HEADER OXIDOREDUCTASE/ELECTRON TRANSPORT 01-AUG-07 2JTI
TITLE SOLUTION STRUCTURE OF THE YEAST ISO-1-CYTOCHROME C (T12A) : YEAST
TITLE 2 CYTOCHROME C PEROXIDASE COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME C PEROXIDASE, MITOCHONDRIAL;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CCP;
COMPND 5 EC: 1.11.1.5;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: CYTOCHROME C ISO-1;
COMPND 10 CHAIN: B;
COMPND 11 ENGINEERED: YES;
COMPND 12 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 STRAIN: DBY939;
SOURCE 6 GENE: CCP1, CCP, CPO;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: VECTOR;
SOURCE 11 EXPRESSION_SYSTEM_VECTOR: PT7CCP;
SOURCE 12 MOL_ID: 2;
SOURCE 13 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 14 ORGANISM_COMMON: YEAST;
SOURCE 15 ORGANISM_TAXID: 4932;
SOURCE 16 STRAIN: OVIFORMIS;
SOURCE 17 GENE: CYC1;
SOURCE 18 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 19 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 20 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 21 EXPRESSION_SYSTEM_VECTOR_TYPE: VECTOR;
SOURCE 22 EXPRESSION_SYSTEM_VECTOR: PBTR1
KEYWDS PROTEIN/PROTEIN, HEME, HYDROGEN PEROXIDE, IRON, METAL-BINDING,
KEYWDS 2 MITOCHONDRION, OXIDOREDUCTASE, PEROXIDASE, TRANSIT PEPTIDE, ELECTRON
KEYWDS 3 TRANSPORT, METHYLATION, RESPIRATORY CHAIN, TRANSPORT,
KEYWDS 4 OXIDOREDUCTASE-ELECTRON TRANSPORT COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR M.UBBINK,A.N.VOLKOV
REVDAT 4 20-OCT-21 2JTI 1 REMARK SEQADV LINK
REVDAT 3 15-SEP-10 2JTI 1 JRNL
REVDAT 2 24-FEB-09 2JTI 1 VERSN
REVDAT 1 22-JUL-08 2JTI 0
JRNL AUTH A.N.VOLKOV,Q.BASHIR,J.A.WORRALL,G.M.ULLMANN,M.UBBINK
JRNL TITL SHIFTING THE EQUILIBRIUM BETWEEN THE ENCOUNTER STATE AND THE
JRNL TITL 2 SPECIFIC FORM OF A PROTEIN COMPLEX BY INTERFACIAL POINT
JRNL TITL 3 MUTATIONS.
JRNL REF J.AM.CHEM.SOC. V. 132 11487 2010
JRNL REFN ISSN 0002-7863
JRNL PMID 20672804
JRNL DOI 10.1021/JA100867C
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : TOPSPIN, X-PLOR NIH
REMARK 3 AUTHORS : BRUKER BIOSPIN (TOPSPIN), SCHWIETERS, KUSZEWSKI,
REMARK 3 TJANDRA AND CLORE (X-PLOR NIH)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: COORDINATES OF BOTH PROTEINS WERE TAKEN
REMARK 3 FROM THE PDB ENTRY 2PCC. SEQUENCES DIFFER SLIGHTLY FROM THE
REMARK 3 EXPERIMENT. STRUCTURE REFINEMENT WAS BASED ON PRE-DERIVED
REMARK 3 DISTANCE RESTRAINTS FOR BACKBONE ATOMS AS A SOLE INPUT. ONLY TWO
REMARK 3 ENERGY TERMS, CORRESPONDING TO RESTRAINTS AND VAN DER WAALS
REMARK 3 FORCES, ARE SPECIFIED DURING THE REFINEMENT PROCEDURE, WHICH
REMARK 3 CONSIST OF TWO STEPS. FIRST, A RIGID-BODY DOCKING OF THE PROTEIN
REMARK 3 MOLECULES IS CARRIED OUT WITH VAN DER WAALS PARAMETERS FOR MTSL
REMARK 3 ATOMS SET TO ZERO. FOR EACH RUN PERFORMED, A SINGLE CLUSTER OF
REMARK 3 LOW-ENERGY SOLUTIONS IS CONSISTENTLY PRODUCED. DURING THE SECOND
REMARK 3 STEP, 30 TO 40 BEST STRUCTURES ARE SUBJECTED TO ENERGY
REMARK 3 MINIMIZATION AND SIDE-CHAIN DYNAMICS WITH FIXED POSITIONS OF
REMARK 3 BACKBONE ATOMS FOR BOTH PROTEINS AND ACTIVE VAN DER WAALS
REMARK 3 PARAMETERS FOR MTSL. FOR THE REFINED STRUCTURES, THE ENTIRE
REMARK 3 DOCKING PROCEDURE IS REPEATED UNTIL NO FURTHER REDUCTION IN
REMARK 3 ENERGY IS OBSERVED.
