HEADER METAL TRANSPORT 22-OCT-15 5EE4
TITLE THE CRYSTAL STRUCTURE OF HPUA FROM KINGELLA DENITRIFICANS IN COMPLEX
TITLE 2 WITH HUMAN HAEMOGLOBIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HPUA;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: HEMOGLOBIN SUBUNIT ALPHA;
COMPND 7 CHAIN: C, E;
COMPND 8 SYNONYM: ALPHA-GLOBIN,HEMOGLOBIN ALPHA CHAIN;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: HEMOGLOBIN SUBUNIT BETA;
COMPND 11 CHAIN: D, F;
COMPND 12 SYNONYM: BETA-GLOBIN,HEMOGLOBIN BETA CHAIN
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: KINGELLA DENITRIFICANS ATCC 33394;
SOURCE 3 ORGANISM_TAXID: 888741;
SOURCE 4 ATCC: 33394;
SOURCE 5 GENE: HMPREF9098_0447;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 TISSUE: BLOOD;
SOURCE 13 MOL_ID: 3;
SOURCE 14 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 15 ORGANISM_COMMON: HUMAN;
SOURCE 16 ORGANISM_TAXID: 9606;
SOURCE 17 TISSUE: BLOOD
KEYWDS OUTER MEMBRANE, RECEPTOR, BETA BARREL, METAL TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR C.T.WONG,S.A.HARE
REVDAT 4 10-JAN-24 5EE4 1 LINK
REVDAT 3 13-SEP-17 5EE4 1 REMARK
REVDAT 2 30-DEC-15 5EE4 1 JRNL
REVDAT 1 04-NOV-15 5EE4 0
JRNL AUTH C.T.WONG,Y.XU,A.GUPTA,J.A.GARNETT,S.J.MATTHEWS,S.A.HARE
JRNL TITL STRUCTURAL ANALYSIS OF HAEMOGLOBIN BINDING BY HPUA FROM THE
JRNL TITL 2 NEISSERIACEAE FAMILY.
JRNL REF NAT COMMUN V. 6 10172 2015
JRNL REFN ESSN 2041-1723
JRNL PMID 26671256
JRNL DOI 10.1038/NCOMMS10172
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0069
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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 123.07
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.7
REMARK 3 NUMBER OF REFLECTIONS : 47357
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) : 0.204
REMARK 3 R VALUE (WORKING SET) : 0.202
REMARK 3 FREE R VALUE : 0.244
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2491
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) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3501
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.66
REMARK 3 BIN R VALUE (WORKING SET) : 0.2860
REMARK 3 BIN FREE R VALUE SET COUNT : 168
REMARK 3 BIN FREE R VALUE : 0.2980
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8742
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 192
REMARK 3 SOLVENT ATOMS : 374
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.17
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.65000
REMARK 3 B22 (A**2) : 0.11000
REMARK 3 B33 (A**2) : -2.62000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.13000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.458
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.256
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.216
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.388
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.936
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.911
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9158 ; 0.013 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 8548 ; 0.005 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12490 ; 1.504 ; 1.978
REMARK 3 BOND ANGLES OTHERS (DEGREES): 19673 ; 1.040 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1393 ; 0.093 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 10476 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 2115 ; 0.005 ; 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): 4648 ; 2.316 ; 3.188
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 4647 ; 2.316 ; 3.188
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5796 ; 3.584 ; 4.773
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 3
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 15 320 B 15 320 15622 0.130 0.050
REMARK 3 2 C 1 141 E 1 141 7599 0.120 0.050
REMARK 3 3 D 6 145 F 6 145 7403 0.120 0.050
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 5EE4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-OCT-15.
