HEADER LYASE 07-MAY-13 4KLR
TITLE E343Q VARIANT OF HUMAN FERROCHELATASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FERROCHELATASE, MITOCHONDRIAL;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: HEME SYNTHASE, PROTOHEME FERRO-LYASE;
COMPND 5 EC: 4.99.1.1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: FECH;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS CHELATASE, MITOCHONDRIA, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR W.N.LANZILOTTA,A.E.MEDLOCK
REVDAT 2 28-FEB-24 4KLR 1 REMARK SEQADV LINK
REVDAT 1 18-JUN-14 4KLR 0
JRNL AUTH W.N.LANZILOTTA,A.E.MEDLOCK
JRNL TITL E343Q VARIANT OF HUMAN FERROCHELATASE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.18 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0102
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) : 2.18
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 70.71
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 43881
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) : 0.203
REMARK 3 R VALUE (WORKING SET) : 0.200
REMARK 3 FREE R VALUE : 0.258
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2339
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) : 2.18
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.24
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3217
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.73
REMARK 3 BIN R VALUE (WORKING SET) : 0.2480
REMARK 3 BIN FREE R VALUE SET COUNT : 152
REMARK 3 BIN FREE R VALUE : 0.2890
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5782
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 264
REMARK 3 SOLVENT ATOMS : 341
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.18
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.63000
REMARK 3 B22 (A**2) : -1.68000
REMARK 3 B33 (A**2) : 3.31000
REMARK 3 B12 (A**2) : 0.00000
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): 0.265
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.219
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.149
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.746
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.930
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6308 ; 0.024 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8591 ; 2.213 ; 2.051
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 736 ; 6.817 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 273 ;36.115 ;23.553
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1084 ;19.898 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 46 ;18.656 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 947 ; 0.156 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4672 ; 0.011 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 3643 ; 1.234 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5934 ; 2.238 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2663 ; 3.502 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2646 ; 5.364 ; 4.500
