HEADER TRANSPORT PROTEIN 15-NOV-04 1Y0C
TITLE T-TO-THIGH QUATERNARY TRANSITIONS IN HUMAN HEMOGLOBIN: ALPHAY140F
TITLE 2 DEOXY LOW-SALT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEMOGLOBIN ALPHA CHAIN;
COMPND 3 CHAIN: A, C;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: HEMOGLOBIN BETA CHAIN;
COMPND 8 CHAIN: B, D
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: HBA1;
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
KEYWDS HEMOGLOBIN MUTANT, GLOBIN, TRANSPORT PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR J.S.KAVANAUGH,P.H.ROGERS,A.ARNONE
REVDAT 5 23-AUG-23 1Y0C 1 REMARK
REVDAT 4 20-OCT-21 1Y0C 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1Y0C 1 VERSN
REVDAT 2 17-MAY-05 1Y0C 1 JRNL
REVDAT 1 07-DEC-04 1Y0C 0
JRNL AUTH J.S.KAVANAUGH,P.H.ROGERS,A.ARNONE
JRNL TITL CRYSTALLOGRAPHIC EVIDENCE FOR A NEW ENSEMBLE OF
JRNL TITL 2 LIGAND-INDUCED ALLOSTERIC TRANSITIONS IN HEMOGLOBIN: THE
JRNL TITL 3 T-TO-T(HIGH) QUATERNARY TRANSITIONS.
JRNL REF BIOCHEMISTRY V. 44 6101 2005
JRNL REFN ISSN 0006-2960
JRNL PMID 15835899
JRNL DOI 10.1021/BI047813A
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PROLSQ
REMARK 3 AUTHORS : KONNERT,HENDRICKSON
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 24004
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : MATCHED TO PDB ENTRY 1XXT
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.169
REMARK 3 FREE R VALUE : 0.256
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2179
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.1700
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.257
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 2187
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 24070
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4378
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 172
REMARK 3 SOLVENT ATOMS : 194
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.011 ; 0.010
REMARK 3 ANGLE DISTANCE (A) : 0.026 ; 0.015
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : 0.041 ; 0.030
REMARK 3 H-BOND OR METAL COORDINATION (A) : 0.139 ; 0.100
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : 0.011 ; 0.010
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : 0.139 ; 0.080
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : 0.165 ; 0.200
REMARK 3 MULTIPLE TORSION (A) : 0.179 ; 0.200
REMARK 3 H-BOND (X...Y) (A) : 0.192 ; 0.200
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : 2.600 ; 5.000
REMARK 3 STAGGERED (DEGREES) : 21.600; 15.000
REMARK 3 TRANSVERSE (DEGREES) : 31.700; 25.000
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 2.610 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 3.736 ; 3.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 6.275 ; 4.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1Y0C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-NOV-04.
REMARK 100 THE DEPOSITION ID IS D_1000030955.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-JUN-98
REMARK 200 TEMPERATURE (KELVIN) : 298.0
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 : GRAPHITE
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : SDMS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : SDMS
REMARK 200 DATA SCALING SOFTWARE : SDMS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29663
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.270
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 200 DATA REDUNDANCY : 8.100
REMARK 200 R MERGE (I) : 0.09400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.27
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.44
REMARK 200 COMPLETENESS FOR SHELL (%) : 89.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : 0.15000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: PDB ENTRY 1XXT
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.07
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG 6000, 10 MM POTASSIUM
REMARK 280 PHOSPHATE, 100 MM POTASSIUM CHLORIDE, 3 MM SODIUM DITHIONITE, 10
