HEADER OXIDOREDUCTASE 02-OCT-15 5FIW
TITLE CRYSTAL STRUCTURE OF HUMAN MYELOPEROXIDASE AT 1.7 ANGSTROMS RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MYELOPEROXIDASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 167-271;
COMPND 5 SYNONYM: MPO;
COMPND 6 EC: 1.11.2.2;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: MYELOPEROXIDASE;
COMPND 9 CHAIN: C, D;
COMPND 10 FRAGMENT: UNP RESIDUES 279-744;
COMPND 11 SYNONYM: MPO;
COMPND 12 EC: 1.11.2.2
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 CELL: NEUTROPHILS;
SOURCE 6 MOL_ID: 2;
SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 8 ORGANISM_COMMON: HUMAN;
SOURCE 9 ORGANISM_TAXID: 9606;
SOURCE 10 CELL: NEUTROPHILS
KEYWDS OXIDOREDUCTASE, HEME-DEPENDENT PEROXIDASE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.BONNEFOND,J.CAVARELLI
REVDAT 3 10-JAN-24 5FIW 1 HETSYN
REVDAT 2 29-JUL-20 5FIW 1 CAVEAT COMPND REMARK HETNAM
REVDAT 2 2 1 LINK SITE ATOM
REVDAT 1 14-OCT-15 5FIW 0
JRNL AUTH L.BONNEFOND,J.CAVARELLI
JRNL TITL CRYSTAL STRUCTURE OF HUMAN MYELOPEROXIDASE AT 1.7 ANGSTROMS
JRNL TITL 2 RESOLUTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0131
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) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 95.31
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 131551
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) : 0.164
REMARK 3 R VALUE (WORKING SET) : 0.163
REMARK 3 FREE R VALUE : 0.193
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 6869
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) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.75
REMARK 3 REFLECTION IN BIN (WORKING SET) : 9401
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.94
REMARK 3 BIN R VALUE (WORKING SET) : 0.3730
REMARK 3 BIN FREE R VALUE SET COUNT : 481
REMARK 3 BIN FREE R VALUE : 0.3810
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9114
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 291
REMARK 3 SOLVENT ATOMS : 926
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.24
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.23000
REMARK 3 B22 (A**2) : -0.23000
REMARK 3 B33 (A**2) : 0.46000
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): 0.096
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.094
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.067
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.179
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.968
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.953
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9674 ; 0.017 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 9100 ; 0.006 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 13138 ; 1.770 ; 1.998
REMARK 3 BOND ANGLES OTHERS (DEGREES): 20870 ; 1.328 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1132 ; 6.133 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 466 ;33.376 ;22.918
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1564 ;12.336 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 108 ;16.226 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1426 ; 0.130 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 10834 ; 0.013 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 2332 ; 0.012 ; 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): 4546 ; 2.763 ; 1.966
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 4545 ; 2.763 ; 1.966
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5668 ; 3.494 ; 2.933
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 5669 ; 3.494 ; 2.934
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 5128 ; 5.511 ; 2.450
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 5128 ; 5.511 ; 2.450
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 7471 ; 7.360 ; 3.486
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 11687 ; 8.375 ;17.213
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 11259 ; 8.368 ;16.735
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 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 2
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 1 102 B 1 102 9240 0.07 0.05
REMARK 3 2 C 114 577 D 114 577 58282 0.06 0.05
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 : 1.10
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 5FIW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-OCT-15.
