HEADER MITOCHONDRIAL ELECTRON TRANSPORT 22-MAR-95 1CRC
TITLE CYTOCHROME C AT LOW IONIC STRENGTH
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME C;
COMPND 3 CHAIN: A, B
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: EQUUS CABALLUS;
SOURCE 3 ORGANISM_COMMON: HORSE;
SOURCE 4 ORGANISM_TAXID: 9796;
SOURCE 5 ORGAN: HEART
KEYWDS FERRIC FORM, LOW IONIC STRENGTH, MITOCHONDRIAL ELECTRON
KEYWDS 2 TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR R.SANISHVILI,K.W.VOLZ,E.M.WESTBROOK,E.MARGOLIASH
REVDAT 2 24-FEB-09 1CRC 1 VERSN
REVDAT 1 08-MAR-96 1CRC 0
JRNL AUTH R.SANISHVILI,K.W.VOLZ,E.M.WESTBROOK,E.MARGOLIASH
JRNL TITL THE LOW IONIC STRENGTH CRYSTAL STRUCTURE OF HORSE
JRNL TITL 2 CYTOCHROME C AT 2.1 A RESOLUTION AND COMPARISON
JRNL TITL 3 WITH ITS HIGH IONIC STRENGTH COUNTERPART.
JRNL REF STRUCTURE V. 3 707 1995
JRNL REFN ISSN 0969-2126
JRNL PMID 8591047
JRNL DOI 10.1016/S0969-2126(01)00205-2
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH R.SANISHVILI,E.MARGOLIASH,M.L.WESTBROOK,
REMARK 1 AUTH 2 E.M.WESTBROOK,K.W.VOLZ
REMARK 1 TITL CRYSTALLIZATION OF WILD-TYPE AND MUTANT
REMARK 1 TITL 2 FERRICYTOCHROMES C AT LOW IONIC STRENGTH: SEEDING
REMARK 1 TITL 3 TECHNIQUE AND X-RAY DIFFRACTION ANALYSIS
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 50 687 1994
REMARK 1 REFN ISSN 0907-4449
REMARK 2
REMARK 2 RESOLUTION. 2.08 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PROFFT, PROLSQ
REMARK 3 AUTHORS : KONNERT,HENDRICKSON,FINZEL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.08
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 60.0
REMARK 3 NUMBER OF REFLECTIONS : 7684
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) : 0.177
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 : 1727
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 86
REMARK 3 SOLVENT ATOMS : 121
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.24
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) : 0.017 ; 0.020
REMARK 3 ANGLE DISTANCE (A) : 0.057 ; 0.040
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : 0.060 ; 0.050
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : 0.012 ; 0.020
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : 0.182 ; 0.150
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : 0.244 ; 0.500
REMARK 3 MULTIPLE TORSION (A) : 0.354 ; 0.500
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : 0.323 ; 0.500
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : 2.000 ; 3.000
REMARK 3 STAGGERED (DEGREES) : 22.000; 15.000
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 0.080 ; 1.000
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 0.100 ; 1.500
REMARK 3 SIDE-CHAIN BOND (A**2) : 0.070 ; 1.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 0.100 ; 0.150
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE SIDE CHAINS OF RESIDUES LYS 72
REMARK 3 AND LYS 87 IN MOLECULE A COULD BE FITTED TO THE ELECTRON
REMARK 3 DENSITY IN MORE THAN ONE CONFORMATION BUT THESE ARE NOT
REMARK 3 CLEARLY EXPRESSED ROTAMERS. THEY ARE IDENTIFIED AS 'C' IN THE
REMARK 3 ALTERNATE LOCATIONS COLUMN. THE SIDE CHAINS OF RESIDUES LYS 8,
REMARK 3 LYS 53, GLU 61, LYS 86 AND LYS 100 IN MOLECULE B HAVE
REMARK 3 ROTAMERS. THEY ARE DESIGNATED 'D' IN THE ALTERNATE
REMARK 3 CONFORMATIONS COLUMN. THE SIDE CHAINS OF RESIDUES LYS 22, LYS
REMARK 3 72 AND LYS 88 IN MOLECULE B COULD BE FITTED TO THE ELECTRON
REMARK 3 DENSITY IN MORE THAN ONE CONFORMATION BUT THESE ARE NOT
REMARK 3 CLEARLY EXPRESSED ROTAMERS. THEY ARE IDENTIFIED AS 'D' IN THE
REMARK 3 ALTERNATE LOCATIONS COLUMN.
