HEADER OXYGEN STORAGE/TRANSPORT 13-DEC-04 1Y8K
TITLE HORSE METHEMOGLOBIN LOW SALT, PH 7.0 (88% RELATIVE HUMIDITY)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEMOGLOBIN ALPHA CHAINS;
COMPND 3 CHAIN: A, C;
COMPND 4 SYNONYM: SLOW AND FAST;
COMPND 5 OTHER_DETAILS: PH 7.0 AQUOMET STRUCTURE;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: HEMOGLOBIN BETA CHAIN;
COMPND 8 CHAIN: B, D
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: EQUUS CABALLUS;
SOURCE 3 ORGANISM_COMMON: HORSE;
SOURCE 4 ORGANISM_TAXID: 9796;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: EQUUS CABALLUS;
SOURCE 7 ORGANISM_COMMON: HORSE;
SOURCE 8 ORGANISM_TAXID: 9796
KEYWDS AQUO METHEMOGLOBIN, QUARTERNARY ASSOCIATION, ALLOSTERIC
KEYWDS 2 TRANSITION, PROTEIN HYDRATION, OXYGEN STORAGE/TRANSPORT
KEYWDS 3 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR R.SANKARANARAYANAN,B.K.BISWAL,M.VIJAYAN
REVDAT 2 24-FEB-09 1Y8K 1 VERSN
REVDAT 1 26-JUL-05 1Y8K 0
JRNL AUTH R.SANKARANARAYANAN,B.K.BISWAL,M.VIJAYAN
JRNL TITL A NEW RELAXED STATE IN HORSE METHEMOGLOBIN
JRNL TITL 2 CHARACTERIZED BY CRYSTALLOGRAPHIC STUDIES.
JRNL REF PROTEINS V. 60 547 2005
JRNL REFN ISSN 0887-3585
JRNL PMID 15887226
JRNL DOI 10.1002/PROT.20510
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH B.K.BISWAL,M.VIJAYAN
REMARK 1 TITL STRUCTURE OF HUMAN METHAEMOGLOBIN: THE VARIATION
REMARK 1 TITL 2 OF A THEME
REMARK 1 REF CURR.SCI. V. 81 1100 2001
REMARK 1 REFN ISSN 0011-3891
REMARK 1 REFERENCE 2
REMARK 1 AUTH B.K.BISWAL,M.VIJAYAN
REMARK 1 TITL STRUCTURES OF HUMAN OXY- AND DEOXYHAEMOGLOBIN AT
REMARK 1 TITL 2 DIFFERENT LEVELS OF HUMIDITY: VARIABILITY IN THE T
REMARK 1 TITL 3 STATE
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 58 1155 2002
REMARK 1 REFN ISSN 0907-4449
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 0.4
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 372154.060
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 92.0
REMARK 3 NUMBER OF REFLECTIONS : 23480
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 SET) : 0.183
REMARK 3 FREE R VALUE : 0.228
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1150
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.007
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.44
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 86.30
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3436
REMARK 3 BIN R VALUE (WORKING SET) : 0.2300
REMARK 3 BIN FREE R VALUE : 0.2850
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.70
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 169
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.022
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4406
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 172
REMARK 3 SOLVENT ATOMS : 386
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 31.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.90000
REMARK 3 B22 (A**2) : -0.20000
REMARK 3 B33 (A**2) : 1.10000
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.25
REMARK 3 ESD FROM SIGMAA (A) : 0.19
REMARK 3 LOW RESOLUTION CUTOFF (A) : 20.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.32
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.27
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.20
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 19.70
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.02
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.31
REMARK 3 BSOL : 49.34
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : PARAM19X.HEME
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : TOPH19X.HEME
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1Y8K COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-JAN-05.