REMARK 100 THE DEPOSITION ID IS D_1290065188.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-JUL-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SOLEIL
REMARK 200 BEAMLINE : PROXIMA 1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9786
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS CBF
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 138420
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 52.900
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 8.400
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.76
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.60
REMARK 200 R MERGE FOR SHELL (I) : 1.24000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.080
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 1CXP
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.54
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG 3350, 100 MM NACL, PH 6
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 112.76000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 52.58000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 52.58000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 169.14000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 52.58000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 52.58000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 56.38000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 52.58000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 52.58000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 169.14000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 52.58000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 52.58000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 56.38000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 112.76000
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 14990 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22810 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -99.3 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, E
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 14700 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22670 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -86.5 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D, F
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 ALA B 104
REMARK 465 ALA B 105
REMARK 465 VAL C 113
REMARK 465 ALA C 578
REMARK 465 VAL D 113
REMARK 465 ALA D 578
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 HOH C 2007 O HOH C 2253 1.88
REMARK 500 O6 BMA E 3 C1 BMA C 644 2.00
REMARK 500 O6 BMA F 3 C1 BMA D 644 2.02
REMARK 500 NH2 ARG D 202 O HOH D 2099 2.07
REMARK 500 O HOH D 2195 O HOH D 2337 2.16
REMARK 500 ND2 ASN C 157 O HOH C 2060 2.16