REMARK 4
REMARK 4 1CRC 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 : 01-JUL-92
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : XENTRONICS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XENGEN
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 8803
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 (%) : 65.0
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : 0.03960
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 (%): 43.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 27.81000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 17.55500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 52.50500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 17.55500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.81000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 52.50500
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: 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O LYS B 39 O HOH B 110 1.70
REMARK 500 OG1 THR A 49 O2D HEM A 105 2.07
REMARK 500 OD1 ASN B 52 O HOH B 109 2.16
REMARK 500 O THR A 47 NZ LYS A 79 2.18
REMARK 500 OE1 GLU B 4 O HOH B 155 2.18
REMARK 500 O THR B 40 O HOH B 123 2.19
REMARK 500
REMARK 500 REMARK: NULL
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 OE2 GLU B 62 NZ LYS B 86 2654 2.08
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 ASP A 2 CB - CG - OD2 ANGL. DEV. = 10.9 DEGREES
REMARK 500 GLU A 4 CA - CB - CG ANGL. DEV. = 17.0 DEGREES
REMARK 500 VAL A 11 O - C - N ANGL. DEV. = 11.7 DEGREES
REMARK 500 ALA A 15 CB - CA - C ANGL. DEV. = 13.4 DEGREES
REMARK 500 HIS A 18 CB - CA - C ANGL. DEV. = -15.0 DEGREES
REMARK 500 GLU A 21 CG - CD - OE2 ANGL. DEV. = 12.5 DEGREES
REMARK 500 LYS A 22 CD - CE - NZ ANGL. DEV. = -15.9 DEGREES
REMARK 500 ARG A 38 N - CA - CB ANGL. DEV. = -11.6 DEGREES
REMARK 500 ARG A 38 NE - CZ - NH1 ANGL. DEV. = -8.2 DEGREES
REMARK 500 THR A 40 CA - CB - CG2 ANGL. DEV. = 8.8 DEGREES
REMARK 500 GLN A 42 CA - CB - CG ANGL. DEV. = 15.1 DEGREES
REMARK 500 THR A 47 CA - CB - CG2 ANGL. DEV. = 8.4 DEGREES
REMARK 500 ASP A 50 CA - CB - CG ANGL. DEV. = 16.6 DEGREES
REMARK 500 ASP A 50 CB - CG - OD1 ANGL. DEV. = 7.0 DEGREES
REMARK 500 LYS A 53 N - CA - CB ANGL. DEV. = 11.8 DEGREES
REMARK 500 TYR A 67 CB - CG - CD2 ANGL. DEV. = 5.1 DEGREES
REMARK 500 GLU A 69 CG - CD - OE1 ANGL. DEV. = 14.3 DEGREES
REMARK 500 GLU A 69 CG - CD - OE2 ANGL. DEV. = -21.4 DEGREES
REMARK 500 PHE A 82 O - C - N ANGL. DEV. = 11.7 DEGREES
REMARK 500 ARG A 91 NE - CZ - NH1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ASP A 93 CB - CG - OD1 ANGL. DEV. = 6.6 DEGREES
REMARK 500 TYR A 97 CB - CG - CD1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 VAL B 11 CG1 - CB - CG2 ANGL. DEV. = 11.2 DEGREES
REMARK 500 GLN B 16 O - C - N ANGL. DEV. = 11.6 DEGREES
REMARK 500 LYS B 25 CA - CB - CG ANGL. DEV. = 14.1 DEGREES