REMARK 100 THE DEPOSITION ID IS D_1000214762.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-OCT-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.92
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.21
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 49897
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 123.071
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 200 DATA REDUNDANCY : 6.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.17500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.42
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.8
REMARK 200 DATA REDUNDANCY IN SHELL : 6.30
REMARK 200 R MERGE FOR SHELL (I) : 0.81800
REMARK 200 R SYM FOR SHELL (I) : 0.81800
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.5.6
REMARK 200 STARTING MODEL: 5EC6, 1HHO
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 35.89
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.92
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM HEPES, 18 % PEG 4,000, 10 %
REMARK 280 ISOPROPANOL, PH 7.8, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 43.60500
REMARK 290 SMTRY3 2 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7380 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24590 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -59.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, D
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6730 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24660 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -61.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, E, 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 GLY A 1
REMARK 465 PRO A 2
REMARK 465 GLY A 3
REMARK 465 GLY A 4
REMARK 465 THR A 5
REMARK 465 ALA A 6
REMARK 465 ILE A 7
REMARK 465 ASN A 8
REMARK 465 GLU A 9
REMARK 465 PRO A 10
REMARK 465 LEU A 11
REMARK 465 THR A 12
REMARK 465 ALA A 13
REMARK 465 ALA A 14
REMARK 465 ARG A 197
REMARK 465 TYR A 198
REMARK 465 SER A 199
REMARK 465 PRO A 200
REMARK 465 TYR A 201
REMARK 465 ASN A 202
REMARK 465 THR A 203
REMARK 465 GLY A 204
REMARK 465 GLN A 205
REMARK 465 SER A 321
REMARK 465 PRO A 322
REMARK 465 GLY B 1
REMARK 465 PRO B 2
REMARK 465 GLY B 3
REMARK 465 GLY B 4
REMARK 465 THR B 5
REMARK 465 ALA B 6
REMARK 465 ILE B 7
REMARK 465 ASN B 8
REMARK 465 GLU B 9
REMARK 465 PRO B 10
REMARK 465 LEU B 11
REMARK 465 THR B 12
REMARK 465 ALA B 13
REMARK 465 ALA B 14
REMARK 465 TYR B 198
REMARK 465 SER B 199
REMARK 465 PRO B 200
REMARK 465 TYR B 201
REMARK 465 ASN B 202
REMARK 465 THR B 203
REMARK 465 GLY B 204
REMARK 465 GLN B 205
REMARK 465 SER B 321
REMARK 465 PRO B 322
REMARK 465 VAL F 1
REMARK 465 HIS F 2
REMARK 465 LEU F 3
REMARK 465 THR F 4
REMARK 465 PRO F 5
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 OE1 GLN B 123 O HOH B 401 1.91
REMARK 500 O HOH B 455 O HOH B 468 2.00
