HEADER ELECTRON TRANSPORT (HEME PROTEIN) 15-FEB-93 1CTY
TITLE MUTATION OF TYROSINE-67 IN CYTOCHROME C SIGNIFICANTLY ALTERS THE LOCAL
TITLE 2 HEME ENVIRONMENT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME C;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932
KEYWDS ELECTRON TRANSPORT (HEME PROTEIN)
EXPDTA X-RAY DIFFRACTION
AUTHOR A.M.BERGHUIS,G.D.BRAYER
REVDAT 4 03-MAR-21 1CTY 1 COMPND REMARK SEQADV HET
REVDAT 4 2 1 HETNAM HETSYN FORMUL LINK
REVDAT 4 3 1 ATOM
REVDAT 3 29-NOV-17 1CTY 1 HELIX
REVDAT 2 24-FEB-09 1CTY 1 VERSN
REVDAT 1 15-JUL-93 1CTY 0
JRNL AUTH A.M.BERGHUIS,J.G.GUILLEMETTE,M.SMITH,G.D.BRAYER
JRNL TITL MUTATION OF TYROSINE-67 TO PHENYLALANINE IN CYTOCHROME C
JRNL TITL 2 SIGNIFICANTLY ALTERS THE LOCAL HEME ENVIRONMENT.
JRNL REF J.MOL.BIOL. V. 235 1326 1994
JRNL REFN ISSN 0022-2836
JRNL PMID 8308895
JRNL DOI 10.1006/JMBI.1994.1086
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.M.BERGHUIS,G.D.BRAYER
REMARK 1 TITL OXIDATION STATE-DEPENDENT CONFORMATIONAL CHANGES IN
REMARK 1 TITL 2 CYTOCHROME C
REMARK 1 REF J.MOL.BIOL. V. 223 959 1992
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 2
REMARK 1 AUTH G.V.LOUIE,G.D.BRAYER
REMARK 1 TITL HIGH-RESOLUTION REFINEMENT OF YEAST ISO-1-CYTOCHROME C AND
REMARK 1 TITL 2 COMPARISONS WITH OTHER EUKARYOTIC CYTOCHROMES C
REMARK 1 REF J.MOL.BIOL. V. 214 527 1990
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 3
REMARK 1 AUTH G.V.LOUIE,G.D.BRAYER
REMARK 1 TITL A POLYPEPTIDE CHAIN-REFOLDING EVENT OCCURS IN THE GLY82
REMARK 1 TITL 2 VARIANT OF YEAST ISO-1-CYTOCHROME C
REMARK 1 REF J.MOL.BIOL. V. 210 313 1989
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 4
REMARK 1 AUTH C.J.LEUNG,B.T.NALL,G.D.BRAYER
REMARK 1 TITL CRYSTALLIZATION OF YEAST ISO-2-CYTOCHROME C USING A NOVEL
REMARK 1 TITL 2 HAIR SEEDING TECHNIQUE
REMARK 1 REF J.MOL.BIOL. V. 206 783 1989
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 5
REMARK 1 AUTH G.V.LOUIE,W.L.B.HUTCHEON,G.D.BRAYER
REMARK 1 TITL YEAST ISO-1-CYTOCHROME C. A 2.8 ANGSTROM RESOLUTION
REMARK 1 TITL 2 THREE-DIMENSIONAL STRUCTURE DETERMINATION
REMARK 1 REF J.MOL.BIOL. V. 199 295 1988
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 6
REMARK 1 AUTH G.V.LOUIE,G.J.PIELAK,M.SMITH,G.D.BRAYER
REMARK 1 TITL ROLE OF PHENYLALANINE-82 IN YEAST ISO-1-CYTOCHROME C AND
REMARK 1 TITL 2 REMOTE CONFORMATIONAL CHANGES INDUCED BY A SERINE RESIDUE AT
REMARK 1 TITL 3 THIS POSITION
REMARK 1 REF BIOCHEMISTRY V. 27 7870 1988
REMARK 1 REFN ISSN 0006-2960
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PROLSQ
REMARK 3 AUTHORS : KONNERT,HENDRICKSON
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : NULL
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 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 + TEST SET) : 0.196
REMARK 3 R VALUE (WORKING SET) : NULL
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
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 850
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 48
REMARK 3 SOLVENT ATOMS : 30
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 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.020 ; NULL
REMARK 3 ANGLE DISTANCE (A) : 0.046 ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; 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 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1CTY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000172532.