REMARK 280 MG/ML HB, PH 7.0, BATCH, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 48.55000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 49.75000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 48.55000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 49.75000
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 300 REMARK: THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT IN THIS ENTRY IS AN
REMARK 300 ALPHA2BETA2 TETRAMER. THE BIOLOGICAL UNIT IS AN ALPHA2BETA2
REMARK 300 TETRAMER. THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT AND BIOLOGICAL UNIT
REMARK 300 ARE EQUIVALENT
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 11220 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23080 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -102.0 KCAL/MOL
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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 MET A 1 CG SD CE
REMARK 470 MET C 1 CG SD CE
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 ASP A 64 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ARG A 141 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ARG B 30 CD - NE - CZ ANGL. DEV. = 8.5 DEGREES
REMARK 500 ARG B 40 CD - NE - CZ ANGL. DEV. = 8.7 DEGREES
REMARK 500 ARG B 40 NE - CZ - NH1 ANGL. DEV. = 7.5 DEGREES
REMARK 500 LEU B 68 CA - CB - CG ANGL. DEV. = 14.4 DEGREES
REMARK 500 ASP B 94 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 ASP C 6 CB - CG - OD1 ANGL. DEV. = 6.8 DEGREES
REMARK 500 ASP C 64 CB - CG - OD1 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ASP C 75 CB - CG - OD2 ANGL. DEV. = -6.5 DEGREES
REMARK 500 ARG C 141 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG C 141 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 HIS D 2 N - CA - CB ANGL. DEV. = 13.2 DEGREES
REMARK 500 ARG D 30 NE - CZ - NH1 ANGL. DEV. = 8.0 DEGREES
REMARK 500 ARG D 30 NE - CZ - NH2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 ARG D 40 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ASP D 73 CB - CG - OD1 ANGL. DEV. = 6.8 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 ASP A 75 44.85 -156.05
REMARK 500 LYS A 90 -65.79 -106.61
REMARK 500 HIS B 2 72.07 -116.94
REMARK 500 PHE D 42 50.48 -118.92
REMARK 500 ASN D 80 64.28 -157.65
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 ARG A 141 0.09 SIDE CHAIN
REMARK 500 ARG C 141 0.10 SIDE CHAIN
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 A 142 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 87 NE2
REMARK 620 2 HEM A 142 NA 102.8
REMARK 620 3 HEM A 142 NB 96.8 87.8
REMARK 620 4 HEM A 142 NC 99.4 157.8 89.1
REMARK 620 5 HEM A 142 ND 106.8 87.9 156.4 86.2
REMARK 620 N 1 2 3 4
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 HEM B 147 NA 98.5
REMARK 620 3 HEM B 147 NB 102.7 89.2
REMARK 620 4 HEM B 147 NC 98.2 163.1 89.5
REMARK 620 5 HEM B 147 ND 94.6 88.6 162.7 87.7
REMARK 620 N 1 2 3 4
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 HEM C 142 NA 106.4
REMARK 620 3 HEM C 142 NB 98.7 85.7
REMARK 620 4 HEM C 142 NC 101.0 152.1 85.2
REMARK 620 5 HEM C 142 ND 112.0 87.3 149.3 87.2
REMARK 620 N 1 2 3 4
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 HEM D 147 NA 101.6
REMARK 620 3 HEM D 147 NB 100.8 88.3
REMARK 620 4 HEM D 147 NC 99.3 159.2 88.0
REMARK 620 5 HEM D 147 ND 101.0 88.9 158.2 87.0
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 142
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 147
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 142
REMARK 800
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: 1XXT RELATED DB: PDB
REMARK 900 WILD-TYPE DEOXYHEMOGLOBIN
DBREF 1Y0C A 1 141 UNP P69905 HBA_HUMAN 1 141
DBREF 1Y0C C 1 141 UNP P69905 HBA_HUMAN 1 141
DBREF 1Y0C B 1 146 UNP P68871 HBB_HUMAN 1 146
DBREF 1Y0C D 1 146 UNP P68871 HBB_HUMAN 1 146
SEQADV 1Y0C MET A 1 UNP P69905 VAL 1 ENGINEERED MUTATION