REMARK 500 N SER B 292 O HOH B 402 2.08
REMARK 500 O HOH A 567 O HOH A 600 2.09
REMARK 500 OD2 ASP E 47 O HOH E 301 2.13
REMARK 500 O HOH B 401 O HOH B 466 2.16
REMARK 500 O HOH F 327 O HOH F 332 2.17
REMARK 500 OE1 GLN A 74 O HOH A 501 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 OG SER A 292 OE2 GLU B 38 1554 2.19
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 37 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG B 37 NE - CZ - NH2 ANGL. DEV. = -3.2 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 GLN A 45 55.26 -144.31
REMARK 500 ILE A 90 120.29 -38.38
REMARK 500 ARG A 132 66.92 -104.21
REMARK 500 ASN A 186 42.71 70.79
REMARK 500 ARG A 238 -76.14 -97.14
REMARK 500 ALA A 266 130.97 88.08
REMARK 500 SER A 292 114.63 -35.82
REMARK 500 ASN A 293 14.10 54.24
REMARK 500 ASN A 308 105.33 -160.98
REMARK 500 GLN B 45 53.67 -144.25
REMARK 500 ILE B 90 123.26 -37.84
REMARK 500 THR B 96 -167.19 -114.74
REMARK 500 ARG B 132 57.04 -101.16
REMARK 500 ARG B 238 -77.36 -98.20
REMARK 500 ALA B 266 129.88 84.97
REMARK 500 SER B 292 118.00 -38.66
REMARK 500 ASN B 293 10.47 58.08
REMARK 500 SER B 313 150.62 -45.67
REMARK 500 ASN D 80 57.17 -148.77
REMARK 500 SER F 44 -8.33 -57.68
REMARK 500 ASN F 80 70.87 -155.31
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 THR A 126 GLY A 127 147.48
REMARK 500 GLY C 51 SER C 52 -146.12
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM C 201 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 87 NE2
REMARK 620 2 HEM C 201 NA 88.8
REMARK 620 3 HEM C 201 NB 85.6 90.8
REMARK 620 4 HEM C 201 NC 95.8 175.3 90.9
REMARK 620 5 HEM C 201 ND 99.0 89.6 175.4 88.3
REMARK 620 6 OXY C 202 O1 179.1 90.9 93.5 84.5 81.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM D 201 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 92 NE2
REMARK 620 2 HEM D 201 NA 88.0
REMARK 620 3 HEM D 201 NB 91.3 88.3
REMARK 620 4 HEM D 201 NC 91.0 178.4 90.4
REMARK 620 5 HEM D 201 ND 86.8 92.1 178.1 89.2
REMARK 620 6 OXY D 202 O1 168.0 97.1 99.6 84.1 82.2
REMARK 620 7 OXY D 202 O2 162.7 107.3 81.2 73.5 100.4 21.3
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM E 201 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS E 87 NE2
REMARK 620 2 HEM E 201 NA 85.1
REMARK 620 3 HEM E 201 NB 84.5 90.6
REMARK 620 4 HEM E 201 NC 99.8 175.0 90.3
REMARK 620 5 HEM E 201 ND 100.2 89.7 175.3 89.1
REMARK 620 6 OXY E 202 O1 171.8 86.8 94.1 88.2 81.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM F 201 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS F 92 NE2
REMARK 620 2 HEM F 201 NA 86.5
REMARK 620 3 HEM F 201 NB 87.1 87.5
REMARK 620 4 HEM F 201 NC 91.0 176.8 90.3
REMARK 620 5 HEM F 201 ND 90.8 92.9 177.8 89.1
REMARK 620 6 OXY F 202 O2 177.7 91.3 93.3 91.2 88.9
