEQRES 15 H 223 SER SER VAL THR VAL PRO SER SER THR TRP PRO SER GLN
SEQRES 16 H 223 THR VAL THR CYS ASN VAL ALA HIS PRO ALA SER SER THR
SEQRES 17 H 223 LYS VAL ASP LYS LYS ILE VAL PRO ARG ASN CYS GLY GLY
SEQRES 18 H 223 ASP CYS
SEQRES 1 F 105 ACE GLY ASP VAL GLU LYS GLY LYS LYS ILE PHE VAL GLN
SEQRES 2 F 105 LYS CYS ALA GLN CYS HIS THR VAL GLU LYS GLY GLY LYS
SEQRES 3 F 105 HIS LYS THR GLY PRO ASN LEU HIS GLY LEU PHE GLY ARG
SEQRES 4 F 105 LYS THR GLY GLN ALA PRO GLY PHE THR TYR THR ASP ALA
SEQRES 5 F 105 ASN LYS ASN LYS GLY ILE THR TRP LYS GLU GLU THR LEU
SEQRES 6 F 105 MET GLU TYR LEU GLU ASN PRO LYS LYS TYR ILE PRO GLY
SEQRES 7 F 105 THR LYS MET ILE PHE ALA GLY ILE LYS LYS LYS THR GLU
SEQRES 8 F 105 ARG GLU ASP LEU ILE ALA TYR LEU LYS LYS ALA THR ASN
SEQRES 9 F 105 GLU
HET ACE F 0 3
HET ZN L 215 1
HET HEM F 105 42
HETNAM ACE ACETYL GROUP
HETNAM ZN ZINC ION
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETSYN HEM HEME
FORMUL 3 ACE C2 H4 O
FORMUL 4 ZN ZN 2+
FORMUL 5 HEM C34 H32 FE N4 O4
FORMUL 6 HOH *637(H2 O)
HELIX 1 1 PRO L 80 ASP L 82 5 3
HELIX 2 2 SER L 122 SER L 127 1 6
HELIX 3 3 LYS L 183 ARG L 188 1 6
HELIX 4 4 ILE H 29 ASP H 31 5 3
HELIX 5 5 PRO H 62 PHE H 64 5 3
HELIX 6 6 SER H 88 ASP H 90 5 3
HELIX 7 7 THR H 132 LEU H 135 5 4
HELIX 8 8 ASN H 159 GLY H 161 5 3
HELIX 9 9 PRO H 204 SER H 206 5 3
HELIX 10 10 VAL F 3 LYS F 13 1 11
HELIX 11 11 ASP F 50 ASN F 54 1 5
HELIX 12 12 GLU F 61 GLU F 69 1 9
HELIX 13 13 PRO F 71 TYR F 74 1 4
HELIX 14 14 LYS F 88 ALA F 101 1 14
SHEET 1 A 4 MET L 4 SER L 7 0
SHEET 2 A 4 VAL L 19 ALA L 25 -1 N ARG L 24 O THR L 5
SHEET 3 A 4 GLN L 70 ILE L 75 -1 N ILE L 75 O VAL L 19
SHEET 4 A 4 PHE L 62 SER L 67 -1 N SER L 67 O GLN L 70
SHEET 1 B 5 SER L 10 ALA L 13 0
SHEET 2 B 5 THR L 102 ILE L 106 1 N LYS L 103 O LEU L 11
SHEET 3 B 5 GLY L 84 HIS L 90 -1 N TYR L 86 O THR L 102
SHEET 4 B 5 LEU L 33 GLN L 38 -1 N GLN L 38 O SER L 85
SHEET 5 B 5 GLN L 45 VAL L 48 -1 N VAL L 48 O TRP L 35
SHEET 1 C 4 THR L 114 PHE L 118 0
SHEET 2 C 4 GLY L 129 ASN L 137 -1 N ASN L 137 O THR L 114
SHEET 3 C 4 MET L 175 THR L 182 -1 N LEU L 181 O ALA L 130
SHEET 4 C 4 VAL L 159 TRP L 163 -1 N SER L 162 O SER L 176
SHEET 1 D 4 SER L 153 ARG L 155 0
SHEET 2 D 4 ASN L 145 ILE L 150 -1 N ILE L 150 O SER L 153
SHEET 3 D 4 SER L 191 THR L 197 -1 N THR L 197 O ASN L 145
SHEET 4 D 4 ILE L 205 ASN L 210 -1 N PHE L 209 O TYR L 192