REMARK 500 O HOH D 2006 O HOH D 2255 2.19
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 D 116 CG GLU D 116 CD 0.092
REMARK 500 GLU D 116 CD GLU D 116 OE2 0.107
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 B 17 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 MET C 175 CG - SD - CE ANGL. DEV. = -11.1 DEGREES
REMARK 500 MET C 243 CG - SD - CE ANGL. DEV. = 13.0 DEGREES
REMARK 500 ASP C 347 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ARG C 382 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 MET D 243 CG - SD - CE ANGL. DEV. = 14.0 DEGREES
REMARK 500 ARG D 358 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG D 382 NE - CZ - NH1 ANGL. DEV. = 3.1 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 SER A 42 -41.44 -150.72
REMARK 500 SER B 42 -39.08 -153.23
REMARK 500 ASN C 206 57.59 38.04
REMARK 500 ASN C 356 67.98 -119.33
REMARK 500 ASN C 457 97.67 -165.65
REMARK 500 ASN C 555 3.57 -150.90
REMARK 500 ASN D 206 57.13 37.63
REMARK 500 ARG D 314 -70.99 -109.65
REMARK 500 ARG D 333 2.91 -67.85
REMARK 500 ASN D 356 69.87 -119.83
REMARK 500 ASN D 457 97.43 -166.54
REMARK 500 ASN D 555 4.38 -154.81
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 C2005 DISTANCE = 5.90 ANGSTROMS
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 BMA C 644
REMARK 610 BMA D 644
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 CA C 601 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 96 O
REMARK 620 2 ASP A 96 OD1 71.3
REMARK 620 3 THR C 168 OG1 136.9 144.2
REMARK 620 4 THR C 168 O 75.7 144.9 70.5
REMARK 620 5 PHE C 170 O 102.8 79.9 106.7 96.3
REMARK 620 6 ASP C 172 OD1 143.6 73.4 73.5 140.7 79.4
REMARK 620 7 SER C 174 OG 84.6 77.7 83.4 110.9 152.7 79.5
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM A 605 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 336 NE2
REMARK 620 2 HEM A 605 NA 102.1
REMARK 620 3 HEM A 605 NB 91.5 89.8
REMARK 620 4 HEM A 605 NC 86.3 170.0 84.5
REMARK 620 5 HEM A 605 ND 95.6 95.3 170.2 89.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 701 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 96 OD1
REMARK 620 2 ASP B 96 O 71.9
REMARK 620 3 THR D 168 OG1 142.9 136.4
REMARK 620 4 THR D 168 O 146.3 75.7 69.9
REMARK 620 5 PHE D 170 O 81.7 102.6 107.1 96.8
REMARK 620 6 ASP D 172 OD1 72.6 143.6 73.7 140.6 79.7
REMARK 620 7 SER D 174 OG 75.3 83.9 83.9 110.4 152.8 79.7
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 605 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 336 NE2
REMARK 620 2 HEM B 605 NA 100.6
REMARK 620 3 HEM B 605 NB 91.6 83.3
REMARK 620 4 HEM B 605 NC 87.8 169.5 90.2
REMARK 620 5 HEM B 605 ND 96.6 91.0 170.8 94.3
REMARK 620 N 1 2 3 4
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 RESIDUES 167 TO 270