REMARK 100 THE RCSB ID CODE IS RCSB031251.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-AUG-02
REMARK 200 TEMPERATURE (KELVIN) : 293.0
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : OSMIC MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24502
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.11200
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) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.52300
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: AMORE
REMARK 200 STARTING MODEL: HORSE METHEMOGLOBIN, PDB ENTRY 2MHB
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.01M PHOSPHATE BUFFER, 30% PEG
REMARK 280 3350, PH 7.0, LIQUID DIFFUSION, TEMPERATURE 293K
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 31.25950
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 55.65750
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.07000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 55.65750
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 31.25950
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 40.07000
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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 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 ASP A 75 49.53 -154.85
REMARK 500 ASN B 80 60.19 -150.33
REMARK 500 LYS B 144 48.08 -70.26
REMARK 500 ASP C 75 58.51 -163.41
REMARK 500 HIS D 77 41.18 -147.01
REMARK 500 TYR D 145 -90.72 -69.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 TYR B 145 0.06 SIDE_CHAIN
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 D 217 DISTANCE = 5.48 ANGSTROMS
REMARK 525 HOH D 228 DISTANCE = 5.61 ANGSTROMS
REMARK 525 HOH A 285 DISTANCE = 8.65 ANGSTROMS
REMARK 525 HOH C 314 DISTANCE = 6.63 ANGSTROMS
REMARK 525 HOH D 238 DISTANCE = 7.01 ANGSTROMS
REMARK 525 HOH A 323 DISTANCE = 5.73 ANGSTROMS
REMARK 525 HOH C 328 DISTANCE = 8.41 ANGSTROMS
REMARK 525 HOH B 404 DISTANCE = 9.53 ANGSTROMS
REMARK 525 HOH B 409 DISTANCE = 5.54 ANGSTROMS
REMARK 525 HOH A 356 DISTANCE = 6.69 ANGSTROMS
REMARK 525 HOH C 360 DISTANCE = 8.79 ANGSTROMS
REMARK 525 HOH A 361 DISTANCE = 6.46 ANGSTROMS
REMARK 525 HOH D 287 DISTANCE = 7.24 ANGSTROMS
REMARK 525 HOH B 428 DISTANCE = 5.76 ANGSTROMS
REMARK 525 HOH D 290 DISTANCE = 7.26 ANGSTROMS
REMARK 525 HOH A 378 DISTANCE = 7.35 ANGSTROMS
REMARK 525 HOH D 310 DISTANCE = 8.54 ANGSTROMS
REMARK 525 HOH B 445 DISTANCE = 5.15 ANGSTROMS
REMARK 525 HOH A 399 DISTANCE = 6.30 ANGSTROMS
REMARK 525 HOH A 400 DISTANCE = 5.35 ANGSTROMS
REMARK 525 HOH A 423 DISTANCE = 8.95 ANGSTROMS
REMARK 525 HOH C 417 DISTANCE = 5.57 ANGSTROMS
REMARK 525 HOH A 437 DISTANCE = 5.64 ANGSTROMS
REMARK 525 HOH C 432 DISTANCE = 9.59 ANGSTROMS
