HEADER ELECTRON TRANSPORT 07-NOV-13 4CDY
TITLE SPECTROSCOPICALLY-VALIDATED STRUCTURE OF CYTOCHROME C PRIME FROM
TITLE 2 ALCALIGENES XYLOSOXIDANS, REDUCED BY X-RAY IRRADIATION AT 160K
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME C';
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CYTOCHROME C PRIME;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ACHROMOBACTER XYLOSOXIDANS;
SOURCE 3 ORGANISM_TAXID: 85698;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS ELECTRON TRANSPORT, RESONANCE RAMAN, VALIDATION, GAS SENSOR, LIGAND
KEYWDS 2 DISCRIMINATION, FERRIC, HAEM, HEME, RADIOLYSIS
EXPDTA X-RAY DIFFRACTION
AUTHOR D.KEKILLI,F.DWORKOWSKI,S.ANTONYUK,M.A.HOUGH
REVDAT 3 20-DEC-23 4CDY 1 REMARK
REVDAT 2 11-MAR-20 4CDY 1 REMARK SEQRES LINK
REVDAT 1 21-MAY-14 4CDY 0
JRNL AUTH D.KEKILLI,F.S.DWORKOWSKI,G.POMPIDOR,M.R.FUCHS,C.R.ANDREW,
JRNL AUTH 2 S.ANTONYUK,R.W.STRANGE,R.R.EADY,S.S.HASNAIN,M.A.HOUGH
JRNL TITL FINGERPRINTING REDOX AND LIGAND STATES IN HAEMPROTEIN
JRNL TITL 2 CRYSTAL STRUCTURES USING RESONANCE RAMAN SPECTROSCOPY.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 70 1289 2014
JRNL REFN ISSN 0907-4449
JRNL PMID 24816098
JRNL DOI 10.1107/S1399004714004039
REMARK 2
REMARK 2 RESOLUTION. 1.77 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0032
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.77
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.03
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 3 NUMBER OF REFLECTIONS : 14900
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.206
REMARK 3 R VALUE (WORKING SET) : 0.204
REMARK 3 FREE R VALUE : 0.239
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 785
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.77
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.82
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1061
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.47
REMARK 3 BIN R VALUE (WORKING SET) : 0.2740
REMARK 3 BIN FREE R VALUE SET COUNT : 56
REMARK 3 BIN FREE R VALUE : 0.2900
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 949
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 43
REMARK 3 SOLVENT ATOMS : 41
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.67
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.60000
REMARK 3 B22 (A**2) : 0.60000
REMARK 3 B33 (A**2) : -1.94000
REMARK 3 B12 (A**2) : 0.60000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.116
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.115
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.080
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.521
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.956
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.941
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1047 ; 0.012 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 973 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1434 ; 2.073 ; 2.046
REMARK 3 BOND ANGLES OTHERS (DEGREES): 2236 ; 0.893 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 135 ; 4.926 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 42 ;30.602 ;23.571
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 159 ;13.066 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 7 ;17.617 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 142 ; 0.095 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1284 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 239 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 522 ; 2.566 ; 3.416
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 521 ; 2.564 ; 3.410
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 657 ; 3.541 ; 5.099
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 525 ; 2.910 ; 3.556
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS. U VALUES REFINED INDIVIDUALLY
REMARK 4
REMARK 4 4CDY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 07-NOV-13.
REMARK 100 THE DEPOSITION ID IS D_1290058883.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-MAR-13
REMARK 200 TEMPERATURE (KELVIN) : 160
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15687
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.770
REMARK 200 RESOLUTION RANGE LOW (A) : 45.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : 0.05000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.77
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.87
REMARK 200 COMPLETENESS FOR SHELL (%) : 79.4
REMARK 200 DATA REDUNDANCY IN SHELL : 4.40
REMARK 200 R MERGE FOR SHELL (I) : 0.70000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 2YLI
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.63