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: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 35.85
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.92
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
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 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 69.54000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 18.23500
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 18.23500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 104.31000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 18.23500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 18.23500
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 34.77000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 18.23500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 18.23500
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 104.31000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 18.23500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 18.23500
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 34.77000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 69.54000
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 400
REMARK 400 COMPOUND
REMARK 400 THIS PROTEIN HAS BEEN STABILIZED FOR ANALYSES BY THE
REMARK 400 MUTATION OF CYSTEINE 102 TO A THREONINE RESIDUE.
REMARK 400
REMARK 400 IN TURN T5 THE H-BOND IS MEDIATED THROUGH A WATER MOLECULE.
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 CG2 THR A -5 O ASN A 56 7555 1.66
REMARK 500 CG2 THR A -5 C ASN A 56 7555 1.88
REMARK 500
REMARK 500 REMARK: NULL
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 GLY A 29 N GLY A 29 CA 0.094
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 LEU A 9 CB - CA - C ANGL. DEV. = 12.1 DEGREES
REMARK 500 LEU A 9 CA - CB - CG ANGL. DEV. = 15.7 DEGREES
REMARK 500 PHE A 10 O - C - N ANGL. DEV. = 10.6 DEGREES
REMARK 500 CYS A 14 CA - CB - SG ANGL. DEV. = 11.9 DEGREES
REMARK 500 GLU A 21 CA - CB - CG ANGL. DEV. = 14.0 DEGREES
REMARK 500 GLU A 21 OE1 - CD - OE2 ANGL. DEV. = 7.5 DEGREES
REMARK 500 ARG A 38 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 GLU A 44 OE1 - CD - OE2 ANGL. DEV. = 9.7 DEGREES
REMARK 500 GLU A 44 CG - CD - OE2 ANGL. DEV. = -12.1 DEGREES
REMARK 500 ASP A 50 CB - CG - OD2 ANGL. DEV. = 5.9 DEGREES
REMARK 500 LEU A 58 CB - CA - C ANGL. DEV. = 19.4 DEGREES
REMARK 500 ASP A 60 CB - CG - OD2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 TYR A 74 CB - CG - CD1 ANGL. DEV. = -3.9 DEGREES
REMARK 500 LYS A 89 O - C - N ANGL. DEV. = 9.8 DEGREES
REMARK 500 ARG A 91 NE - CZ - NH2 ANGL. DEV. = -5.1 DEGREES
REMARK 500 ASP A 93 CB - CG - OD1 ANGL. DEV. = 11.1 DEGREES
REMARK 500 ASP A 93 CB - CG - OD2 ANGL. DEV. = -6.1 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 GLU A -4 40.54 -147.71
REMARK 500 LYS A 27 -131.15 -134.58
REMARK 500 ASN A 70 102.12 -163.18
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 HEC A 104 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 18 NE2
REMARK 620 2 HEC A 104 NA 90.4
REMARK 620 3 HEC A 104 NB 90.9 89.7
REMARK 620 4 HEC A 104 NC 88.8 178.9 89.5
REMARK 620 5 HEC A 104 ND 87.6 91.9 177.8 88.9
REMARK 620 6 MET A 80 SD 172.0 95.6 94.4 85.3 86.9
REMARK 620 N 1 2 3 4 5
REMARK 650
REMARK 650 HELIX
REMARK 650 THE END OF THE 50 HELIX (RESIDUE 55) IS DISTORTED.