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 GOL A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM C 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OXY C 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM D 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OXY D 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM E 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OXY E 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM F 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OXY F 202
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5EC6 RELATED DB: PDB
REMARK 900 5EC6 CONTAINS APO HPUA FROM KINGELLA DENITRIFICANS
REMARK 900 RELATED ID: 5EE2 RELATED DB: PDB
REMARK 900 5EE2 CONTAINS THE C-TERMINAL BETA BARREL OF HPUA FROM NEISSERIA
REMARK 900 GONORRHOEAE
DBREF 5EE4 A 3 322 UNP F0EX68 F0EX68_9NEIS 21 340
DBREF 5EE4 B 3 322 UNP F0EX68 F0EX68_9NEIS 21 340
DBREF 5EE4 C 1 141 UNP P69905 HBA_HUMAN 2 142
DBREF 5EE4 D 1 146 UNP P68871 HBB_HUMAN 2 147
DBREF 5EE4 E 1 141 UNP P69905 HBA_HUMAN 2 142
DBREF 5EE4 F 1 146 UNP P68871 HBB_HUMAN 2 147
SEQADV 5EE4 GLY A 1 UNP F0EX68 EXPRESSION TAG
SEQADV 5EE4 PRO A 2 UNP F0EX68 EXPRESSION TAG
SEQADV 5EE4 THR A 5 UNP F0EX68 SER 23 CLONING ARTIFACT
SEQADV 5EE4 GLY B 1 UNP F0EX68 EXPRESSION TAG
SEQADV 5EE4 PRO B 2 UNP F0EX68 EXPRESSION TAG
SEQADV 5EE4 THR B 5 UNP F0EX68 SER 23 CLONING ARTIFACT
SEQRES 1 A 322 GLY PRO GLY GLY THR ALA ILE ASN GLU PRO LEU THR ALA
SEQRES 2 A 322 ALA PRO ILE PRO VAL LEU ARG ALA VAL ASP THR THR SER
SEQRES 3 A 322 PRO ASN ILE VAL ALA ASP THR SER THR ASP ARG GLU GLN
SEQRES 4 A 322 ARG THR PHE ALA THR GLN GLY GLY SER VAL LYS PRO PHE
SEQRES 5 A 322 THR ILE THR LYS PRO SER PRO TYR ILE PRO GLY LEU MET
SEQRES 6 A 322 LEU THR ASN GLN GLU ILE LEU TYR GLN ALA PRO ASP GLY
SEQRES 7 A 322 LYS TYR TYR ASP PHE GLY THR TYR ASN THR LEU ILE MET
SEQRES 8 A 322 PRO SER SER SER THR SER ALA ARG VAL LEU PRO ASN SER
SEQRES 9 A 322 HIS PRO MET GLN PRO LEU ASP SER GLY GLY LYS MET ILE
SEQRES 10 A 322 ALA CYS CYS THR ASN GLN THR SER THR GLY MET ASN ALA
SEQRES 11 A 322 LEU ARG LEU LYS SER MET GLN PHE GLY ALA TRP MET SER
SEQRES 12 A 322 PRO SER LYS THR VAL SER LEU PHE ALA GLY GLY THR PRO
SEQRES 13 A 322 ALA PRO THR ASP THR LEU GLN GLY VAL ASP THR ALA GLY
SEQRES 14 A 322 ARG PRO THR GLY LYS ALA THR TYR GLU VAL ILE GLY LEU
SEQRES 15 A 322 ARG VAL LYS ASN ASP ARG ALA VAL THR SER SER TYR GLU
SEQRES 16 A 322 THR ARG TYR SER PRO TYR ASN THR GLY GLN VAL VAL THR
SEQRES 17 A 322 GLY SER PHE LEU THR VAL ASN PHE ASN THR GLY LYS LEU
SEQRES 18 A 322 GLY GLY THR ILE VAL GLY ASN SER GLU PHE GLY ASP SER
SEQRES 19 A 322 ILE GLU MET ARG ASP VAL ASN VAL ASN GLY ASN GLN PHE
SEQRES 20 A 322 SER GLY THR ALA SER SER GLY GLY HIS THR GLY GLN VAL
SEQRES 21 A 322 SER GLY GLY LEU PHE ALA LYS GLU GLU ARG PHE TYR SER
SEQRES 22 A 322 GLY THR LEU GLU HIS PRO SER GLY GLY GLU ILE GLY GLY