REMARK 525 HOH B 512 DISTANCE = 7.56 ANGSTROMS
REMARK 525 HOH B 513 DISTANCE = 6.17 ANGSTROMS
REMARK 525 HOH C 461 DISTANCE = 5.52 ANGSTROMS
REMARK 525 HOH C 474 DISTANCE = 5.11 ANGSTROMS
REMARK 525 HOH D 386 DISTANCE = 8.80 ANGSTROMS
REMARK 525 HOH A 484 DISTANCE = 9.90 ANGSTROMS
REMARK 525 HOH A 500 DISTANCE = 10.57 ANGSTROMS
REMARK 525 HOH A 504 DISTANCE = 10.19 ANGSTROMS
REMARK 525 HOH A 507 DISTANCE = 8.97 ANGSTROMS
REMARK 525 HOH D 420 DISTANCE = 6.83 ANGSTROMS
REMARK 525 HOH C 529 DISTANCE = 9.33 ANGSTROMS
REMARK 525 HOH D 436 DISTANCE = 6.12 ANGSTROMS
REMARK 525 HOH D 456 DISTANCE = 6.88 ANGSTROMS
REMARK 525 HOH D 472 DISTANCE = 6.96 ANGSTROMS
REMARK 525 HOH D 475 DISTANCE = 9.88 ANGSTROMS
REMARK 525 HOH D 487 DISTANCE = 7.14 ANGSTROMS
REMARK 525 HOH D 495 DISTANCE = 6.76 ANGSTROMS
REMARK 525 HOH D 499 DISTANCE = 7.45 ANGSTROMS
REMARK 525 HOH D 511 DISTANCE = 5.47 ANGSTROMS
REMARK 525 HOH D 531 DISTANCE = 5.17 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM A 142 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 87 NE2
REMARK 620 2 HOH A 900 O 175.4
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM C 142 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 87 NE2
REMARK 620 2 HOH C 902 O 178.7
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 147 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 92 NE2
REMARK 620 2 HOH B 901 O 171.0
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM D 147 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 92 NE2
REMARK 620 2 HOH D 903 O 176.4
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 142
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 147
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 142
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM D 147
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1JY7 RELATED DB: PDB
REMARK 900 RELATED ID: 1LFQ RELATED DB: PDB
REMARK 900 RELATED ID: 1Y8H RELATED DB: PDB
REMARK 900 RELATED ID: 1Y8I RELATED DB: PDB
DBREF 1Y8K A 1 141 UNP P01958 HBA_HORSE 1 141
DBREF 1Y8K C 1 141 UNP P01958 HBA_HORSE 1 141
DBREF 1Y8K B 1 146 UNP P02062 HBB_HORSE 1 146
DBREF 1Y8K D 1 146 UNP P02062 HBB_HORSE 1 146
SEQADV 1Y8K ASP A 82 UNP P01958 ASN 82 CONFLICT
SEQADV 1Y8K ASN A 85 UNP P01958 ASP 85 CONFLICT
SEQADV 1Y8K ASP C 82 UNP P01958 ASN 82 CONFLICT
SEQADV 1Y8K ASN C 85 UNP P01958 ASP 85 CONFLICT
SEQRES 1 A 141 VAL LEU SER ALA ALA ASP LYS THR ASN VAL LYS ALA ALA
SEQRES 2 A 141 TRP SER LYS VAL GLY GLY HIS ALA GLY GLU TYR GLY ALA
SEQRES 3 A 141 GLU ALA LEU GLU ARG MET PHE LEU GLY PHE PRO THR THR
SEQRES 4 A 141 LYS THR TYR PHE PRO HIS PHE ASP LEU SER HIS GLY SER