REMARK 999 RESIDUES 279 TO 744
DBREF 5FIW A 1 105 UNP P05164 PERM_HUMAN 167 271
DBREF 5FIW B 1 105 UNP P05164 PERM_HUMAN 167 271
DBREF 5FIW C 113 578 UNP P05164 PERM_HUMAN 279 744
DBREF 5FIW D 113 578 UNP P05164 PERM_HUMAN 279 744
SEQRES 1 A 105 CYS PRO GLU GLN ASP LYS TYR ARG THR ILE THR GLY MET
SEQRES 2 A 105 CYS ASN ASN ARG ARG SER PRO THR LEU GLY ALA SER ASN
SEQRES 3 A 105 ARG ALA PHE VAL ARG TRP LEU PRO ALA GLU TYR GLU ASP
SEQRES 4 A 105 GLY PHE SER LEU PRO TYR GLY TRP THR PRO GLY VAL LYS
SEQRES 5 A 105 ARG ASN GLY PHE PRO VAL ALA LEU ALA ARG ALA VAL SER
SEQRES 6 A 105 ASN GLU ILE VAL ARG PHE PRO THR ASP GLN LEU THR PRO
SEQRES 7 A 105 ASP GLN GLU ARG SER LEU MET PHE MET GLN TRP GLY GLN
SEQRES 8 A 105 LEU LEU ASP HIS ASP LEU ASP PHE THR PRO GLU PRO ALA
SEQRES 9 A 105 ALA
SEQRES 1 B 105 CYS PRO GLU GLN ASP LYS TYR ARG THR ILE THR GLY MET
SEQRES 2 B 105 CYS ASN ASN ARG ARG SER PRO THR LEU GLY ALA SER ASN
SEQRES 3 B 105 ARG ALA PHE VAL ARG TRP LEU PRO ALA GLU TYR GLU ASP
SEQRES 4 B 105 GLY PHE SER LEU PRO TYR GLY TRP THR PRO GLY VAL LYS
SEQRES 5 B 105 ARG ASN GLY PHE PRO VAL ALA LEU ALA ARG ALA VAL SER
SEQRES 6 B 105 ASN GLU ILE VAL ARG PHE PRO THR ASP GLN LEU THR PRO
SEQRES 7 B 105 ASP GLN GLU ARG SER LEU MET PHE MET GLN TRP GLY GLN
SEQRES 8 B 105 LEU LEU ASP HIS ASP LEU ASP PHE THR PRO GLU PRO ALA
SEQRES 9 B 105 ALA
SEQRES 1 C 466 VAL ASN CYS GLU THR SER CYS VAL GLN GLN PRO PRO CYS
SEQRES 2 C 466 PHE PRO LEU LYS ILE PRO PRO ASN ASP PRO ARG ILE LYS
SEQRES 3 C 466 ASN GLN ALA ASP CYS ILE PRO PHE PHE ARG SER CSO PRO
SEQRES 4 C 466 ALA CYS PRO GLY SER ASN ILE THR ILE ARG ASN GLN ILE
SEQRES 5 C 466 ASN ALA LEU THR SER PHE VAL ASP ALA SER MET VAL TYR
SEQRES 6 C 466 GLY SER GLU GLU PRO LEU ALA ARG ASN LEU ARG ASN MET
SEQRES 7 C 466 SER ASN GLN LEU GLY LEU LEU ALA VAL ASN GLN ARG PHE
SEQRES 8 C 466 GLN ASP ASN GLY ARG ALA LEU LEU PRO PHE ASP ASN LEU
SEQRES 9 C 466 HIS ASP ASP PRO CYS LEU LEU THR ASN ARG SER ALA ARG
SEQRES 10 C 466 ILE PRO CYS PHE LEU ALA GLY ASP THR ARG SER SER GLU
SEQRES 11 C 466 MET PRO GLU LEU THR SER MET HIS THR LEU LEU LEU ARG
SEQRES 12 C 466 GLU HIS ASN ARG LEU ALA THR GLU LEU LYS SER LEU ASN
SEQRES 13 C 466 PRO ARG TRP ASP GLY GLU ARG LEU TYR GLN GLU ALA ARG
SEQRES 14 C 466 LYS ILE VAL GLY ALA MET VAL GLN ILE ILE THR TYR ARG
SEQRES 15 C 466 ASP TYR LEU PRO LEU VAL LEU GLY PRO THR ALA MET ARG
SEQRES 16 C 466 LYS TYR LEU PRO THR TYR ARG SER TYR ASN ASP SER VAL
SEQRES 17 C 466 ASP PRO ARG ILE ALA ASN VAL PHE THR ASN ALA PHE ARG
SEQRES 18 C 466 TYR GLY HIS THR LEU ILE GLN PRO PHE MET PHE ARG LEU
SEQRES 19 C 466 ASP ASN ARG TYR GLN PRO MET GLU PRO ASN PRO ARG VAL
SEQRES 20 C 466 PRO LEU SER ARG VAL PHE PHE ALA SER TRP ARG VAL VAL