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 : 1.40
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
REMARK 4
REMARK 4 4KLR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-MAY-13.
REMARK 100 THE DEPOSITION ID IS D_1000079497.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-SEP-10
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-BM
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 : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 49841
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 70.710
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.5
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: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
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 (%): 53.48
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALS WERE GROWN USING HANGING DROP
REMARK 280 WITH A PRECIPITATING SOLUTION CONSISTING OF 0.1 BIS-TRIS PH 6.5,
REMARK 280 0.075 M AMMONIUM SULFATE AND 30 % PENTAERYTHRITOL ETHOXYLATE (15/
REMARK 280 4 EO/OH), VAPOR DIFFUSION, HANGING DROP
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 43.06350
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 54.63100
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 46.28050
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 54.63100
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 43.06350
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 46.28050
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: 11370 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28260 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -89.0 KCAL/MOL
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. (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 MET A 54
REMARK 465 GLY A 55
REMARK 465 GLY A 56
REMARK 465 SER A 57
REMARK 465 HIS A 58
REMARK 465 HIS A 59
REMARK 465 HIS A 60
REMARK 465 HIS A 61
REMARK 465 HIS A 62
REMARK 465 HIS A 63
REMARK 465 GLY A 64
REMARK 465 MET B 54
REMARK 465 GLY B 55
REMARK 465 GLY B 56
REMARK 465 SER B 57
REMARK 465 HIS B 58
REMARK 465 HIS B 59
REMARK 465 HIS B 60
REMARK 465 HIS B 61
REMARK 465 HIS B 62
REMARK 465 HIS B 63
REMARK 465 GLY B 64
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 CD LYS A 68 CB ALA A 155 1.55
REMARK 500 SD MET B 308 O12 CHD B 503 1.68
REMARK 500 SD MET B 308 O12 CHD B 503 1.69
REMARK 500 CE MET B 308 O12 CHD B 503 1.74
REMARK 500 SD MET B 308 C12 CHD B 503 1.85
REMARK 500 SD MET B 308 C12 CHD B 503 1.87
REMARK 500 NH1 ARG A 125 O HOH A 738 1.93
REMARK 500 O HOH A 660 O HOH A 666 1.96
REMARK 500 O HOH A 711 O HOH A 742 2.01
REMARK 500 O GLY A 181 O HOH A 717 2.02
REMARK 500 O PRO B 375 N PHE B 377 2.10
REMARK 500 SD MET B 308 C11 CHD B 503 2.12
REMARK 500 OE2 GLU A 289 O HOH A 731 2.14
REMARK 500 CG2 THR A 170 O HOH A 647 2.14
REMARK 500 O ASP A 95 O ASP A 97 2.16
REMARK 500 O HOH B 608 O HOH B 642 2.18