SEQRES 23 A 322 THR VAL ASN PHE GLY SER ASN SER PRO LEU ASN ALA SER
SEQRES 24 A 322 PHE GLY GLY THR ARG ARG GLU TYR ASN ALA ALA ASP THR
SEQRES 25 A 322 SER THR ASP THR SER HIS LEU VAL SER PRO
SEQRES 1 B 322 GLY PRO GLY GLY THR ALA ILE ASN GLU PRO LEU THR ALA
SEQRES 2 B 322 ALA PRO ILE PRO VAL LEU ARG ALA VAL ASP THR THR SER
SEQRES 3 B 322 PRO ASN ILE VAL ALA ASP THR SER THR ASP ARG GLU GLN
SEQRES 4 B 322 ARG THR PHE ALA THR GLN GLY GLY SER VAL LYS PRO PHE
SEQRES 5 B 322 THR ILE THR LYS PRO SER PRO TYR ILE PRO GLY LEU MET
SEQRES 6 B 322 LEU THR ASN GLN GLU ILE LEU TYR GLN ALA PRO ASP GLY
SEQRES 7 B 322 LYS TYR TYR ASP PHE GLY THR TYR ASN THR LEU ILE MET
SEQRES 8 B 322 PRO SER SER SER THR SER ALA ARG VAL LEU PRO ASN SER
SEQRES 9 B 322 HIS PRO MET GLN PRO LEU ASP SER GLY GLY LYS MET ILE
SEQRES 10 B 322 ALA CYS CYS THR ASN GLN THR SER THR GLY MET ASN ALA
SEQRES 11 B 322 LEU ARG LEU LYS SER MET GLN PHE GLY ALA TRP MET SER
SEQRES 12 B 322 PRO SER LYS THR VAL SER LEU PHE ALA GLY GLY THR PRO
SEQRES 13 B 322 ALA PRO THR ASP THR LEU GLN GLY VAL ASP THR ALA GLY
SEQRES 14 B 322 ARG PRO THR GLY LYS ALA THR TYR GLU VAL ILE GLY LEU
SEQRES 15 B 322 ARG VAL LYS ASN ASP ARG ALA VAL THR SER SER TYR GLU
SEQRES 16 B 322 THR ARG TYR SER PRO TYR ASN THR GLY GLN VAL VAL THR
SEQRES 17 B 322 GLY SER PHE LEU THR VAL ASN PHE ASN THR GLY LYS LEU
SEQRES 18 B 322 GLY GLY THR ILE VAL GLY ASN SER GLU PHE GLY ASP SER
SEQRES 19 B 322 ILE GLU MET ARG ASP VAL ASN VAL ASN GLY ASN GLN PHE
SEQRES 20 B 322 SER GLY THR ALA SER SER GLY GLY HIS THR GLY GLN VAL
SEQRES 21 B 322 SER GLY GLY LEU PHE ALA LYS GLU GLU ARG PHE TYR SER
SEQRES 22 B 322 GLY THR LEU GLU HIS PRO SER GLY GLY GLU ILE GLY GLY
SEQRES 23 B 322 THR VAL ASN PHE GLY SER ASN SER PRO LEU ASN ALA SER
SEQRES 24 B 322 PHE GLY GLY THR ARG ARG GLU TYR ASN ALA ALA ASP THR
SEQRES 25 B 322 SER THR ASP THR SER HIS LEU VAL SER PRO
SEQRES 1 C 141 VAL LEU SER PRO ALA ASP LYS THR ASN VAL LYS ALA ALA
SEQRES 2 C 141 TRP GLY LYS VAL GLY ALA HIS ALA GLY GLU TYR GLY ALA
SEQRES 3 C 141 GLU ALA LEU GLU ARG MET PHE LEU SER PHE PRO THR THR
SEQRES 4 C 141 LYS THR TYR PHE PRO HIS PHE ASP LEU SER HIS GLY SER
SEQRES 5 C 141 ALA GLN VAL LYS GLY HIS GLY LYS LYS VAL ALA ASP ALA
SEQRES 6 C 141 LEU THR ASN ALA VAL ALA HIS VAL ASP ASP MET PRO ASN
SEQRES 7 C 141 ALA LEU SER ALA LEU SER ASP LEU HIS ALA HIS LYS LEU
SEQRES 8 C 141 ARG VAL ASP PRO VAL ASN PHE LYS LEU LEU SER HIS CYS
SEQRES 9 C 141 LEU LEU VAL THR LEU ALA ALA HIS LEU PRO ALA GLU PHE
SEQRES 10 C 141 THR PRO ALA VAL HIS ALA SER LEU ASP LYS PHE LEU ALA
SEQRES 11 C 141 SER VAL SER THR VAL LEU THR SER LYS TYR ARG
SEQRES 1 D 146 VAL HIS LEU THR PRO GLU GLU LYS SER ALA VAL THR ALA
SEQRES 2 D 146 LEU TRP GLY LYS VAL ASN VAL ASP GLU VAL GLY GLY GLU
SEQRES 3 D 146 ALA LEU GLY ARG LEU LEU VAL VAL TYR PRO TRP THR GLN
SEQRES 4 D 146 ARG PHE PHE GLU SER PHE GLY ASP LEU SER THR PRO ASP