REMARK 500 PRO B 30 O - C - N ANGL. DEV. = 10.8 DEGREES
REMARK 500 ARG B 38 CD - NE - CZ ANGL. DEV. = 12.1 DEGREES
REMARK 500 PHE B 46 O - C - N ANGL. DEV. = 9.8 DEGREES
REMARK 500 THR B 49 N - CA - CB ANGL. DEV. = 14.8 DEGREES
REMARK 500 ASP B 50 CA - CB - CG ANGL. DEV. = 37.1 DEGREES
REMARK 500 ASP B 50 CB - CG - OD1 ANGL. DEV. = 8.3 DEGREES
REMARK 500 ALA B 51 N - CA - CB ANGL. DEV. = 9.5 DEGREES
REMARK 500 TRP B 59 O - C - N ANGL. DEV. = 11.1 DEGREES
REMARK 500 GLU B 61 OE1 - CD - OE2 ANGL. DEV. = -7.7 DEGREES
REMARK 500 GLU B 62 CG - CD - OE1 ANGL. DEV. = 13.6 DEGREES
REMARK 500 GLU B 62 O - C - N ANGL. DEV. = 12.8 DEGREES
REMARK 500 TYR B 67 O - C - N ANGL. DEV. = 9.9 DEGREES
REMARK 500 LYS B 88 CA - C - O ANGL. DEV. = 14.1 DEGREES
REMARK 500 THR B 89 N - CA - CB ANGL. DEV. = -14.1 DEGREES
REMARK 500 ARG B 91 NE - CZ - NH1 ANGL. DEV. = -8.1 DEGREES
REMARK 500 ARG B 91 NE - CZ - NH2 ANGL. DEV. = 6.5 DEGREES
REMARK 500 GLU B 90 O - C - N ANGL. DEV. = 10.1 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 LYS A 27 -142.25 -115.53
REMARK 500 PHE A 36 104.54 -51.22
REMARK 500 ASN A 70 86.87 -159.81
REMARK 500 PHE A 82 117.32 -165.43
REMARK 500 LYS A 100 -70.21 -69.70
REMARK 500 LYS B 13 -9.37 -165.20
REMARK 500 HIS B 26 135.28 -38.55
REMARK 500 LYS B 27 -147.94 -112.24
REMARK 500 HIS B 33 103.95 -46.78
REMARK 500 TYR B 48 -177.31 -60.49
REMARK 500 THR B 49 -115.49 -69.99
REMARK 500 ASP B 50 -12.34 -167.01
REMARK 500 GLU B 61 -28.50 -38.40
REMARK 500 ASN B 70 82.96 -168.47
REMARK 500 TYR B 74 -72.57 -81.20
REMARK 500 ILE B 75 67.19 -112.22
REMARK 500 LYS B 100 -104.33 -69.73
REMARK 500 ALA B 101 -46.42 -22.57
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 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: (11X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 GLU A 61 24.9 L L OUTSIDE RANGE
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 B 107 DISTANCE = 5.20 ANGSTROMS
REMARK 525 HOH B 146 DISTANCE = 5.53 ANGSTROMS
REMARK 525 HOH A 158 DISTANCE = 5.74 ANGSTROMS
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 COMPND
REMARK 600 MOLECULE: CYTOCHROME C. THE HEME IS OXIDIZED (FE 3+).
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 105 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 18 NE2
REMARK 620 2 MET A 80 SD 171.6
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 105 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 18 NE2
REMARK 620 2 MET B 80 SD 174.4
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 HEM A 105
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 105
DBREF 1CRC A 1 104 UNP P00004 CYC_HORSE 1 104
DBREF 1CRC B 1 104 UNP P00004 CYC_HORSE 1 104
SEQRES 1 A 105 ACE GLY ASP VAL GLU LYS GLY LYS LYS ILE PHE VAL GLN
SEQRES 2 A 105 LYS CYS ALA GLN CYS HIS THR VAL GLU LYS GLY GLY LYS
SEQRES 3 A 105 HIS LYS THR GLY PRO ASN LEU HIS GLY LEU PHE GLY ARG