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 NH1 ARG B 125 O HOH B 741 3655 2.02
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 GLU A 255 CB GLU A 255 CG 0.118
REMARK 500 VAL A 269 CB VAL A 269 CG2 0.142
REMARK 500 GLU A 317 CD GLU A 317 OE1 0.070
REMARK 500 CYS B 360 CB CYS B 360 SG -0.104
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 ARG A 125 NE - CZ - NH1 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ARG A 226 NE - CZ - NH1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ARG A 226 NE - CZ - NH2 ANGL. DEV. = -5.0 DEGREES
REMARK 500 ARG A 327 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 PRO B 156 C - N - CA ANGL. DEV. = -10.9 DEGREES
REMARK 500 ARG B 226 NE - CZ - NH1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ARG B 226 NE - CZ - NH2 ANGL. DEV. = -7.1 DEGREES
REMARK 500 PRO B 375 C - N - CA ANGL. DEV. = 11.0 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 66 117.80 92.85
REMARK 500 LEU A 98 -66.87 78.04
REMARK 500 ILE A 103 62.79 37.27
REMARK 500 ASP A 148 -36.84 -38.64
REMARK 500 ALA A 155 -136.80 84.63
REMARK 500 THR A 198 -93.97 -119.47
REMARK 500 TRP A 227 53.38 -156.62
REMARK 500 LYS A 304 137.08 -38.31
REMARK 500 ASN A 372 -93.80 50.62
REMARK 500 ASN A 374 153.23 -21.45
REMARK 500 LYS B 66 118.62 56.57
REMARK 500 ALA B 155 -124.63 70.10
REMARK 500 THR B 198 -91.97 -126.31
REMARK 500 TRP B 227 55.04 -161.94
REMARK 500 SER B 303 -118.38 -84.82
REMARK 500 SER B 303 -116.26 -86.45
REMARK 500 LYS B 304 -156.12 171.73
REMARK 500 VAL B 305 -80.35 -67.42
REMARK 500 ASN B 374 -166.30 -66.64
REMARK 500 PRO B 375 -84.75 -108.20
REMARK 500 LEU B 376 -2.63 -27.60
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ARG A 65 LYS A 66 -148.68
REMARK 500 THR A 154 ALA A 155 142.06
REMARK 500 LEU A 371 ASN A 372 149.29
REMARK 500 THR B 154 ALA B 155 145.62
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 FES A 508 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 196 SG
REMARK 620 2 FES A 508 S1 108.0
REMARK 620 3 FES A 508 S2 107.7 100.5
REMARK 620 4 CYS A 403 SG 100.2 122.3 117.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES A 508 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 406 SG
REMARK 620 2 FES A 508 S1 109.5
REMARK 620 3 FES A 508 S2 111.5 103.5
REMARK 620 4 CYS A 411 SG 107.0 124.3 100.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM A 507 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 IMD A 501 N1
REMARK 620 2 HEM A 507 NA 83.6
REMARK 620 3 HEM A 507 NB 84.0 87.5
REMARK 620 4 HEM A 507 NC 94.9 178.5 92.4
REMARK 620 5 HEM A 507 ND 94.5 90.9 177.9 89.2
REMARK 620 6 BCT A 502 O2 172.7 90.2 91.8 91.2 89.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES B 507 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 196 SG
REMARK 620 2 FES B 507 S1 112.7
REMARK 620 3 FES B 507 S2 110.2 101.7
REMARK 620 4 CYS B 403 SG 99.0 119.1 114.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES B 507 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 406 SG