SEQRES 21 C 466 LEU GLU GLY GLY ILE ASP PRO ILE LEU ARG GLY LEU MET
SEQRES 22 C 466 ALA THR PRO ALA LYS LEU ASN ARG GLN ASN GLN ILE ALA
SEQRES 23 C 466 VAL ASP GLU ILE ARG GLU ARG LEU PHE GLU GLN VAL MET
SEQRES 24 C 466 ARG ILE GLY LEU ASP LEU PRO ALA LEU ASN MET GLN ARG
SEQRES 25 C 466 SER ARG ASP HIS GLY LEU PRO GLY TYR ASN ALA TRP ARG
SEQRES 26 C 466 ARG PHE CYS GLY LEU PRO GLN PRO GLU THR VAL GLY GLN
SEQRES 27 C 466 LEU GLY THR VAL LEU ARG ASN LEU LYS LEU ALA ARG LYS
SEQRES 28 C 466 LEU MET GLU GLN TYR GLY THR PRO ASN ASN ILE ASP ILE
SEQRES 29 C 466 TRP MET GLY GLY VAL SER GLU PRO LEU LYS ARG LYS GLY
SEQRES 30 C 466 ARG VAL GLY PRO LEU LEU ALA CYS ILE ILE GLY THR GLN
SEQRES 31 C 466 PHE ARG LYS LEU ARG ASP GLY ASP ARG PHE TRP TRP GLU
SEQRES 32 C 466 ASN GLU GLY VAL PHE SER MET GLN GLN ARG GLN ALA LEU
SEQRES 33 C 466 ALA GLN ILE SER LEU PRO ARG ILE ILE CYS ASP ASN THR
SEQRES 34 C 466 GLY ILE THR THR VAL SER LYS ASN ASN ILE PHE MET SER
SEQRES 35 C 466 ASN SER TYR PRO ARG ASP PHE VAL ASN CYS SER THR LEU
SEQRES 36 C 466 PRO ALA LEU ASN LEU ALA SER TRP ARG GLU ALA
SEQRES 1 D 466 VAL ASN CYS GLU THR SER CYS VAL GLN GLN PRO PRO CYS
SEQRES 2 D 466 PHE PRO LEU LYS ILE PRO PRO ASN ASP PRO ARG ILE LYS
SEQRES 3 D 466 ASN GLN ALA ASP CYS ILE PRO PHE PHE ARG SER CSO PRO
SEQRES 4 D 466 ALA CYS PRO GLY SER ASN ILE THR ILE ARG ASN GLN ILE
SEQRES 5 D 466 ASN ALA LEU THR SER PHE VAL ASP ALA SER MET VAL TYR
SEQRES 6 D 466 GLY SER GLU GLU PRO LEU ALA ARG ASN LEU ARG ASN MET
SEQRES 7 D 466 SER ASN GLN LEU GLY LEU LEU ALA VAL ASN GLN ARG PHE
SEQRES 8 D 466 GLN ASP ASN GLY ARG ALA LEU LEU PRO PHE ASP ASN LEU
SEQRES 9 D 466 HIS ASP ASP PRO CYS LEU LEU THR ASN ARG SER ALA ARG
SEQRES 10 D 466 ILE PRO CYS PHE LEU ALA GLY ASP THR ARG SER SER GLU
SEQRES 11 D 466 MET PRO GLU LEU THR SER MET HIS THR LEU LEU LEU ARG
SEQRES 12 D 466 GLU HIS ASN ARG LEU ALA THR GLU LEU LYS SER LEU ASN
SEQRES 13 D 466 PRO ARG TRP ASP GLY GLU ARG LEU TYR GLN GLU ALA ARG
SEQRES 14 D 466 LYS ILE VAL GLY ALA MET VAL GLN ILE ILE THR TYR ARG
SEQRES 15 D 466 ASP TYR LEU PRO LEU VAL LEU GLY PRO THR ALA MET ARG
SEQRES 16 D 466 LYS TYR LEU PRO THR TYR ARG SER TYR ASN ASP SER VAL
SEQRES 17 D 466 ASP PRO ARG ILE ALA ASN VAL PHE THR ASN ALA PHE ARG
SEQRES 18 D 466 TYR GLY HIS THR LEU ILE GLN PRO PHE MET PHE ARG LEU
SEQRES 19 D 466 ASP ASN ARG TYR GLN PRO MET GLU PRO ASN PRO ARG VAL
SEQRES 20 D 466 PRO LEU SER ARG VAL PHE PHE ALA SER TRP ARG VAL VAL
SEQRES 21 D 466 LEU GLU GLY GLY ILE ASP PRO ILE LEU ARG GLY LEU MET
SEQRES 22 D 466 ALA THR PRO ALA LYS LEU ASN ARG GLN ASN GLN ILE ALA
SEQRES 23 D 466 VAL ASP GLU ILE ARG GLU ARG LEU PHE GLU GLN VAL MET
SEQRES 24 D 466 ARG ILE GLY LEU ASP LEU PRO ALA LEU ASN MET GLN ARG