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, HEPES PH 7.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
REMARK 290 7555 Y,X,-Z+2/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+1/3
REMARK 290 10555 -Y,-X,-Z+1/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+5/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 121.14933
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 60.57467
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 90.86200
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 30.28733
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 151.43667
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 121.14933
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 60.57467
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 30.28733
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 90.86200
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 151.43667
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3620 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12670 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -52.6 KCAL/MOL
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 BIOMT1 2 0.500000 -0.866025 0.000000 26.81150
REMARK 350 BIOMT2 2 -0.866025 -0.500000 0.000000 46.43888
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 30.28733
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 LYS A 127
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 LYS A 31 NZ
REMARK 480 GLU A 46 CD OE1 OE2
REMARK 480 LYS A 49 CD CE NZ
REMARK 480 ASP A 75 OD1 OD2
REMARK 480 ALA A 77 CB
REMARK 480 LYS A 80 NZ
REMARK 480 GLN A 81 NE2
REMARK 480 ASP A 98 OD2
REMARK 480 ASP A 101 OD1 OD2
REMARK 480 ASP A 103 CG OD1 OD2
REMARK 480 LYS A 104 NZ
REMARK 480 LYS A 117 CE NZ
REMARK 480 LYS A 126 CB CG CD CE NZ
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 SG CYS A 119 CAC HEC A 1127 2.07
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 A1127 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 120 NE2
REMARK 620 2 HEC A1127 NA 101.0
REMARK 620 3 HEC A1127 NB 94.5 88.0
REMARK 620 4 HEC A1127 NC 94.6 164.4 90.1
REMARK 620 5 HEC A1127 ND 99.6 90.5 165.8 87.5
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC A 1127
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4CDV RELATED DB: PDB
REMARK 900 SPECTROSCOPICALLY-VALIDATED STRUCTURE OF CYTOCHROME C PRIME FROM
REMARK 900 ALCALIGENES XYLOSOXIDANS, REDUCED BY X-RAY IRRADIATION AT 100K
DBREF 4CDY A 1 127 UNP P00138 CYCP_ALCXX 1 127
SEQRES 1 A 127 PCA PHE ALA LYS PRO GLU ASP ALA VAL LYS TYR ARG GLN
SEQRES 2 A 127 SER ALA LEU THR LEU MET ALA SER HIS PHE GLY ARG MET
SEQRES 3 A 127 THR PRO VAL VAL LYS GLY GLN ALA PRO TYR ASP ALA ALA
SEQRES 4 A 127 GLN ILE LYS ALA ASN VAL GLU VAL LEU LYS THR LEU SER
SEQRES 5 A 127 ALA LEU PRO TRP ALA ALA PHE GLY PRO GLY THR GLU GLY
SEQRES 6 A 127 GLY ASP ALA ARG PRO GLU ILE TRP SER ASP ALA ALA SER
SEQRES 7 A 127 PHE LYS GLN LYS GLN GLN ALA PHE GLN ASP ASN ILE VAL
SEQRES 8 A 127 LYS LEU SER ALA ALA ALA ASP ALA GLY ASP LEU ASP LYS
SEQRES 9 A 127 LEU ARG ALA ALA PHE GLY ASP VAL GLY ALA SER CYS LYS
SEQRES 10 A 127 ALA CYS HIS ASP ALA TYR ARG LYS LYS LYS
MODRES 4CDY PCA A 1 GLU PYROGLUTAMIC ACID
HET PCA A 1 8
HET HEC A1127 43
HETNAM PCA PYROGLUTAMIC ACID
HETNAM HEC HEME C
FORMUL 1 PCA C5 H7 N O3
FORMUL 2 HEC C34 H34 FE N4 O4
FORMUL 3 HOH *41(H2 O)
HELIX 1 1 LYS A 4 ARG A 25 1 22
HELIX 2 2 MET A 26 LYS A 31 1 6
HELIX 3 3 ASP A 37 ALA A 53 1 17
HELIX 4 4 PRO A 55 PHE A 59 5 5
HELIX 5 5 PRO A 70 ASP A 75 1 6
HELIX 6 6 ASP A 75 GLY A 100 1 26
HELIX 7 7 ASP A 101 ARG A 124 1 24
LINK C PCA A 1 N PHE A 2 1555 1555 1.33
LINK NE2 HIS A 120 FE HEC A1127 1555 1555 2.15
SITE 1 AC1 17 ARG A 12 GLN A 13 LEU A 16 THR A 17
SITE 2 AC1 17 ALA A 20 TRP A 56 ASP A 67 ILE A 72
SITE 3 AC1 17 GLN A 83 PHE A 86 CYS A 116 CYS A 119
SITE 4 AC1 17 HIS A 120 TYR A 123 ARG A 124 HOH A2004
SITE 5 AC1 17 HOH A2041
CRYST1 53.623 53.623 181.724 90.00 90.00 120.00 P 65 2 2 12
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 0.018649 0.010767 0.000000 0.00000
SCALE2 0.000000 0.021534 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005503 0.00000
HETATM 1 N PCA A 1 -5.451 24.284 28.217 1.00 36.21 N
HETATM 2 CA PCA A 1 -5.655 23.458 27.035 1.00 37.34 C
HETATM 3 CB PCA A 1 -6.004 24.494 25.962 1.00 38.19 C
HETATM 4 CG PCA A 1 -5.587 25.854 26.511 1.00 36.10 C
HETATM 5 CD PCA A 1 -5.324 25.562 27.982 1.00 36.43 C
HETATM 6 OE PCA A 1 -5.054 26.407 28.817 1.00 34.92 O
HETATM 7 C PCA A 1 -4.418 22.727 26.647 1.00 39.89 C
HETATM 8 O PCA A 1 -4.374 22.123 25.595 1.00 44.38 O
(ATOM LINES ARE NOT SHOWN.)
END