SEQADV 1Y0C PHE A 140 UNP P69905 TYR 140 ENGINEERED MUTATION
SEQADV 1Y0C MET C 1 UNP P69905 VAL 1 ENGINEERED MUTATION
SEQADV 1Y0C PHE C 140 UNP P69905 TYR 140 ENGINEERED MUTATION
SEQRES 1 A 141 MET LEU SER PRO ALA ASP LYS THR ASN VAL LYS ALA ALA
SEQRES 2 A 141 TRP GLY LYS VAL GLY ALA HIS ALA GLY GLU TYR GLY ALA
SEQRES 3 A 141 GLU ALA LEU GLU ARG MET PHE LEU SER 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 GLY HIS GLY LYS LYS VAL ALA ASP ALA
SEQRES 6 A 141 LEU THR ASN ALA VAL ALA HIS VAL ASP ASP MET PRO ASN
SEQRES 7 A 141 ALA LEU SER ALA LEU SER ASP 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 VAL THR LEU ALA ALA HIS LEU PRO ALA GLU PHE
SEQRES 10 A 141 THR PRO ALA VAL HIS ALA SER LEU ASP LYS PHE LEU ALA
SEQRES 11 A 141 SER VAL SER THR VAL LEU THR SER LYS PHE ARG
SEQRES 1 B 146 VAL HIS LEU THR PRO GLU GLU LYS SER ALA VAL THR ALA
SEQRES 2 B 146 LEU TRP GLY LYS VAL ASN VAL ASP 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 GLU SER PHE GLY ASP LEU SER THR PRO ASP
SEQRES 5 B 146 ALA VAL MET GLY ASN PRO LYS VAL LYS ALA HIS GLY LYS
SEQRES 6 B 146 LYS VAL LEU GLY ALA PHE SER ASP GLY LEU ALA HIS LEU
SEQRES 7 B 146 ASP ASN LEU LYS GLY THR PHE ALA THR 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 CYS VAL LEU ALA HIS HIS
SEQRES 10 B 146 PHE GLY LYS GLU PHE THR PRO PRO VAL GLN ALA ALA 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 MET 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 PHE 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
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 *194(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 HIS A 72 1 21
HELIX 5 5 ASP A 75 LEU A 80 1 6
HELIX 6 6 LEU A 80 LYS A 90 1 11
HELIX 7 7 PRO A 95 ALA A 111 1 17
HELIX 8 8 THR A 118 THR A 137 1 20
HELIX 9 9 THR B 4 VAL B 18 1 15
HELIX 10 10 ASN B 19 TYR B 35 1 17
HELIX 11 11 PRO B 36 GLY B 46 5 11
HELIX 12 12 THR B 50 ASN B 57 1 8
HELIX 13 13 ASN B 57 LEU B 75 1 19
HELIX 14 14 ASN B 80 LYS B 95 1 16
HELIX 15 15 PRO B 100 GLY B 119 1 20
HELIX 16 16 LYS B 120 PHE B 122 5 3
HELIX 17 17 THR B 123 HIS B 143 1 21
HELIX 18 18 SER C 3 GLY C 18 1 16
HELIX 19 19 HIS C 20 PHE C 36 1 17
HELIX 20 20 PRO C 37 PHE C 43 5 7
HELIX 21 21 SER C 52 HIS C 72 1 21
HELIX 22 22 ASP C 75 LEU C 80 1 6
HELIX 23 23 LEU C 80 LYS C 90 1 11
HELIX 24 24 PRO C 95 LEU C 113 1 19
HELIX 25 25 THR C 118 THR C 137 1 20
HELIX 26 26 THR D 4 GLY D 16 1 13
HELIX 27 27 ASN D 19 TYR D 35 1 17
HELIX 28 28 PRO D 36 GLY D 46 5 11
HELIX 29 29 THR D 50 ASN D 57 1 8
HELIX 30 30 ASN D 57 LEU D 75 1 19
HELIX 31 31 ASN D 80 PHE D 85 1 6
HELIX 32 32 PHE D 85 LYS D 95 1 11
HELIX 33 33 PRO D 100 GLY D 119 1 20
HELIX 34 34 LYS D 120 PHE D 122 5 3
HELIX 35 35 THR D 123 HIS D 143 1 21
LINK NE2 HIS A 87 FE HEM A 142 1555 1555 2.19
LINK NE2 HIS B 92 FE HEM B 147 1555 1555 2.21
LINK NE2 HIS C 87 FE HEM C 142 1555 1555 2.20
LINK NE2 HIS D 92 FE HEM D 147 1555 1555 2.18
SITE 1 AC1 17 TYR A 42 PHE A 43 HIS A 45 HIS A 58
SITE 2 AC1 17 LYS A 61 LEU A 83 LEU A 86 HIS A 87
SITE 3 AC1 17 LEU A 91 VAL A 93 ASN A 97 PHE A 98
SITE 4 AC1 17 LEU A 101 VAL A 132 LEU A 136 HOH A 219
SITE 5 AC1 17 HOH A 336
SITE 1 AC2 14 HIS A 72 ASP A 75 PHE B 41 HIS B 63
SITE 2 AC2 14 VAL B 67 ALA B 70 LEU B 91 HIS B 92
SITE 3 AC2 14 LEU B 96 ASN B 102 PHE B 103 LEU B 141
SITE 4 AC2 14 HOH B 244 HOH B 262
SITE 1 AC3 17 LYS B 17 LYS B 120 TYR C 42 PHE C 43
SITE 2 AC3 17 HIS C 45 PHE C 46 HIS C 58 LYS C 61
SITE 3 AC3 17 LEU C 83 HIS C 87 LEU C 91 VAL C 93
SITE 4 AC3 17 ASN C 97 PHE C 98 LEU C 101 LEU C 136
SITE 5 AC3 17 HOH C 256
SITE 1 AC4 9 PHE D 42 HIS D 63 LYS D 66 VAL D 67
SITE 2 AC4 9 HIS D 92 LEU D 96 ASN D 102 PHE D 103
SITE 3 AC4 9 LEU D 141
CRYST1 97.100 99.500 66.000 90.00 90.00 90.00 P 21 21 2 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 0.010299 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010050 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015152 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