SEQRES 5 A 141 ALA GLN VAL LYS ALA HIS GLY LYS LYS VAL GLY ASP ALA
SEQRES 6 A 141 LEU THR LEU ALA VAL GLY HIS LEU ASP ASP LEU PRO GLY
SEQRES 7 A 141 ALA LEU SER ASP LEU SER ASN LEU HIS ALA HIS LYS LEU
SEQRES 8 A 141 ARG VAL ASP PRO VAL ASN PHE LYS LEU LEU SER HIS CYS
SEQRES 9 A 141 LEU LEU SER THR LEU ALA VAL HIS LEU PRO ASN ASP PHE
SEQRES 10 A 141 THR PRO ALA VAL HIS ALA SER LEU ASP LYS PHE LEU SER
SEQRES 11 A 141 SER VAL SER THR VAL LEU THR SER LYS TYR ARG
SEQRES 1 B 146 VAL GLN LEU SER GLY GLU GLU LYS ALA ALA VAL LEU ALA
SEQRES 2 B 146 LEU TRP ASP LYS VAL ASN GLU GLU GLU VAL GLY GLY GLU
SEQRES 3 B 146 ALA LEU GLY ARG LEU LEU VAL VAL TYR PRO TRP THR GLN
SEQRES 4 B 146 ARG PHE PHE ASP SER PHE GLY ASP LEU SER ASN PRO GLY
SEQRES 5 B 146 ALA VAL MET GLY ASN PRO LYS VAL LYS ALA HIS GLY LYS
SEQRES 6 B 146 LYS VAL LEU HIS SER PHE GLY GLU GLY VAL HIS HIS LEU
SEQRES 7 B 146 ASP ASN LEU LYS GLY THR PHE ALA ALA LEU SER GLU LEU
SEQRES 8 B 146 HIS CYS ASP LYS LEU HIS VAL ASP PRO GLU ASN PHE ARG
SEQRES 9 B 146 LEU LEU GLY ASN VAL LEU VAL VAL VAL LEU ALA ARG HIS
SEQRES 10 B 146 PHE GLY LYS ASP PHE THR PRO GLU LEU GLN ALA SER TYR
SEQRES 11 B 146 GLN LYS VAL VAL ALA GLY VAL ALA ASN ALA LEU ALA HIS
SEQRES 12 B 146 LYS TYR HIS
SEQRES 1 C 141 VAL LEU SER ALA ALA ASP LYS THR ASN VAL LYS ALA ALA
SEQRES 2 C 141 TRP SER LYS VAL GLY GLY HIS ALA GLY GLU TYR GLY ALA
SEQRES 3 C 141 GLU ALA LEU GLU ARG MET PHE LEU GLY 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 ALA HIS GLY LYS LYS VAL GLY ASP ALA
SEQRES 6 C 141 LEU THR LEU ALA VAL GLY HIS LEU ASP ASP LEU PRO GLY
SEQRES 7 C 141 ALA LEU SER ASP LEU SER ASN 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 SER THR LEU ALA VAL HIS LEU PRO ASN ASP PHE
SEQRES 10 C 141 THR PRO ALA VAL HIS ALA SER LEU ASP LYS PHE LEU SER
SEQRES 11 C 141 SER VAL SER THR VAL LEU THR SER LYS TYR ARG
SEQRES 1 D 146 VAL GLN LEU SER GLY GLU GLU LYS ALA ALA VAL LEU ALA
SEQRES 2 D 146 LEU TRP ASP LYS VAL ASN GLU GLU 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 ASP SER PHE GLY ASP LEU SER ASN PRO GLY
SEQRES 5 D 146 ALA VAL MET GLY ASN PRO LYS VAL LYS ALA HIS GLY LYS
SEQRES 6 D 146 LYS VAL LEU HIS SER PHE GLY GLU GLY VAL HIS HIS LEU
SEQRES 7 D 146 ASP ASN LEU LYS GLY THR PHE ALA ALA 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 VAL VAL LEU ALA ARG HIS
SEQRES 10 D 146 PHE GLY LYS ASP PHE THR PRO GLU LEU GLN ALA SER 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
HET HEM A 142 43
HET HEM B 147 43
HET HEM C 142 43
HET HEM D 147 43
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETSYN HEM HEME
FORMUL 5 HEM 4(C34 H32 FE N4 O4)
FORMUL 9 HOH *386(H2 O)
HELIX 1 1 SER A 3 GLY A 18 1 16