REMARK 4
REMARK 4 2JTI COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-AUG-07.
REMARK 100 THE DEPOSITION ID IS D_1000100270.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 6.00
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.3-0.4 MM [U-15N] CC, 0.3-0.4
REMARK 210 MM CCP, 93% H2O/7% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-15N HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : AZARA, ANSIG, X-PLOR NIH
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 120
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: FOUR SINGLE-CYSTEINE CCP VARIANTS HAVE BEEN PREPARED AND
REMARK 210 LABELLED WITH A PARAMAGNETIC SPIN-LABEL. FOR EACH VARIANT, TWO
REMARK 210 2D [1H,15N] HSQC SPECTRA WERE ACQUIRED, ONE OF THE COMPLEX
REMARK 210 BETWEEN THE SPIN-LABELLED PROTEIN AND 15N CC AND THE OTHER OF
REMARK 210 THE CONTROL SAMPLE CONTAINING THE COMPLEX OF DIAMAGNETICALLY-
REMARK 210 LABELLED CCP WITH 15N CC. FROM THESE, SPIN-LABEL INDUCED
REMARK 210 PARAMAGNETIC RELAXATION ENHANCEMENTS (PRES) OF 15N CC BACKBONE
REMARK 210 AMIDE RESONANCES WERE DETERMINED AND CONVERTED INTO
REMARK 210 INTERMOLECULAR DISTANCE RESTRAINTS, WHICH WERE USED FOR
REMARK 210 SUBSEQUENT STRUCTURE CALCULATION OF THE PROTEIN COMPLEX.
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-10
REMARK 465 RES C SSSEQI
REMARK 465 THR B -4
REMARK 465 GLU B -3
REMARK 465 PHE B -2
REMARK 465 LYS B -1
REMARK 465 ALA B 0
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O ALA A 147 HG2 PRO A 233 1.25
REMARK 500 H THR A 180 O GLY A 189 1.31
REMARK 500 O TYR A 23 H ALA A 27 1.43
REMARK 500 O HIS A 6 H THR A 275 1.47
REMARK 500 O PHE A 262 H PHE A 266 1.54
REMARK 500 O ASN A 38 HB2 ALA B 12 1.55
REMARK 500 O GLU A 214 H GLN A 222 1.57
REMARK 500 O GLN A 255 H PHE A 259 1.59
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 1 GLY B 1 N GLY B 1 CA 0.108
REMARK 500 2 GLY B 1 N GLY B 1 CA 0.110
REMARK 500 3 GLY B 1 N GLY B 1 CA 0.109
REMARK 500 4 GLY B 1 N GLY B 1 CA 0.110
REMARK 500 5 GLY B 1 N GLY B 1 CA 0.109
REMARK 500 6 GLY B 1 N GLY B 1 CA 0.110
REMARK 500 7 GLY B 1 N GLY B 1 CA 0.109
REMARK 500 8 GLY B 1 N GLY B 1 CA 0.110