REMARK 700
REMARK 700 SHEET
REMARK 700 RESIDUES IN SHEET S1 FORM A HIGHLY DISTORTED BETA TYPE
REMARK 700 CONFORMATION.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 117
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC A 104
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1YCC RELATED DB: PDB
REMARK 900 REDUCED - WILD-TYPE
REMARK 900 RELATED ID: 2YCC RELATED DB: PDB
REMARK 900 OXIDIZED - C102T MUTANT
REMARK 900 RELATED ID: 1CTZ RELATED DB: PDB
REMARK 900 REDUCED - Y67F, C102T MUTANT
DBREF 1CTY A -5 103 UNP P00044 CYC1_YEAST 1 108
SEQADV 1CTY PHE A 67 UNP P00044 TYR 72 CONFLICT
SEQADV 1CTY THR A 102 UNP P00044 CYS 107 CONFLICT
SEQRES 1 A 108 THR GLU PHE LYS ALA GLY SER ALA LYS LYS GLY ALA THR
SEQRES 2 A 108 LEU PHE LYS THR ARG CYS LEU GLN CYS HIS THR VAL GLU
SEQRES 3 A 108 LYS GLY GLY PRO HIS LYS VAL GLY PRO ASN LEU HIS GLY
SEQRES 4 A 108 ILE PHE GLY ARG HIS SER GLY GLN ALA GLU GLY TYR SER
SEQRES 5 A 108 TYR THR ASP ALA ASN ILE LYS LYS ASN VAL LEU TRP ASP
SEQRES 6 A 108 GLU ASN ASN MET SER GLU PHE LEU THR ASN PRO M3L LYS
SEQRES 7 A 108 TYR ILE PRO GLY THR LYS MET ALA PHE GLY GLY LEU LYS
SEQRES 8 A 108 LYS GLU LYS ASP ARG ASN ASP LEU ILE THR TYR LEU LYS
SEQRES 9 A 108 LYS ALA THR GLU
MODRES 1CTY M3L A 72 LYS N-TRIMETHYLLYSINE
HET M3L A 72 12
HET SO4 A 117 5
HET HEC A 104 43
HETNAM M3L N-TRIMETHYLLYSINE
HETNAM SO4 SULFATE ION
HETNAM HEC HEME C
FORMUL 1 M3L C9 H21 N2 O2 1+
FORMUL 2 SO4 O4 S 2-
FORMUL 3 HEC C34 H34 FE N4 O4
FORMUL 4 HOH *30(H2 O)
HELIX 1 NT SER A 2 CYS A 14 1 13
HELIX 2 50 THR A 49 LYS A 55 1RESIDUE 55 DISTORTED 7
HELIX 3 60 ASP A 60 ASN A 70 1 11
HELIX 4 70 ASN A 70 ILE A 75 1 6
HELIX 5 CT LYS A 87 THR A 102 1 16
SHEET 1 S1 2 GLY A 37 SER A 40 0
SHEET 2 S1 2 VAL A 57 TRP A 59 -1 O VAL A 57 N SER A 40
LINK SG CYS A 14 CAB HEC A 104 1555 1555 1.79
LINK SG CYS A 17 CAC HEC A 104 1555 1555 1.77
LINK C PRO A 71 N M3L A 72 1555 1555 1.31
LINK C M3L A 72 N LYS A 73 1555 1555 1.29
LINK NE2 HIS A 18 FE HEC A 104 1555 1555 2.05
LINK SD MET A 80 FE HEC A 104 1555 1555 2.44
SITE 1 AC1 7 GLY A 1 SER A 2 ALA A 3 LYS A 4
SITE 2 AC1 7 SER A 47 LYS A 73 HOH A 164
SITE 1 AC2 21 ARG A 13 CYS A 14 CYS A 17 HIS A 18
SITE 2 AC2 21 GLY A 23 GLY A 29 ILE A 35 SER A 40
SITE 3 AC2 21 GLY A 41 TYR A 48 THR A 49 ASN A 52
SITE 4 AC2 21 TRP A 59 MET A 64 PHE A 67 LEU A 68
SITE 5 AC2 21 THR A 78 LYS A 79 MET A 80 LEU A 94
SITE 6 AC2 21 HOH A 121
CRYST1 36.470 36.470 139.080 90.00 90.00 90.00 P 43 21 2 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 0.027420 0.000000 0.000000 0.00000
SCALE2 0.000000 0.027420 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007190 0.00000
(ATOM LINES ARE NOT SHOWN.)
END