SEQRES 5 D 146 ALA VAL MET GLY ASN PRO LYS VAL LYS ALA HIS GLY LYS
SEQRES 6 D 146 LYS VAL LEU GLY ALA PHE SER ASP GLY LEU ALA HIS LEU
SEQRES 7 D 146 ASP ASN LEU LYS GLY THR PHE ALA THR LEU SER GLU LEU
SEQRES 8 D 146 HIS CYS ASP LYS LEU HIS VAL ASP PRO GLU ASN PHE ARG
SEQRES 9 D 146 LEU LEU GLY ASN VAL LEU VAL CYS VAL LEU ALA HIS HIS
SEQRES 10 D 146 PHE GLY LYS GLU PHE THR PRO PRO VAL GLN ALA ALA TYR
SEQRES 11 D 146 GLN LYS VAL VAL ALA GLY VAL ALA ASN ALA LEU ALA HIS
SEQRES 12 D 146 LYS TYR HIS
SEQRES 1 E 141 VAL LEU SER PRO ALA ASP LYS THR ASN VAL LYS ALA ALA
SEQRES 2 E 141 TRP GLY LYS VAL GLY ALA HIS ALA GLY GLU TYR GLY ALA
SEQRES 3 E 141 GLU ALA LEU GLU ARG MET PHE LEU SER PHE PRO THR THR
SEQRES 4 E 141 LYS THR TYR PHE PRO HIS PHE ASP LEU SER HIS GLY SER
SEQRES 5 E 141 ALA GLN VAL LYS GLY HIS GLY LYS LYS VAL ALA ASP ALA
SEQRES 6 E 141 LEU THR ASN ALA VAL ALA HIS VAL ASP ASP MET PRO ASN
SEQRES 7 E 141 ALA LEU SER ALA LEU SER ASP LEU HIS ALA HIS LYS LEU
SEQRES 8 E 141 ARG VAL ASP PRO VAL ASN PHE LYS LEU LEU SER HIS CYS
SEQRES 9 E 141 LEU LEU VAL THR LEU ALA ALA HIS LEU PRO ALA GLU PHE
SEQRES 10 E 141 THR PRO ALA VAL HIS ALA SER LEU ASP LYS PHE LEU ALA
SEQRES 11 E 141 SER VAL SER THR VAL LEU THR SER LYS TYR ARG
SEQRES 1 F 146 VAL HIS LEU THR PRO GLU GLU LYS SER ALA VAL THR ALA
SEQRES 2 F 146 LEU TRP GLY LYS VAL ASN VAL ASP GLU VAL GLY GLY GLU
SEQRES 3 F 146 ALA LEU GLY ARG LEU LEU VAL VAL TYR PRO TRP THR GLN
SEQRES 4 F 146 ARG PHE PHE GLU SER PHE GLY ASP LEU SER THR PRO ASP
SEQRES 5 F 146 ALA VAL MET GLY ASN PRO LYS VAL LYS ALA HIS GLY LYS
SEQRES 6 F 146 LYS VAL LEU GLY ALA PHE SER ASP GLY LEU ALA HIS LEU
SEQRES 7 F 146 ASP ASN LEU LYS GLY THR PHE ALA THR LEU SER GLU LEU
SEQRES 8 F 146 HIS CYS ASP LYS LEU HIS VAL ASP PRO GLU ASN PHE ARG
SEQRES 9 F 146 LEU LEU GLY ASN VAL LEU VAL CYS VAL LEU ALA HIS HIS
SEQRES 10 F 146 PHE GLY LYS GLU PHE THR PRO PRO VAL GLN ALA ALA TYR
SEQRES 11 F 146 GLN LYS VAL VAL ALA GLY VAL ALA ASN ALA LEU ALA HIS
SEQRES 12 F 146 LYS TYR HIS
HET GOL A 401 6
HET HEM C 201 43
HET OXY C 202 2
HET HEM D 201 43
HET OXY D 202 2
HET GOL D 203 6
HET HEM E 201 43
HET OXY E 202 2
HET HEM F 201 43
HET OXY F 202 2
HETNAM GOL GLYCEROL
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM OXY OXYGEN MOLECULE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN HEM HEME
FORMUL 7 GOL 2(C3 H8 O3)
FORMUL 8 HEM 4(C34 H32 FE N4 O4)
FORMUL 9 OXY 4(O2)
FORMUL 17 HOH *374(H2 O)
HELIX 1 AA1 SER A 34 GLU A 38 5 5
HELIX 2 AA2 MET A 128 ARG A 132 5 5
HELIX 3 AA3 PRO A 158 LEU A 162 5 5
HELIX 4 AA4 GLY A 164 GLY A 169 1 6
HELIX 5 AA5 SER B 34 GLU B 38 5 5
HELIX 6 AA6 MET B 128 ARG B 132 5 5
HELIX 7 AA7 PRO B 158 LEU B 162 5 5
HELIX 8 AA8 GLY B 164 GLY B 169 1 6
HELIX 9 AA9 SER C 3 GLY C 18 1 16
HELIX 10 AB1 HIS C 20 PHE C 36 1 17
HELIX 11 AB2 PRO C 37 PHE C 43 5 7