REMARK 500 9 GLY B 1 N GLY B 1 CA 0.109
REMARK 500 10 GLY B 1 N GLY B 1 CA 0.108
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 1 LEU A 28 O - C - N ANGL. DEV. = 11.3 DEGREES
REMARK 500 1 GLU A 214 O - C - N ANGL. DEV. = 10.7 DEGREES
REMARK 500 1 ASP A 217 O - C - N ANGL. DEV. = 10.4 DEGREES
REMARK 500 1 GLY B 1 N - CA - C ANGL. DEV. = 15.6 DEGREES
REMARK 500 2 LEU A 28 O - C - N ANGL. DEV. = 11.3 DEGREES
REMARK 500 2 GLU A 214 O - C - N ANGL. DEV. = 10.7 DEGREES
REMARK 500 2 ASP A 217 O - C - N ANGL. DEV. = 10.4 DEGREES
REMARK 500 2 GLY B 1 N - CA - C ANGL. DEV. = 15.7 DEGREES
REMARK 500 3 LEU A 28 O - C - N ANGL. DEV. = 11.3 DEGREES
REMARK 500 3 GLU A 214 O - C - N ANGL. DEV. = 10.7 DEGREES
REMARK 500 3 ASP A 217 O - C - N ANGL. DEV. = 10.4 DEGREES
REMARK 500 3 GLY B 1 N - CA - C ANGL. DEV. = 15.6 DEGREES
REMARK 500 4 LEU A 28 O - C - N ANGL. DEV. = 11.3 DEGREES
REMARK 500 4 GLU A 214 O - C - N ANGL. DEV. = 10.7 DEGREES
REMARK 500 4 ASP A 217 O - C - N ANGL. DEV. = 10.4 DEGREES
REMARK 500 4 GLY B 1 N - CA - C ANGL. DEV. = 15.5 DEGREES
REMARK 500 5 LEU A 28 O - C - N ANGL. DEV. = 11.3 DEGREES
REMARK 500 5 GLU A 214 O - C - N ANGL. DEV. = 10.7 DEGREES
REMARK 500 5 ASP A 217 O - C - N ANGL. DEV. = 10.4 DEGREES
REMARK 500 5 GLY B 1 N - CA - C ANGL. DEV. = 15.6 DEGREES
REMARK 500 6 LEU A 28 O - C - N ANGL. DEV. = 11.3 DEGREES
REMARK 500 6 GLU A 214 O - C - N ANGL. DEV. = 10.7 DEGREES
REMARK 500 6 ASP A 217 O - C - N ANGL. DEV. = 10.4 DEGREES
REMARK 500 6 GLY B 1 N - CA - C ANGL. DEV. = 15.7 DEGREES
REMARK 500 7 LEU A 28 O - C - N ANGL. DEV. = 11.3 DEGREES
REMARK 500 7 GLU A 214 O - C - N ANGL. DEV. = 10.7 DEGREES
REMARK 500 7 ASP A 217 O - C - N ANGL. DEV. = 10.4 DEGREES
REMARK 500 7 GLY B 1 N - CA - C ANGL. DEV. = 15.5 DEGREES
REMARK 500 8 LEU A 28 O - C - N ANGL. DEV. = 11.3 DEGREES
REMARK 500 8 GLU A 214 O - C - N ANGL. DEV. = 10.7 DEGREES
REMARK 500 8 ASP A 217 O - C - N ANGL. DEV. = 10.4 DEGREES
REMARK 500 8 GLY B 1 N - CA - C ANGL. DEV. = 15.7 DEGREES
REMARK 500 9 LEU A 28 O - C - N ANGL. DEV. = 11.3 DEGREES
REMARK 500 9 GLU A 214 O - C - N ANGL. DEV. = 10.7 DEGREES