SEQRES 25 D 466 SER ARG ASP HIS GLY LEU PRO GLY TYR ASN ALA TRP ARG
SEQRES 26 D 466 ARG PHE CYS GLY LEU PRO GLN PRO GLU THR VAL GLY GLN
SEQRES 27 D 466 LEU GLY THR VAL LEU ARG ASN LEU LYS LEU ALA ARG LYS
SEQRES 28 D 466 LEU MET GLU GLN TYR GLY THR PRO ASN ASN ILE ASP ILE
SEQRES 29 D 466 TRP MET GLY GLY VAL SER GLU PRO LEU LYS ARG LYS GLY
SEQRES 30 D 466 ARG VAL GLY PRO LEU LEU ALA CYS ILE ILE GLY THR GLN
SEQRES 31 D 466 PHE ARG LYS LEU ARG ASP GLY ASP ARG PHE TRP TRP GLU
SEQRES 32 D 466 ASN GLU GLY VAL PHE SER MET GLN GLN ARG GLN ALA LEU
SEQRES 33 D 466 ALA GLN ILE SER LEU PRO ARG ILE ILE CYS ASP ASN THR
SEQRES 34 D 466 GLY ILE THR THR VAL SER LYS ASN ASN ILE PHE MET SER
SEQRES 35 D 466 ASN SER TYR PRO ARG ASP PHE VAL ASN CYS SER THR LEU
SEQRES 36 D 466 PRO ALA LEU ASN LEU ALA SER TRP ARG GLU ALA
MODRES 5FIW ASN C 189 ASN GLYCOSYLATION SITE
MODRES 5FIW ASN C 225 ASN GLYCOSYLATION SITE
MODRES 5FIW ASN C 317 ASN GLYCOSYLATION SITE
MODRES 5FIW ASN D 189 ASN GLYCOSYLATION SITE
MODRES 5FIW ASN D 225 ASN GLYCOSYLATION SITE
MODRES 5FIW ASN D 317 ASN GLYCOSYLATION SITE
MODRES 5FIW CSO C 150 CYS S-HYDROXYCYSTEINE
MODRES 5FIW CSO D 150 CYS S-HYDROXYCYSTEINE
HET CSO C 150 7
HET CSO D 150 7
HET NAG E 1 14
HET NAG E 2 14
HET BMA E 3 11
HET MAN E 4 11
HET FUC E 5 10
HET NAG F 1 14
HET NAG F 2 14
HET BMA F 3 11
HET MAN F 4 11
HET FUC F 5 10
HET CL A 602 1
HET HEM A 605 43
HET CL B 201 1
HET HEM B 605 43
HET CA C 601 1
HET CL C 611 1
HET CL C 612 1
HET NAG C 620 14
HET NAG C 630 14
HET BMA C 644 11
HET CL D 612 1
HET NAG D 620 14
HET NAG D 630 14
HET BMA D 644 11
HET CA D 701 1
HETNAM CSO S-HYDROXYCYSTEINE
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
HETNAM FUC ALPHA-L-FUCOPYRANOSE
HETNAM CL CHLORIDE ION
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM CA CALCIUM ION
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE
HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE
HETSYN FUC ALPHA-L-FUCOSE; 6-DEOXY-ALPHA-L-GALACTOPYRANOSE; L-
HETSYN 2 FUC FUCOSE; FUCOSE
HETSYN HEM HEME
FORMUL 3 CSO 2(C3 H7 N O3 S)
FORMUL 5 NAG 8(C8 H15 N O6)
FORMUL 5 BMA 4(C6 H12 O6)
FORMUL 5 MAN 2(C6 H12 O6)
FORMUL 5 FUC 2(C6 H12 O5)
FORMUL 7 CL 5(CL 1-)
FORMUL 8 HEM 2(C34 H32 FE N4 O4)
FORMUL 11 CA 2(CA 2+)
FORMUL 22 HOH *926(H2 O)
HELIX 1 1 LEU A 60 VAL A 69 1 10
HELIX 2 2 PRO A 72 LEU A 76 5 5
HELIX 3 3 LEU A 84 ASP A 98 1 15
HELIX 4 4 LEU B 60 VAL B 69 1 10
HELIX 5 5 PRO B 72 LEU B 76 5 5
HELIX 6 6 LEU B 84 ASP B 98 1 15
HELIX 7 7 ALA C 173 GLY C 178 1 6
HELIX 8 8 GLU C 180 LEU C 187 1 8
HELIX 9 9 ASP C 219 THR C 224 1 6
HELIX 10 10 MET C 243 ASN C 268 1 26
HELIX 11 11 ASP C 272 ASP C 295 1 24
HELIX 12 12 TYR C 296 GLY C 302 1 7
HELIX 13 13 GLY C 302 LEU C 310 1 9
HELIX 14 14 VAL C 327 PHE C 332 1 6