REMARK 620 2 FES B 507 S1 109.4
REMARK 620 3 FES B 507 S2 109.2 102.7
REMARK 620 4 CYS B 411 SG 105.7 124.7 104.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 506 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 IMD B 501 N1
REMARK 620 2 HEM B 506 NA 81.7
REMARK 620 3 HEM B 506 NB 83.7 88.6
REMARK 620 4 HEM B 506 NC 100.4 177.8 91.1
REMARK 620 5 HEM B 506 ND 98.8 91.1 177.5 89.2
REMARK 620 6 BCT B 502 O1 177.8 98.0 94.2 79.9 83.4
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 IMD A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCT A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CHD A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CHD A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES A 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCT B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CHD B 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CHD B 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CHD B 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES B 507
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4KLA RELATED DB: PDB
REMARK 900 RELATED ID: 4KLC RELATED DB: PDB
DBREF 4KLR A 65 423 UNP P22830 HEMH_HUMAN 65 423
DBREF 4KLR B 65 423 UNP P22830 HEMH_HUMAN 65 423
SEQADV 4KLR MET A 54 UNP P22830 EXPRESSION TAG
SEQADV 4KLR GLY A 55 UNP P22830 EXPRESSION TAG
SEQADV 4KLR GLY A 56 UNP P22830 EXPRESSION TAG
SEQADV 4KLR SER A 57 UNP P22830 EXPRESSION TAG
SEQADV 4KLR HIS A 58 UNP P22830 EXPRESSION TAG
SEQADV 4KLR HIS A 59 UNP P22830 EXPRESSION TAG
SEQADV 4KLR HIS A 60 UNP P22830 EXPRESSION TAG
SEQADV 4KLR HIS A 61 UNP P22830 EXPRESSION TAG
SEQADV 4KLR HIS A 62 UNP P22830 EXPRESSION TAG
SEQADV 4KLR HIS A 63 UNP P22830 EXPRESSION TAG
SEQADV 4KLR GLY A 64 UNP P22830 EXPRESSION TAG
SEQADV 4KLR GLN A 343 UNP P22830 GLU 343 ENGINEERED MUTATION
SEQADV 4KLR MET B 54 UNP P22830 EXPRESSION TAG
SEQADV 4KLR GLY B 55 UNP P22830 EXPRESSION TAG
SEQADV 4KLR GLY B 56 UNP P22830 EXPRESSION TAG
SEQADV 4KLR SER B 57 UNP P22830 EXPRESSION TAG
SEQADV 4KLR HIS B 58 UNP P22830 EXPRESSION TAG
SEQADV 4KLR HIS B 59 UNP P22830 EXPRESSION TAG
SEQADV 4KLR HIS B 60 UNP P22830 EXPRESSION TAG
SEQADV 4KLR HIS B 61 UNP P22830 EXPRESSION TAG
SEQADV 4KLR HIS B 62 UNP P22830 EXPRESSION TAG
SEQADV 4KLR HIS B 63 UNP P22830 EXPRESSION TAG
SEQADV 4KLR GLY B 64 UNP P22830 EXPRESSION TAG
SEQADV 4KLR GLN B 343 UNP P22830 GLU 343 ENGINEERED MUTATION
SEQRES 1 A 370 MET GLY GLY SER HIS HIS HIS HIS HIS HIS GLY ARG LYS
SEQRES 2 A 370 PRO LYS THR GLY ILE LEU MET LEU ASN MET GLY GLY PRO
SEQRES 3 A 370 GLU THR LEU GLY ASP VAL HIS ASP PHE LEU LEU ARG LEU
SEQRES 4 A 370 PHE LEU ASP ARG ASP LEU MET THR LEU PRO ILE GLN ASN
SEQRES 5 A 370 LYS LEU ALA PRO PHE ILE ALA LYS ARG ARG THR PRO LYS
SEQRES 6 A 370 ILE GLN GLU GLN TYR ARG ARG ILE GLY GLY GLY SER PRO
SEQRES 7 A 370 ILE LYS ILE TRP THR SER LYS GLN GLY GLU GLY MET VAL