REMARK 500 9 ASP A 217 O - C - N ANGL. DEV. = 10.4 DEGREES
REMARK 500 9 GLY B 1 N - CA - C ANGL. DEV. = 15.6 DEGREES
REMARK 500 10 LEU A 28 O - C - N ANGL. DEV. = 11.3 DEGREES
REMARK 500 10 GLU A 214 O - C - N ANGL. DEV. = 10.7 DEGREES
REMARK 500 10 ASP A 217 O - C - N ANGL. DEV. = 10.4 DEGREES
REMARK 500 10 GLY B 1 N - CA - C ANGL. DEV. = 15.5 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 1 THR A 2 167.48 73.32
REMARK 500 1 LYS A 12 106.44 -40.17
REMARK 500 1 ASP A 33 47.41 -89.15
REMARK 500 1 TYR A 39 36.85 76.76
REMARK 500 1 TYR A 67 -70.15 -24.78
REMARK 500 1 PHE A 99 64.31 -114.52
REMARK 500 1 PRO A 125 151.30 -47.53
REMARK 500 1 PRO A 134 152.02 -45.57
REMARK 500 1 ASP A 148 43.24 -80.44
REMARK 500 1 ASN A 162 38.16 82.14
REMARK 500 1 ASN A 219 14.01 88.99
REMARK 500 1 CYS B 14 -158.66 -107.06
REMARK 500 1 LEU B 15 -42.57 86.49
REMARK 500 1 LYS B 27 -86.97 -82.37
REMARK 500 1 ASN B 56 83.98 44.58
REMARK 500 2 THR A 2 167.48 73.32
REMARK 500 2 LYS A 12 106.44 -40.17
REMARK 500 2 ASP A 33 47.41 -89.15
REMARK 500 2 TYR A 39 36.85 76.76
REMARK 500 2 TYR A 67 -70.15 -24.78
REMARK 500 2 PHE A 99 64.31 -114.52
REMARK 500 2 PRO A 125 151.30 -47.53
REMARK 500 2 PRO A 134 152.02 -45.57
REMARK 500 2 ASP A 148 43.24 -80.44
REMARK 500 2 ASN A 162 38.16 82.14
REMARK 500 2 ASN A 219 14.01 88.99
REMARK 500 2 ALA B 12 -58.04 -121.81
REMARK 500 2 CYS B 14 -161.13 -105.63
REMARK 500 2 LEU B 15 -43.52 89.28
REMARK 500 2 LYS B 27 -80.75 -81.21
REMARK 500 2 ASN B 56 83.14 45.65
REMARK 500 2 ASP B 60 -168.12 -113.56
REMARK 500 3 THR A 2 167.48 73.32
REMARK 500 3 LYS A 12 106.44 -40.17
REMARK 500 3 ASP A 33 47.41 -89.15
REMARK 500 3 TYR A 39 36.85 76.76
REMARK 500 3 TYR A 67 -70.15 -24.78
REMARK 500 3 PHE A 99 64.31 -114.52
REMARK 500 3 PRO A 125 151.30 -47.53
REMARK 500 3 PRO A 134 152.02 -45.57
REMARK 500 3 ASP A 148 43.24 -80.44
REMARK 500 3 ASN A 162 38.16 82.14
REMARK 500 3 ASN A 219 14.01 88.99
REMARK 500 3 CYS B 14 -160.01 -107.63
REMARK 500 3 LEU B 15 -41.96 87.39
REMARK 500 3 LYS B 27 -88.66 -81.75
REMARK 500 3 ASN B 56 83.26 44.06
REMARK 500 3 CYS B 102 79.50 -102.65