SHEET 1 E 4 GLN H 3 GLN H 6 0
SHEET 2 E 4 VAL H 18 SER H 25 -1 N SER H 25 O GLN H 3
SHEET 3 E 4 THR H 78 LEU H 83 -1 N LEU H 83 O VAL H 18
SHEET 4 E 4 ALA H 68 ASP H 73 -1 N ASP H 73 O THR H 78
SHEET 1 F 6 GLU H 10 VAL H 12 0
SHEET 2 F 6 THR H 111 VAL H 115 1 N THR H 114 O GLU H 10
SHEET 3 F 6 ALA H 92 GLY H 98 -1 N TYR H 94 O THR H 111
SHEET 4 F 6 TYR H 33 GLN H 39 -1 N GLN H 39 O VAL H 93
SHEET 5 F 6 LEU H 45 ASP H 52 -1 N ILE H 51 O MET H 34
SHEET 6 F 6 ASN H 57 TYR H 60 -1 N LYS H 59 O ARG H 50
SHEET 1 G 2 ALA H 97 TYR H 99 0
SHEET 2 G 2 ASP H 105 TRP H 107 -1 N TYR H 106 O GLY H 98
SHEET 1 H 4 SER H 124 LEU H 128 0
SHEET 2 H 4 MET H 139 TYR H 149 -1 N LYS H 147 O SER H 124
SHEET 3 H 4 TYR H 179 PRO H 188 -1 N VAL H 187 O VAL H 140
SHEET 4 H 4 VAL H 167 THR H 169 -1 N HIS H 168 O SER H 184
SHEET 1 I 3 THR H 155 TRP H 158 0
SHEET 2 I 3 THR H 198 HIS H 203 -1 N ALA H 202 O THR H 155
SHEET 3 I 3 THR H 208 LYS H 213 -1 N LYS H 212 O CYS H 199
SHEET 1 J 2 VAL H 173 GLN H 175 0
SHEET 2 J 2 LEU H 178 THR H 180 -1 N THR H 180 O VAL H 173
SSBOND 1 CYS L 23 CYS L 88 1555 1555 2.03
SSBOND 2 CYS L 134 CYS L 194 1555 1555 2.02
SSBOND 3 CYS L 214 CYS H 219 1555 1555 2.03
SSBOND 4 CYS H 22 CYS H 96 1555 1555 2.02
SSBOND 5 CYS H 144 CYS H 199 1555 1555 2.03
LINK C ACE F 0 N GLY F 1 1555 1555 1.33
LINK CAB HEM F 105 SG CYS F 14 1555 1555 1.79
LINK CAC HEM F 105 SG CYS F 17 1555 1555 1.78
LINK ZN ZN L 215 OD2 ASP L 151 1555 1555 1.76
LINK ZN ZN L 215 ND1 HIS L 189 1555 1555 2.45
CISPEP 1 SER L 7 PRO L 8 0 -0.33
CISPEP 2 THR L 94 PRO L 95 0 -0.01
CISPEP 3 TYR L 140 PRO L 141 0 -0.06
CISPEP 4 PHE H 150 PRO H 151 0 -0.17
CISPEP 5 GLU H 152 PRO H 153 0 -0.08
CISPEP 6 TRP H 192 PRO H 193 0 0.23
SITE 1 AC1 3 ASP L 151 HIS L 189 HOH L 368
SITE 1 AC2 21 LYS F 13 CYS F 14 GLN F 16 CYS F 17
SITE 2 AC2 21 HIS F 18 THR F 28 GLY F 29 PRO F 30
SITE 3 AC2 21 THR F 40 GLY F 41 TYR F 48 THR F 49
SITE 4 AC2 21 ASN F 52 TRP F 59 TYR F 67 LEU F 68
SITE 5 AC2 21 THR F 78 LYS F 79 MET F 80 PHE F 82
SITE 6 AC2 21 HOH F 208
CRYST1 79.580 72.540 94.380 90.00 90.00 90.00 P 21 21 21 4
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 0.012566 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013785 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010595 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