HELIX 2 2 HIS A 20 PHE A 36 1 17
HELIX 3 3 PRO A 37 PHE A 43 5 7
HELIX 4 4 SER A 52 GLY A 71 1 20
HELIX 5 5 HIS A 72 ASP A 74 5 3
HELIX 6 6 ASP A 75 LEU A 80 1 6
HELIX 7 7 LEU A 80 HIS A 89 1 10
HELIX 8 8 PRO A 95 LEU A 113 1 19
HELIX 9 9 THR A 118 SER A 138 1 21
HELIX 10 10 SER B 4 ASP B 16 1 13
HELIX 11 11 GLU B 21 TYR B 35 1 15
HELIX 12 12 PRO B 36 GLY B 46 5 11
HELIX 13 13 ASN B 50 ASN B 57 1 8
HELIX 14 14 ASN B 57 HIS B 76 1 20
HELIX 15 15 HIS B 77 ASP B 79 5 3
HELIX 16 16 ASN B 80 PHE B 85 1 6
HELIX 17 17 PHE B 85 LYS B 95 1 11
HELIX 18 18 ASP B 99 GLY B 119 1 21
HELIX 19 19 LYS B 120 PHE B 122 5 3
HELIX 20 20 THR B 123 LYS B 144 1 22
HELIX 21 21 SER C 3 GLY C 18 1 16
HELIX 22 22 HIS C 20 PHE C 36 1 17
HELIX 23 23 PRO C 37 PHE C 43 5 7
HELIX 24 24 SER C 52 GLY C 71 1 20
HELIX 25 25 HIS C 72 ASP C 74 5 3
HELIX 26 26 ASP C 75 LEU C 80 1 6
HELIX 27 27 LEU C 80 HIS C 89 1 10
HELIX 28 28 PRO C 95 LEU C 113 1 19
HELIX 29 29 THR C 118 SER C 138 1 21
HELIX 30 30 SER D 4 ASP D 16 1 13
HELIX 31 31 ASN D 19 TYR D 35 1 17
HELIX 32 32 PRO D 36 GLY D 46 5 11
HELIX 33 33 ASN D 50 GLY D 56 1 7
HELIX 34 34 ASN D 57 HIS D 76 1 20
HELIX 35 35 HIS D 77 ASP D 79 5 3
HELIX 36 36 ASN D 80 PHE D 85 1 6
HELIX 37 37 PHE D 85 LYS D 95 1 11
HELIX 38 38 PRO D 100 GLY D 119 1 20
HELIX 39 39 LYS D 120 PHE D 122 5 3
HELIX 40 40 THR D 123 ALA D 142 1 20
LINK NE2 HIS A 87 FE HEM A 142 1555 1555 2.16
LINK NE2 HIS C 87 FE HEM C 142 1555 1555 2.06
LINK NE2 HIS B 92 FE HEM B 147 1555 1555 2.12
LINK NE2 HIS D 92 FE HEM D 147 1555 1555 2.09
LINK FE HEM A 142 O HOH A 900 1555 1555 2.14
LINK FE HEM B 147 O HOH B 901 1555 1555 2.13
LINK FE HEM C 142 O HOH C 902 1555 1555 2.14
LINK FE HEM D 147 O HOH D 903 1555 1555 2.14
SITE 1 AC1 13 TYR A 42 PHE A 43 HIS A 45 PHE A 46
SITE 2 AC1 13 HIS A 58 LYS A 61 HIS A 87 LEU A 91
SITE 3 AC1 13 VAL A 93 PHE A 98 LEU A 101 HOH A 439
SITE 4 AC1 13 HOH A 900
SITE 1 AC2 15 LYS A 90 ARG A 141 PHE B 41 PHE B 42
SITE 2 AC2 15 HIS B 63 LYS B 66 SER B 70 PHE B 71
SITE 3 AC2 15 LEU B 88 HIS B 92 LEU B 96 ASN B 102
SITE 4 AC2 15 LEU B 106 LEU B 141 HOH B 901
SITE 1 AC3 11 TYR C 42 PHE C 43 HIS C 45 HIS C 58
SITE 2 AC3 11 LYS C 61 HIS C 87 LEU C 91 ASN C 97
SITE 3 AC3 11 PHE C 98 LEU C 101 HOH C 902
SITE 1 AC4 13 LYS C 11 PHE D 41 PHE D 42 HIS D 63
SITE 2 AC4 13 SER D 70 PHE D 71 HIS D 92 LEU D 96
SITE 3 AC4 13 ASN D 102 LEU D 141 HOH D 231 HOH D 477
SITE 4 AC4 13 HOH D 903
CRYST1 62.519 80.140 111.315 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 0.015995 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012478 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008984 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