REMARK 500 4 THR A 2 167.48 73.32
REMARK 500 4 LYS A 12 106.44 -40.17
REMARK 500
REMARK 500 THIS ENTRY HAS 162 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 1 ARG A 14 0.32 SIDE CHAIN
REMARK 500 1 ARG A 31 0.29 SIDE CHAIN
REMARK 500 1 ARG A 48 0.25 SIDE CHAIN
REMARK 500 1 ARG A 72 0.30 SIDE CHAIN
REMARK 500 1 ARG A 127 0.30 SIDE CHAIN
REMARK 500 1 ARG A 130 0.29 SIDE CHAIN
REMARK 500 1 ARG A 143 0.32 SIDE CHAIN
REMARK 500 1 ARG A 155 0.30 SIDE CHAIN
REMARK 500 1 ARG A 160 0.30 SIDE CHAIN
REMARK 500 1 ARG A 166 0.32 SIDE CHAIN
REMARK 500 1 ARG B 13 0.31 SIDE CHAIN
REMARK 500 1 ARG B 38 0.30 SIDE CHAIN
REMARK 500 1 ARG B 91 0.31 SIDE CHAIN
REMARK 500 2 ARG A 14 0.33 SIDE CHAIN
REMARK 500 2 ARG A 31 0.30 SIDE CHAIN
REMARK 500 2 ARG A 48 0.26 SIDE CHAIN
REMARK 500 2 ARG A 72 0.31 SIDE CHAIN
REMARK 500 2 ARG A 127 0.30 SIDE CHAIN
REMARK 500 2 ARG A 130 0.31 SIDE CHAIN
REMARK 500 2 ARG A 143 0.31 SIDE CHAIN
REMARK 500 2 ARG A 155 0.31 SIDE CHAIN
REMARK 500 2 ARG A 160 0.30 SIDE CHAIN
REMARK 500 2 ARG A 166 0.32 SIDE CHAIN
REMARK 500 2 ARG B 13 0.31 SIDE CHAIN
REMARK 500 2 ARG B 38 0.31 SIDE CHAIN
REMARK 500 2 ARG B 91 0.31 SIDE CHAIN
REMARK 500 3 ARG A 14 0.32 SIDE CHAIN
REMARK 500 3 ARG A 31 0.29 SIDE CHAIN
REMARK 500 3 ARG A 48 0.25 SIDE CHAIN
REMARK 500 3 ARG A 72 0.30 SIDE CHAIN
REMARK 500 3 ARG A 127 0.30 SIDE CHAIN
REMARK 500 3 ARG A 130 0.29 SIDE CHAIN
REMARK 500 3 ARG A 143 0.32 SIDE CHAIN
REMARK 500 3 ARG A 155 0.30 SIDE CHAIN
REMARK 500 3 ARG A 160 0.30 SIDE CHAIN
REMARK 500 3 ARG A 166 0.32 SIDE CHAIN
REMARK 500 3 ARG B 13 0.32 SIDE CHAIN
REMARK 500 3 ARG B 38 0.30 SIDE CHAIN
REMARK 500 3 ARG B 91 0.31 SIDE CHAIN
REMARK 500 4 ARG A 14 0.32 SIDE CHAIN
REMARK 500 4 ARG A 31 0.29 SIDE CHAIN
REMARK 500 4 ARG A 48 0.25 SIDE CHAIN
REMARK 500 4 ARG A 72 0.30 SIDE CHAIN
REMARK 500 4 ARG A 127 0.30 SIDE CHAIN
REMARK 500 4 ARG A 130 0.29 SIDE CHAIN
REMARK 500 4 ARG A 143 0.32 SIDE CHAIN
REMARK 500 4 ARG A 155 0.30 SIDE CHAIN
REMARK 500 4 ARG A 160 0.30 SIDE CHAIN
REMARK 500 4 ARG A 166 0.32 SIDE CHAIN
REMARK 500 4 ARG B 13 0.32 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 130 PLANE DEVIATIONS.