HELIX 15 15 ARG C 333 ILE C 339 5 7
HELIX 16 16 SER C 362 VAL C 364 5 3
HELIX 17 17 ALA C 367 GLU C 374 1 8
HELIX 18 18 ILE C 377 ALA C 386 1 10
HELIX 19 19 VAL C 399 GLU C 404 1 6
HELIX 20 20 ASP C 416 HIS C 428 1 13
HELIX 21 21 GLY C 432 CYS C 440 1 9
HELIX 22 22 THR C 447 ARG C 456 1 10
HELIX 23 23 ASN C 457 GLY C 469 1 13
HELIX 24 24 THR C 470 ILE C 474 5 5
HELIX 25 25 ASP C 475 GLU C 483 1 9
HELIX 26 26 GLY C 492 GLY C 509 1 18
HELIX 27 27 SER C 521 ALA C 529 1 9
HELIX 28 28 SER C 532 THR C 541 1 10
HELIX 29 29 SER C 565 LEU C 567 5 3
HELIX 30 30 LEU C 572 ARG C 576 5 5
HELIX 31 31 ALA D 173 GLY D 178 1 6
HELIX 32 32 GLU D 180 LEU D 187 1 8
HELIX 33 33 ASP D 219 ASN D 225 1 7
HELIX 34 34 MET D 243 ASN D 268 1 26
HELIX 35 35 ASP D 272 ASP D 295 1 24
HELIX 36 36 TYR D 296 GLY D 302 1 7
HELIX 37 37 GLY D 302 LEU D 310 1 9
HELIX 38 38 ALA D 325 PHE D 332 1 8
HELIX 39 39 ARG D 333 ILE D 339 5 7
HELIX 40 40 SER D 362 VAL D 364 5 3
HELIX 41 41 ALA D 367 GLU D 374 1 8
HELIX 42 42 ILE D 377 ALA D 386 1 10
HELIX 43 43 VAL D 399 GLU D 404 1 6
HELIX 44 44 ASP D 416 HIS D 428 1 13
HELIX 45 45 GLY D 432 CYS D 440 1 9
HELIX 46 46 THR D 447 ARG D 456 1 10
HELIX 47 47 ASN D 457 GLY D 469 1 13
HELIX 48 48 THR D 470 ILE D 474 5 5
HELIX 49 49 ASP D 475 GLU D 483 1 9
HELIX 50 50 GLY D 492 GLY D 509 1 18
HELIX 51 51 SER D 521 ALA D 529 1 9
HELIX 52 52 SER D 532 THR D 541 1 10
HELIX 53 53 SER D 565 LEU D 567 5 3
HELIX 54 54 LEU D 572 ARG D 576 5 5
SHEET 1 AA 2 ARG A 27 ALA A 28 0
SHEET 2 AA 2 ILE C 164 ASN C 165 -1 N ASN C 165 O ARG A 27
SHEET 1 AB 2 PRO A 78 SER A 83 0
SHEET 2 AB 2 PRO C 388 LYS C 390 -1 O ALA C 389 N ASP A 79
SHEET 1 BA 2 ARG B 27 ALA B 28 0
SHEET 2 BA 2 ILE D 164 ASN D 165 -1 N ASN D 165 O ARG B 27
SHEET 1 BB 2 PRO B 78 SER B 83 0
SHEET 2 BB 2 PRO D 388 LYS D 390 -1 O ALA D 389 N ASP B 79
SHEET 1 CA 2 PHE C 342 PHE C 344 0
SHEET 2 CA 2 ARG C 358 PRO C 360 -1 O VAL C 359 N MET C 343
SHEET 1 CB 2 THR C 545 SER C 547 0
SHEET 2 CB 2 PHE C 561 ASN C 563 -1 O VAL C 562 N VAL C 546
SHEET 1 DA 2 PHE D 342 PHE D 344 0
SHEET 2 DA 2 ARG D 358 PRO D 360 -1 O VAL D 359 N MET D 343
SHEET 1 DB 2 THR D 545 SER D 547 0
SHEET 2 DB 2 PHE D 561 ASN D 563 -1 O VAL D 562 N VAL D 546
SSBOND 1 CYS A 1 CYS A 14 1555 1555 2.16
SSBOND 2 CYS B 1 CYS B 14 1555 1555 2.20
SSBOND 3 CYS C 115 CYS C 125 1555 1555 2.08
SSBOND 4 CYS C 119 CYS C 143 1555 1555 2.18
SSBOND 5 CYS C 153 CYS D 153 1555 1555 2.09
SSBOND 6 CYS C 221 CYS C 232 1555 1555 2.11
SSBOND 7 CYS C 440 CYS C 497 1555 1555 2.37
SSBOND 8 CYS C 538 CYS C 564 1555 1555 2.08
SSBOND 9 CYS D 115 CYS D 125 1555 1555 2.08
SSBOND 10 CYS D 119 CYS D 143 1555 1555 2.12
SSBOND 11 CYS D 221 CYS D 232 1555 1555 2.10
SSBOND 12 CYS D 440 CYS D 497 1555 1555 2.82