SEQRES 8 A 370 LYS LEU LEU ASP GLU LEU SER PRO ASN THR ALA PRO HIS
SEQRES 9 A 370 LYS TYR TYR ILE GLY PHE ARG TYR VAL HIS PRO LEU THR
SEQRES 10 A 370 GLU GLU ALA ILE GLU GLU MET GLU ARG ASP GLY LEU GLU
SEQRES 11 A 370 ARG ALA ILE ALA PHE THR GLN TYR PRO GLN TYR SER CYS
SEQRES 12 A 370 SER THR THR GLY SER SER LEU ASN ALA ILE TYR ARG TYR
SEQRES 13 A 370 TYR ASN GLN VAL GLY ARG LYS PRO THR MET LYS TRP SER
SEQRES 14 A 370 THR ILE ASP ARG TRP PRO THR HIS HIS LEU LEU ILE GLN
SEQRES 15 A 370 CYS PHE ALA ASP HIS ILE LEU LYS GLU LEU ASP HIS PHE
SEQRES 16 A 370 PRO LEU GLU LYS ARG SER GLU VAL VAL ILE LEU PHE SER
SEQRES 17 A 370 ALA HIS SER LEU PRO MET SER VAL VAL ASN ARG GLY ASP
SEQRES 18 A 370 PRO TYR PRO GLN GLU VAL SER ALA THR VAL GLN LYS VAL
SEQRES 19 A 370 MET GLU ARG LEU GLU TYR CYS ASN PRO TYR ARG LEU VAL
SEQRES 20 A 370 TRP GLN SER LYS VAL GLY PRO MET PRO TRP LEU GLY PRO
SEQRES 21 A 370 GLN THR ASP GLU SER ILE LYS GLY LEU CYS GLU ARG GLY
SEQRES 22 A 370 ARG LYS ASN ILE LEU LEU VAL PRO ILE ALA PHE THR SER
SEQRES 23 A 370 ASP HIS ILE GLN THR LEU TYR GLU LEU ASP ILE GLU TYR
SEQRES 24 A 370 SER GLN VAL LEU ALA LYS GLU CYS GLY VAL GLU ASN ILE
SEQRES 25 A 370 ARG ARG ALA GLU SER LEU ASN GLY ASN PRO LEU PHE SER
SEQRES 26 A 370 LYS ALA LEU ALA ASP LEU VAL HIS SER HIS ILE GLN SER
SEQRES 27 A 370 ASN GLU LEU CYS SER LYS GLN LEU THR LEU SER CYS PRO
SEQRES 28 A 370 LEU CYS VAL ASN PRO VAL CYS ARG GLU THR LYS SER PHE
SEQRES 29 A 370 PHE THR SER GLN GLN LEU
SEQRES 1 B 370 MET GLY GLY SER HIS HIS HIS HIS HIS HIS GLY ARG LYS
SEQRES 2 B 370 PRO LYS THR GLY ILE LEU MET LEU ASN MET GLY GLY PRO
SEQRES 3 B 370 GLU THR LEU GLY ASP VAL HIS ASP PHE LEU LEU ARG LEU
SEQRES 4 B 370 PHE LEU ASP ARG ASP LEU MET THR LEU PRO ILE GLN ASN
SEQRES 5 B 370 LYS LEU ALA PRO PHE ILE ALA LYS ARG ARG THR PRO LYS
SEQRES 6 B 370 ILE GLN GLU GLN TYR ARG ARG ILE GLY GLY GLY SER PRO
SEQRES 7 B 370 ILE LYS ILE TRP THR SER LYS GLN GLY GLU GLY MET VAL
SEQRES 8 B 370 LYS LEU LEU ASP GLU LEU SER PRO ASN THR ALA PRO HIS
SEQRES 9 B 370 LYS TYR TYR ILE GLY PHE ARG TYR VAL HIS PRO LEU THR
SEQRES 10 B 370 GLU GLU ALA ILE GLU GLU MET GLU ARG ASP GLY LEU GLU
SEQRES 11 B 370 ARG ALA ILE ALA PHE THR GLN TYR PRO GLN TYR SER CYS
SEQRES 12 B 370 SER THR THR GLY SER SER LEU ASN ALA ILE TYR ARG TYR
SEQRES 13 B 370 TYR ASN GLN VAL GLY ARG LYS PRO THR MET LYS TRP SER
SEQRES 14 B 370 THR ILE ASP ARG TRP PRO THR HIS HIS LEU LEU ILE GLN
SEQRES 15 B 370 CYS PHE ALA ASP HIS ILE LEU LYS GLU LEU ASP HIS PHE
SEQRES 16 B 370 PRO LEU GLU LYS ARG SER GLU VAL VAL ILE LEU PHE SER
SEQRES 17 B 370 ALA HIS SER LEU PRO MET SER VAL VAL ASN ARG GLY ASP
SEQRES 18 B 370 PRO TYR PRO GLN GLU VAL SER ALA THR VAL GLN LYS VAL
SEQRES 19 B 370 MET GLU ARG LEU GLU TYR CYS ASN PRO TYR ARG LEU VAL
SEQRES 20 B 370 TRP GLN SER LYS VAL GLY PRO MET PRO TRP LEU GLY PRO
SEQRES 21 B 370 GLN THR ASP GLU SER ILE LYS GLY LEU CYS GLU ARG GLY