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 HEM A 295 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 175 NE2
REMARK 620 2 HEM A 295 NA 102.1
REMARK 620 3 HEM A 295 NB 99.7 90.1
REMARK 620 4 HEM A 295 NC 90.4 167.5 87.5
REMARK 620 5 HEM A 295 ND 95.4 87.9 164.9 91.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEC B 104 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 18 NE2
REMARK 620 2 HEC B 104 NA 88.9
REMARK 620 3 HEC B 104 NB 81.0 92.9
REMARK 620 4 HEC B 104 NC 83.0 171.7 87.2
REMARK 620 5 HEC B 104 ND 88.1 88.3 169.0 90.0
REMARK 620 6 MET B 80 SD 175.1 87.2 102.0 100.9 89.0
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 295
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC B 104
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2GB8 RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF WT CC-CCP COMPLEX
REMARK 900 RELATED ID: 2PCC RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF WT CC-CCP COMPLEX
REMARK 900 RELATED ID: 1YCC RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF YEAST ISO-1-CYTOCHROME C
REMARK 900 RELATED ID: 1ZBY RELATED DB: PDB
REMARK 900 HIGH-RESOLUTION CRYSTAL STRUCTURE OF YEAST CYTOCHROME C PEROXIDASE
DBREF 2JTI A 1 294 UNP P00431 CCPR_YEAST 68 361
DBREF 2JTI B -4 103 UNP P00044 CYC1_YEAST 2 109
SEQADV 2JTI ILE A 53 UNP P00431 THR 120 VARIANT
SEQADV 2JTI GLY A 152 UNP P00431 ASP 219 VARIANT
SEQADV 2JTI ALA B 12 UNP P00044 THR 18 ENGINEERED MUTATION
SEQRES 1 A 294 THR THR PRO LEU VAL HIS VAL ALA SER VAL GLU LYS GLY
SEQRES 2 A 294 ARG SER TYR GLU ASP PHE GLN LYS VAL TYR ASN ALA ILE
SEQRES 3 A 294 ALA LEU LYS LEU ARG GLU ASP ASP GLU TYR ASP ASN TYR
SEQRES 4 A 294 ILE GLY TYR GLY PRO VAL LEU VAL ARG LEU ALA TRP HIS
SEQRES 5 A 294 ILE SER GLY THR TRP ASP LYS HIS ASP ASN THR GLY GLY
SEQRES 6 A 294 SER TYR GLY GLY THR TYR ARG PHE LYS LYS GLU PHE ASN
SEQRES 7 A 294 ASP PRO SER ASN ALA GLY LEU GLN ASN GLY PHE LYS PHE
SEQRES 8 A 294 LEU GLU PRO ILE HIS LYS GLU PHE PRO TRP ILE SER SER
SEQRES 9 A 294 GLY ASP LEU PHE SER LEU GLY GLY VAL THR ALA VAL GLN
SEQRES 10 A 294 GLU MET GLN GLY PRO LYS ILE PRO TRP ARG CYS GLY ARG
SEQRES 11 A 294 VAL ASP THR PRO GLU ASP THR THR PRO ASP ASN GLY ARG
SEQRES 12 A 294 LEU PRO ASP ALA ASP LYS ASP ALA GLY TYR VAL ARG THR
SEQRES 13 A 294 PHE PHE GLN ARG LEU ASN MET ASN ASP ARG GLU VAL VAL
SEQRES 14 A 294 ALA LEU MET GLY ALA HIS ALA LEU GLY LYS THR HIS LEU
SEQRES 15 A 294 LYS ASN SER GLY TYR GLU GLY PRO TRP GLY ALA ALA ASN
SEQRES 16 A 294 ASN VAL PHE THR ASN GLU PHE TYR LEU ASN LEU LEU ASN
SEQRES 17 A 294 GLU ASP TRP LYS LEU GLU LYS ASN ASP ALA ASN ASN GLU
SEQRES 18 A 294 GLN TRP ASP SER LYS SER GLY TYR MET MET LEU PRO THR
SEQRES 19 A 294 ASP TYR SER LEU ILE GLN ASP PRO LYS TYR LEU SER ILE
SEQRES 20 A 294 VAL LYS GLU TYR ALA ASN ASP GLN ASP LYS PHE PHE LYS