SEQRES 4 A 105 LYS THR GLY GLN ALA PRO GLY PHE THR TYR THR ASP ALA
SEQRES 5 A 105 ASN LYS ASN LYS GLY ILE THR TRP LYS GLU GLU THR LEU
SEQRES 6 A 105 MET GLU TYR LEU GLU ASN PRO LYS LYS TYR ILE PRO GLY
SEQRES 7 A 105 THR LYS MET ILE PHE ALA GLY ILE LYS LYS LYS THR GLU
SEQRES 8 A 105 ARG GLU ASP LEU ILE ALA TYR LEU LYS LYS ALA THR ASN
SEQRES 9 A 105 GLU
SEQRES 1 B 105 ACE GLY ASP VAL GLU LYS GLY LYS LYS ILE PHE VAL GLN
SEQRES 2 B 105 LYS CYS ALA GLN CYS HIS THR VAL GLU LYS GLY GLY LYS
SEQRES 3 B 105 HIS LYS THR GLY PRO ASN LEU HIS GLY LEU PHE GLY ARG
SEQRES 4 B 105 LYS THR GLY GLN ALA PRO GLY PHE THR TYR THR ASP ALA
SEQRES 5 B 105 ASN LYS ASN LYS GLY ILE THR TRP LYS GLU GLU THR LEU
SEQRES 6 B 105 MET GLU TYR LEU GLU ASN PRO LYS LYS TYR ILE PRO GLY
SEQRES 7 B 105 THR LYS MET ILE PHE ALA GLY ILE LYS LYS LYS THR GLU
SEQRES 8 B 105 ARG GLU ASP LEU ILE ALA TYR LEU LYS LYS ALA THR ASN
SEQRES 9 B 105 GLU
HET ACE A 0 3
HET ACE B 0 3
HET HEM A 105 43
HET HEM B 105 43
HETNAM ACE ACETYL GROUP
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETSYN HEM HEME
FORMUL 1 ACE 2(C2 H4 O)
FORMUL 3 HEM 2(C34 H32 FE N4 O4)
FORMUL 5 HOH *120(H2 O)
HELIX 1 1 ASP A 2 CYS A 14 1 13
HELIX 2 2 THR A 49 LYS A 55 1 7
HELIX 3 3 LYS A 60 GLU A 69 1 10
HELIX 4 4 ASN A 70 ILE A 75 1 6
HELIX 5 5 LYS A 87 GLU A 104 1 18
HELIX 6 6 ASP B 2 CYS B 14 1 13
HELIX 7 7 LYS B 60 GLU B 69 1 10
HELIX 8 8 ASN B 70 ILE B 75 1 6
HELIX 9 9 LYS B 87 GLU B 104 1 18
LINK C ACE A 0 N GLY A 1 1555 1555 1.37
LINK C ACE B 0 N GLY B 1 1555 1555 1.35
LINK SG CYS A 14 CAB HEM A 105 1555 1555 1.81
LINK SG CYS A 17 CAC HEM A 105 1555 1555 1.86
LINK FE HEM A 105 NE2 HIS A 18 1555 1555 2.17
LINK FE HEM A 105 SD MET A 80 1555 1555 2.66
LINK SG CYS B 14 CAB HEM B 105 1555 1555 1.73
LINK SG CYS B 17 CAC HEM B 105 1555 1555 1.79
LINK NE2 HIS B 18 FE HEM B 105 1555 1555 1.96
LINK SD MET B 80 FE HEM B 105 1555 1555 2.02
SITE 1 AC1 20 LYS A 13 CYS A 14 CYS A 17 HIS A 18
SITE 2 AC1 20 GLY A 29 PRO A 30 THR A 40 GLY A 41
SITE 3 AC1 20 TYR A 48 THR A 49 ASN A 52 TRP A 59
SITE 4 AC1 20 TYR A 67 THR A 78 LYS A 79 MET A 80
SITE 5 AC1 20 ILE A 81 PHE A 82 HOH A 107 HOH A 110
SITE 1 AC2 24 LYS A 55 LYS B 13 CYS B 14 CYS B 17
SITE 2 AC2 24 HIS B 18 THR B 28 PRO B 30 LEU B 32
SITE 3 AC2 24 LEU B 35 THR B 40 GLY B 41 GLN B 42
SITE 4 AC2 24 PHE B 46 TYR B 48 THR B 49 ASN B 52
SITE 5 AC2 24 TRP B 59 TYR B 67 THR B 78 LYS B 79
SITE 6 AC2 24 MET B 80 ILE B 81 PHE B 82 HOH B 112
CRYST1 55.620 105.010 35.110 90.00 90.00 90.00 P 21 21 21 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 0.017979 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009523 0.000000 0.00000
SCALE3 0.000000 0.000000 0.028482 0.00000
HETATM 1 C ACE A 0 6.678 30.002 -8.077 1.00 18.66 C
HETATM 2 O ACE A 0 5.617 30.099 -8.722 1.00 17.70 O
HETATM 3 CH3 ACE A 0 8.016 30.384 -8.645 1.00 18.46 C
(ATOM LINES ARE NOT SHOWN.)
END