HELIX 12 AB3 SER C 52 HIS C 72 1 21
HELIX 13 AB4 ASP C 75 LEU C 80 1 6
HELIX 14 AB5 LEU C 80 HIS C 89 1 10
HELIX 15 AB6 ASP C 94 LEU C 113 1 20
HELIX 16 AB7 THR C 118 THR C 137 1 20
HELIX 17 AB8 THR D 4 VAL D 18 1 15
HELIX 18 AB9 GLU D 22 TYR D 35 1 14
HELIX 19 AC1 PRO D 36 GLY D 46 5 11
HELIX 20 AC2 THR D 50 GLY D 56 1 7
HELIX 21 AC3 ASN D 57 ALA D 76 1 20
HELIX 22 AC4 HIS D 77 ASP D 79 5 3
HELIX 23 AC5 ASN D 80 PHE D 85 1 6
HELIX 24 AC6 PHE D 85 LYS D 95 1 11
HELIX 25 AC7 PRO D 100 GLY D 119 1 20
HELIX 26 AC8 LYS D 120 PHE D 122 5 3
HELIX 27 AC9 THR D 123 ALA D 142 1 20
HELIX 28 AD1 HIS D 143 HIS D 146 5 4
HELIX 29 AD2 SER E 3 GLY E 18 1 16
HELIX 30 AD3 HIS E 20 PHE E 36 1 17
HELIX 31 AD4 PRO E 37 PHE E 43 5 7
HELIX 32 AD5 SER E 52 HIS E 72 1 21
HELIX 33 AD6 ASP E 75 LEU E 80 1 6
HELIX 34 AD7 LEU E 80 HIS E 89 1 10
HELIX 35 AD8 ASP E 94 LEU E 113 1 20
HELIX 36 AD9 THR E 118 THR E 137 1 20
HELIX 37 AE1 GLU F 7 VAL F 18 1 12
HELIX 38 AE2 GLU F 22 TYR F 35 1 14
HELIX 39 AE3 PRO F 36 GLY F 46 5 11
HELIX 40 AE4 THR F 50 GLY F 56 1 7
HELIX 41 AE5 ASN F 57 ALA F 76 1 20
HELIX 42 AE6 ASN F 80 PHE F 85 1 6
HELIX 43 AE7 PHE F 85 LYS F 95 1 11
HELIX 44 AE8 PRO F 100 GLY F 119 1 20
HELIX 45 AE9 LYS F 120 PHE F 122 5 3
HELIX 46 AF1 THR F 123 ALA F 142 1 20
HELIX 47 AF2 HIS F 143 HIS F 146 5 4
SHEET 1 AA1 4 ILE A 29 ALA A 31 0
SHEET 2 AA1 4 SER A 48 PRO A 57 -1 O THR A 53 N VAL A 30
SHEET 3 AA1 4 MET A 65 GLN A 74 -1 O GLU A 70 N PHE A 52
SHEET 4 AA1 4 TYR A 80 TYR A 81 -1 O TYR A 81 N TYR A 73
SHEET 1 AA2 5 ARG A 40 ALA A 43 0
SHEET 2 AA2 5 VAL A 148 GLY A 154 -1 O ALA A 152 N PHE A 42
SHEET 3 AA2 5 MET A 136 MET A 142 -1 N TRP A 141 O SER A 149
SHEET 4 AA2 5 LYS A 115 ALA A 118 -1 N LYS A 115 O MET A 142
SHEET 5 AA2 5 GLN A 108 PRO A 109 -1 N GLN A 108 O MET A 116
SHEET 1 AA3 2 ARG A 99 VAL A 100 0
SHEET 2 AA3 2 GLU A 195 THR A 196 -1 O THR A 196 N ARG A 99
SHEET 1 AA411 SER A 104 PRO A 106 0
SHEET 2 AA411 ARG A 188 THR A 191 -1 O ALA A 189 N HIS A 105
SHEET 3 AA411 LYS A 174 VAL A 184 -1 N ARG A 183 O VAL A 190
SHEET 4 AA411 ALA A 298 ASN A 308 -1 O GLU A 306 N THR A 176
SHEET 5 AA411 GLU A 283 ASN A 289 -1 N VAL A 288 O ALA A 298
SHEET 6 AA411 HIS A 256 PHE A 265 -1 N PHE A 265 O GLU A 283
SHEET 7 AA411 GLN A 246 SER A 253 -1 N GLY A 249 O VAL A 260
SHEET 8 AA411 ILE A 235 ASN A 243 -1 N ASN A 243 O GLN A 246
SHEET 9 AA411 LYS A 220 ILE A 225 -1 N GLY A 223 O MET A 237
SHEET 10 AA411 SER A 210 ASN A 215 -1 N ASN A 215 O LYS A 220
SHEET 11 AA411 LYS A 174 VAL A 184 -1 N TYR A 177 O LEU A 212
SHEET 1 AA5 2 GLU A 269 ARG A 270 0
SHEET 2 AA5 2 LEU A 276 HIS A 278 -1 O GLU A 277 N GLU A 269
SHEET 1 AA6 4 ILE B 29 ALA B 31 0
SHEET 2 AA6 4 SER B 48 PRO B 57 -1 O THR B 53 N VAL B 30
SHEET 3 AA6 4 MET B 65 GLN B 74 -1 O LEU B 66 N LYS B 56
SHEET 4 AA6 4 TYR B 80 TYR B 81 -1 O TYR B 81 N TYR B 73