SEQRES 21 A 294 ASP PHE SER LYS ALA PHE GLU LYS LEU LEU GLU ASN GLY
SEQRES 22 A 294 ILE THR PHE PRO LYS ASP ALA PRO SER PRO PHE ILE PHE
SEQRES 23 A 294 LYS THR LEU GLU GLU GLN GLY LEU
SEQRES 1 B 108 THR GLU PHE LYS ALA GLY SER ALA LYS LYS GLY ALA THR
SEQRES 2 B 108 LEU PHE LYS ALA ARG CYS LEU GLN CYS HIS THR VAL GLU
SEQRES 3 B 108 LYS GLY GLY PRO HIS LYS VAL GLY PRO ASN LEU HIS GLY
SEQRES 4 B 108 ILE PHE GLY ARG HIS SER GLY GLN ALA GLU GLY TYR SER
SEQRES 5 B 108 TYR THR ASP ALA ASN ILE LYS LYS ASN VAL LEU TRP ASP
SEQRES 6 B 108 GLU ASN ASN MET SER GLU TYR LEU THR ASN PRO LYS LYS
SEQRES 7 B 108 TYR ILE PRO GLY THR LYS MET ALA PHE GLY GLY LEU LYS
SEQRES 8 B 108 LYS GLU LYS ASP ARG ASN ASP LEU ILE THR TYR LEU LYS
SEQRES 9 B 108 LYS ALA CYS GLU
HET HEM A 295 73
HET HEC B 104 75
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM HEC HEME C
HETSYN HEM HEME
FORMUL 3 HEM C34 H32 FE N4 O4
FORMUL 4 HEC C34 H34 FE N4 O4
HELIX 1 1 SER A 15 ASP A 33 1 19
HELIX 2 2 GLU A 35 ILE A 40 1 6
HELIX 3 3 TYR A 42 GLY A 55 1 14
HELIX 4 4 GLY A 69 ARG A 72 5 4
HELIX 5 5 PHE A 73 ASN A 78 1 6
HELIX 6 6 ASP A 79 GLY A 84 5 6
HELIX 7 7 LEU A 85 PHE A 99 1 15
HELIX 8 8 SER A 103 MET A 119 1 17
HELIX 9 9 PRO A 134 THR A 138 5 5
HELIX 10 10 ASP A 150 LEU A 161 1 12
HELIX 11 11 ASN A 164 GLY A 173 1 10
HELIX 12 12 ALA A 174 LEU A 177 5 4
HELIX 13 13 HIS A 181 GLY A 186 1 6
HELIX 14 14 ASN A 200 GLU A 209 1 10
HELIX 15 15 LEU A 232 ASP A 241 1 10
HELIX 16 16 TYR A 244 ASP A 254 1 11
HELIX 17 17 ASP A 254 ASN A 272 1 19
HELIX 18 18 LEU A 289 GLY A 293 5 5
HELIX 19 19 ALA B 3 LYS B 11 1 9
HELIX 20 20 THR B 49 LYS B 54 1 6
HELIX 21 21 ASN B 63 ASN B 70 1 8
HELIX 22 22 ASN B 70 ILE B 75 1 6
HELIX 23 23 LYS B 87 CYS B 102 1 16
SHEET 1 A 2 LYS A 179 THR A 180 0
SHEET 2 A 2 GLY A 189 PRO A 190 -1 O GLY A 189 N THR A 180
SHEET 1 B 3 TRP A 211 LYS A 215 0
SHEET 2 B 3 GLU A 221 SER A 225 -1 O GLN A 222 N GLU A 214
SHEET 3 B 3 MET A 230 MET A 231 -1 O MET A 231 N TRP A 223
LINK SG CYS B 14 CAB HEC B 104 1555 1555 2.25
LINK SG CYS B 17 CAC HEC B 104 1555 1555 2.35
LINK NE2 HIS A 175 FE HEM A 295 1555 1555 1.93
LINK NE2 HIS B 18 FE HEC B 104 1555 1555 1.92
LINK SD MET B 80 FE HEC B 104 1555 1555 2.23
SITE 1 AC1 17 PRO A 44 VAL A 47 ARG A 48 PRO A 145
SITE 2 AC1 17 ASP A 146 ALA A 147 ALA A 174 HIS A 175
SITE 3 AC1 17 LEU A 177 GLY A 178 LYS A 179 THR A 180
SITE 4 AC1 17 HIS A 181 ASN A 184 SER A 185 TRP A 191
SITE 5 AC1 17 THR A 234
SITE 1 AC2 19 ALA A 193 ALA A 194 CYS B 14 CYS B 17
SITE 2 AC2 19 HIS B 18 VAL B 28 PRO B 30 ILE B 35
SITE 3 AC2 19 SER B 40 GLY B 41 TYR B 46 TYR B 48
SITE 4 AC2 19 THR B 49 ASN B 52 TRP B 59 LEU B 68
SITE 5 AC2 19 LYS B 79 MET B 80 PHE B 82
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
(ATOM LINES ARE NOT SHOWN.)
END