SEQRES 22 B 370 ARG LYS ASN ILE LEU LEU VAL PRO ILE ALA PHE THR SER
SEQRES 23 B 370 ASP HIS ILE GLN THR LEU TYR GLU LEU ASP ILE GLU TYR
SEQRES 24 B 370 SER GLN VAL LEU ALA LYS GLU CYS GLY VAL GLU ASN ILE
SEQRES 25 B 370 ARG ARG ALA GLU SER LEU ASN GLY ASN PRO LEU PHE SER
SEQRES 26 B 370 LYS ALA LEU ALA ASP LEU VAL HIS SER HIS ILE GLN SER
SEQRES 27 B 370 ASN GLU LEU CYS SER LYS GLN LEU THR LEU SER CYS PRO
SEQRES 28 B 370 LEU CYS VAL ASN PRO VAL CYS ARG GLU THR LYS SER PHE
SEQRES 29 B 370 PHE THR SER GLN GLN LEU
HET IMD A 501 5
HET BCT A 502 4
HET GOL A 503 12
HET CHD A 504 29
HET CHD A 505 29
HET CL A 506 1
HET HEM A 507 43
HET FES A 508 4
HET IMD B 501 5
HET BCT B 502 4
HET CHD B 503 29
HET CHD B 504 29
HET CHD B 505 29
HET HEM B 506 43
HET FES B 507 4
HETNAM IMD IMIDAZOLE
HETNAM BCT BICARBONATE ION
HETNAM GOL GLYCEROL
HETNAM CHD CHOLIC ACID
HETNAM CL CHLORIDE ION
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM FES FE2/S2 (INORGANIC) CLUSTER
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN HEM HEME
FORMUL 3 IMD 2(C3 H5 N2 1+)
FORMUL 4 BCT 2(C H O3 1-)
FORMUL 5 GOL C3 H8 O3
FORMUL 6 CHD 5(C24 H40 O5)
FORMUL 8 CL CL 1-
FORMUL 9 HEM 2(C34 H32 FE N4 O4)
FORMUL 10 FES 2(FE2 S2)
FORMUL 18 HOH *341(H2 O)
HELIX 1 1 THR A 81 GLY A 83 5 3
HELIX 2 2 ASP A 84 LEU A 94 1 11
HELIX 3 3 ILE A 103 ARG A 125 1 23
HELIX 4 4 PRO A 131 SER A 151 1 21
HELIX 5 5 PRO A 152 ALA A 155 5 4
HELIX 6 6 LEU A 169 ASP A 180 1 12
HELIX 7 7 THR A 198 VAL A 213 1 16
HELIX 8 8 HIS A 230 ASP A 246 1 17
HELIX 9 9 LYS A 252 VAL A 256 5 5
HELIX 10 10 PRO A 266 ARG A 272 1 7
HELIX 11 11 PRO A 275 LEU A 291 1 17
HELIX 12 12 GLN A 314 ARG A 325 1 12
HELIX 13 13 THR A 344 ASP A 349 1 6
HELIX 14 14 ASP A 349 CYS A 360 1 12
HELIX 15 15 PRO A 375 ASN A 392 1 18
HELIX 16 16 SER A 396 LEU A 401 5 6
HELIX 17 17 ASN A 408 SER A 420 1 13
HELIX 18 18 THR B 81 GLY B 83 5 3
HELIX 19 19 ASP B 84 LEU B 94 1 11
HELIX 20 20 ILE B 103 ARG B 125 1 23
HELIX 21 21 PRO B 131 SER B 151 1 21
HELIX 22 22 PRO B 152 ALA B 155 5 4
HELIX 23 23 LEU B 169 ASP B 180 1 12
HELIX 24 24 THR B 198 GLY B 214 1 17
HELIX 25 25 HIS B 230 ASP B 246 1 17
HELIX 26 26 LYS B 252 VAL B 256 5 5
HELIX 27 27 PRO B 266 ARG B 272 1 7
HELIX 28 28 PRO B 275 LEU B 291 1 17
HELIX 29 29 GLN B 314 ARG B 325 1 12
HELIX 30 30 THR B 344 ASP B 349 1 6
HELIX 31 31 ASP B 349 GLY B 361 1 13
HELIX 32 32 LEU B 376 ASN B 392 1 17
HELIX 33 33 SER B 396 LEU B 401 5 6
HELIX 34 34 ASN B 408 SER B 420 1 13
SHEET 1 A 4 HIS A 157 PHE A 163 0
SHEET 2 A 4 THR A 69 ASN A 75 1 N MET A 73 O TYR A 160
SHEET 3 A 4 ARG A 184 THR A 189 1 O PHE A 188 N LEU A 72
SHEET 4 A 4 LYS A 220 ILE A 224 1 O SER A 222 N ALA A 187
SHEET 1 B 4 TYR A 297 GLN A 302 0
SHEET 2 B 4 VAL A 257 HIS A 263 1 N PHE A 260 O VAL A 300
SHEET 3 B 4 ASN A 329 PRO A 334 1 O LEU A 331 N VAL A 257
SHEET 4 B 4 ASN A 364 ARG A 367 1 O ARG A 366 N LEU A 332
SHEET 1 C 4 HIS B 157 PHE B 163 0
SHEET 2 C 4 THR B 69 ASN B 75 1 N ILE B 71 O LYS B 158