SSBOND 13 CYS D 538 CYS D 564 1555 1555 2.06
LINK OD2 ASP A 94 CMD HEM A 605 1555 1555 1.44
LINK CMB HEM A 605 OE2 GLU C 242 1555 1555 1.42
LINK CBB HEM A 605 SD MET C 243 1555 1555 1.71
LINK OD2 ASP B 94 CMD HEM B 605 1555 1555 1.42
LINK CMB HEM B 605 OE2 GLU D 242 1555 1555 1.38
LINK CBB HEM B 605 SD MET D 243 1555 1555 1.68
LINK C SER C 149 N CSO C 150 1555 1555 1.33
LINK C CSO C 150 N PRO C 151 1555 1555 1.33
LINK ND2 ASN C 189 C1 NAG C 620 1555 1555 1.43
LINK ND2 ASN C 225 C1 NAG C 630 1555 1555 1.44
LINK ND2 ASN C 317 C1 NAG E 1 1555 1555 1.45
LINK C SER D 149 N CSO D 150 1555 1555 1.33
LINK C CSO D 150 N PRO D 151 1555 1555 1.33
LINK ND2 ASN D 189 C1 NAG D 620 1555 1555 1.43
LINK ND2 ASN D 225 C1 NAG D 630 1555 1555 1.45
LINK ND2 ASN D 317 C1 NAG F 1 1555 1555 1.44
LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.54
LINK O6 NAG E 1 C1 FUC E 5 1555 1555 1.63
LINK O4 NAG E 2 C1 BMA E 3 1555 1555 1.48
LINK O3 BMA E 3 C1 MAN E 4 1555 1555 1.73
LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.52
LINK O6 NAG F 1 C1 FUC F 5 1555 1555 1.66
LINK O4 NAG F 2 C1 BMA F 3 1555 1555 1.51
LINK O3 BMA F 3 C1 MAN F 4 1555 1555 1.74
LINK O ASP A 96 CA CA C 601 1555 1555 2.29
LINK OD1 ASP A 96 CA CA C 601 1555 1555 2.38
LINK FE HEM A 605 NE2 HIS C 336 1555 1555 2.08
LINK OD1 ASP B 96 CA CA D 701 1555 1555 2.38
LINK O ASP B 96 CA CA D 701 1555 1555 2.27
LINK FE HEM B 605 NE2 HIS D 336 1555 1555 2.07
LINK OG1 THR C 168 CA CA C 601 1555 1555 2.34
LINK O THR C 168 CA CA C 601 1555 1555 2.35
LINK O PHE C 170 CA CA C 601 1555 1555 2.34
LINK OD1 ASP C 172 CA CA C 601 1555 1555 2.36
LINK OG SER C 174 CA CA C 601 1555 1555 2.34
LINK OG1 THR D 168 CA CA D 701 1555 1555 2.36
LINK O THR D 168 CA CA D 701 1555 1555 2.38
LINK O PHE D 170 CA CA D 701 1555 1555 2.36
LINK OD1 ASP D 172 CA CA D 701 1555 1555 2.36
LINK OG SER D 174 CA CA D 701 1555 1555 2.35
CISPEP 1 PRO C 123 PRO C 124 0 10.13
CISPEP 2 GLU C 354 PRO C 355 0 6.07
CISPEP 3 ASN C 549 ASN C 550 0 3.10
CISPEP 4 TYR C 557 PRO C 558 0 5.17
CISPEP 5 PRO D 123 PRO D 124 0 12.69
CISPEP 6 GLU D 354 PRO D 355 0 3.16
CISPEP 7 ASN D 549 ASN D 550 0 4.15
CISPEP 8 TYR D 557 PRO D 558 0 3.66
CRYST1 105.160 105.160 225.520 90.00 90.00 90.00 P 43 21 2 16
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 0.009509 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009509 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004434 0.00000
MTRIX1 1 0.000000 0.000000 0.000000 0.00000 1
MTRIX2 1 0.000000 0.000000 0.000000 0.00000 1
MTRIX3 1 0.000000 0.000000 0.000000 0.00000 1
MTRIX1 2 0.000000 0.000000 0.000000 0.00000 1
MTRIX2 2 0.000000 0.000000 0.000000 0.00000 1
MTRIX3 2 0.000000 0.000000 0.000000 0.00000 1
(ATOM LINES ARE NOT SHOWN.)
END