SHEET 1 AA7 5 ARG B 40 ALA B 43 0
SHEET 2 AA7 5 VAL B 148 GLY B 154 -1 O ALA B 152 N PHE B 42
SHEET 3 AA7 5 MET B 136 MET B 142 -1 N TRP B 141 O SER B 149
SHEET 4 AA7 5 LYS B 115 ALA B 118 -1 N LYS B 115 O MET B 142
SHEET 5 AA7 5 GLN B 108 PRO B 109 -1 N GLN B 108 O MET B 116
SHEET 1 AA8 2 ARG B 99 VAL B 100 0
SHEET 2 AA8 2 GLU B 195 THR B 196 -1 O THR B 196 N ARG B 99
SHEET 1 AA911 SER B 104 PRO B 106 0
SHEET 2 AA911 ARG B 188 THR B 191 -1 O ALA B 189 N HIS B 105
SHEET 3 AA911 LYS B 174 VAL B 184 -1 N ARG B 183 O VAL B 190
SHEET 4 AA911 ALA B 298 ASN B 308 -1 O GLU B 306 N THR B 176
SHEET 5 AA911 GLU B 283 ASN B 289 -1 N VAL B 288 O ALA B 298
SHEET 6 AA911 HIS B 256 PHE B 265 -1 N PHE B 265 O GLU B 283
SHEET 7 AA911 GLN B 246 SER B 253 -1 N GLY B 249 O VAL B 260
SHEET 8 AA911 ILE B 235 ASN B 243 -1 N GLU B 236 O SER B 252
SHEET 9 AA911 LYS B 220 ILE B 225 -1 N GLY B 223 O MET B 237
SHEET 10 AA911 SER B 210 ASN B 215 -1 N ASN B 215 O LYS B 220
SHEET 11 AA911 LYS B 174 VAL B 184 -1 N TYR B 177 O LEU B 212
SHEET 1 AB1 2 GLU B 269 ARG B 270 0
SHEET 2 AB1 2 LEU B 276 HIS B 278 -1 O GLU B 277 N GLU B 269
LINK NE2 HIS C 87 FE HEM C 201 1555 1555 2.29
LINK FE HEM C 201 O1 OXY C 202 1555 1555 2.08
LINK NE2 HIS D 92 FE HEM D 201 1555 1555 2.15
LINK FE HEM D 201 O1 OXY D 202 1555 1555 1.82
LINK FE HEM D 201 O2 OXY D 202 1555 1555 2.72
LINK NE2 HIS E 87 FE HEM E 201 1555 1555 2.32
LINK FE HEM E 201 O1 OXY E 202 1555 1555 2.07
LINK NE2 HIS F 92 FE HEM F 201 1555 1555 2.24
LINK FE HEM F 201 O2 OXY F 202 1555 1555 1.87
SITE 1 AC1 4 GLU A 269 HIS A 278 GLY A 282 ARG A 304
SITE 1 AC2 13 TYR C 42 PHE C 43 PHE C 46 HIS C 58
SITE 2 AC2 13 LEU C 83 LEU C 86 HIS C 87 LEU C 91
SITE 3 AC2 13 ASN C 97 PHE C 98 OXY C 202 HOH C 306
SITE 4 AC2 13 HOH C 327
SITE 1 AC3 3 HIS C 58 VAL C 62 HEM C 201
SITE 1 AC4 11 PHE D 41 PHE D 42 HIS D 63 LEU D 88
SITE 2 AC4 11 HIS D 92 LEU D 96 ASN D 102 LEU D 106
SITE 3 AC4 11 VAL D 137 LEU D 141 OXY D 202
SITE 1 AC5 3 HIS D 63 VAL D 67 HEM D 201
SITE 1 AC6 6 VAL D 1 LEU D 78 ASP D 79 ASN D 80
SITE 2 AC6 6 LEU D 81 LYS D 82
SITE 1 AC7 14 TYR E 42 PHE E 43 HIS E 58 LYS E 61
SITE 2 AC7 14 LEU E 83 HIS E 87 LEU E 91 ASN E 97
SITE 3 AC7 14 PHE E 98 LEU E 101 LEU E 136 OXY E 202
SITE 4 AC7 14 HOH E 320 HOH E 339
SITE 1 AC8 3 HIS E 58 VAL E 62 HEM E 201
SITE 1 AC9 13 PHE F 41 PHE F 42 HIS F 63 PHE F 71
SITE 2 AC9 13 LEU F 88 LEU F 91 HIS F 92 LEU F 96
SITE 3 AC9 13 ASN F 102 LEU F 106 VAL F 137 LEU F 141
SITE 4 AC9 13 OXY F 202
SITE 1 AD1 3 HIS F 63 VAL F 67 HEM F 201
CRYST1 54.790 87.210 124.320 90.00 98.13 90.00 P 1 21 1 4
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 0.018252 0.000000 0.002607 0.00000
SCALE2 0.000000 0.011467 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008125 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