SHEET 3 C 4 ARG B 184 THR B 189 1 O PHE B 188 N LEU B 72
SHEET 4 C 4 LYS B 220 ILE B 224 1 O SER B 222 N ALA B 187
SHEET 1 D 4 TYR B 297 GLN B 302 0
SHEET 2 D 4 VAL B 257 HIS B 263 1 N PHE B 260 O VAL B 300
SHEET 3 D 4 ASN B 329 PRO B 334 1 O LEU B 331 N VAL B 257
SHEET 4 D 4 ASN B 364 ARG B 367 1 O ARG B 366 N LEU B 332
LINK SG CYS A 196 FE2 FES A 508 1555 1555 2.33
LINK SG CYS A 403 FE2 FES A 508 1555 1555 2.34
LINK SG CYS A 406 FE1 FES A 508 1555 1555 2.38
LINK SG CYS A 411 FE1 FES A 508 1555 1555 2.32
LINK N1 IMD A 501 FE HEM A 507 1555 1555 1.93
LINK O2 BCT A 502 FE HEM A 507 1555 1555 2.43
LINK SG CYS B 196 FE2 FES B 507 1555 1555 2.32
LINK SG CYS B 403 FE2 FES B 507 1555 1555 2.36
LINK SG CYS B 406 FE1 FES B 507 1555 1555 2.41
LINK SG CYS B 411 FE1 FES B 507 1555 1555 2.33
LINK N1 IMD B 501 FE HEM B 506 1555 1555 2.00
LINK O1 BCT B 502 FE HEM B 506 1555 1555 2.45
CISPEP 1 HIS A 167 PRO A 168 0 -3.40
CISPEP 2 GLY A 312 PRO A 313 0 5.44
CISPEP 3 ASN A 372 GLY A 373 0 -5.25
CISPEP 4 HIS B 167 PRO B 168 0 -5.83
CISPEP 5 GLY B 312 PRO B 313 0 2.47
SITE 1 AC1 5 SER A 264 SER A 303 TRP A 310 HEM A 507
SITE 2 AC1 5 HOH A 618
SITE 1 AC2 4 MET A 76 LEU A 98 TYR A 165 HEM A 507
SITE 1 AC3 11 PRO A 277 GLN A 278 SER A 281 TRP A 301
SITE 2 AC3 11 HOH A 723 HOH A 724 PRO B 277 SER B 281
SITE 3 AC3 11 TRP B 301 HOH B 673 HOH B 733
SITE 1 AC4 11 THR A 100 LEU A 101 ARG A 114 ARG A 115
SITE 2 AC4 11 PRO A 266 SER A 268 VAL A 305 GLY A 306
SITE 3 AC4 11 MET A 308 CHD A 505 HOH A 758
SITE 1 AC5 2 ARG A 114 CHD A 504
SITE 1 AC6 5 LYS A 220 TRP A 221 LEU A 394 GLN A 422
SITE 2 AC6 5 HOH A 756
SITE 1 AC7 19 MET A 76 LEU A 92 PHE A 93 ARG A 115
SITE 2 AC7 19 TYR A 123 SER A 197 THR A 198 HIS A 263
SITE 3 AC7 19 PRO A 266 VAL A 305 ALA A 336 PHE A 337
SITE 4 AC7 19 HIS A 341 ILE A 342 IMD A 501 BCT A 502
SITE 5 AC7 19 HOH A 618 HOH A 619 HOH A 675
SITE 1 AC8 6 CYS A 196 ARG A 272 CYS A 403 CYS A 406
SITE 2 AC8 6 CYS A 411 HOH A 707
SITE 1 AC9 6 HIS B 263 GLN B 302 SER B 303 TRP B 310
SITE 2 AC9 6 HEM B 506 HOH B 665
SITE 1 BC1 4 MET B 76 LEU B 98 TYR B 165 HEM B 506
SITE 1 BC2 9 THR B 100 ARG B 115 PRO B 266 SER B 268
SITE 2 BC2 9 LYS B 304 VAL B 305 GLY B 306 MET B 308
SITE 3 BC2 9 CHD B 504
SITE 1 BC3 4 LYS A 106 PHE A 110 LEU B 101 CHD B 503
SITE 1 BC4 5 GLU B 393 HOH B 620 HOH B 703 HOH B 718
SITE 2 BC4 5 HOH B 751
SITE 1 BC5 17 MET B 76 PHE B 93 LEU B 98 ARG B 115
SITE 2 BC5 17 TYR B 123 SER B 197 THR B 198 HIS B 263
SITE 3 BC5 17 PRO B 266 ALA B 336 HIS B 341 ILE B 342
SITE 4 BC5 17 IMD B 501 BCT B 502 HOH B 656 HOH B 665
SITE 5 BC5 17 HOH B 680
SITE 1 BC6 4 CYS B 196 CYS B 403 CYS B 406 CYS B 411
CRYST1 86.127 92.561 109.262 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 0.011611 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010804 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009152 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
