HEADER OXYGEN TRANSPORT 13-JUL-09 3IA3
TITLE A CIS-PROLINE IN ALPHA-HEMOGLOBIN STABILIZING PROTEIN DIRECTS THE
TITLE 2 STRUCTURAL REORGANIZATION OF ALPHA-HEMOGLOBIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA-HEMOGLOBIN-STABILIZING PROTEIN;
COMPND 3 CHAIN: A, C;
COMPND 4 SYNONYM: ERYTHROID-ASSOCIATED FACTOR, ERYTHROID DIFFERENTIATION-
COMPND 5 RELATED FACTOR;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: HEMOGLOBIN SUBUNIT ALPHA;
COMPND 9 CHAIN: B, D;
COMPND 10 SYNONYM: HEMOGLOBIN ALPHA CHAIN, ALPHA-GLOBIN;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: AHSP, EDRF, ERAF;
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 GENE: HBA1, HBA2;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HEMOGLOBIN, CIS-PROLINE, AHSP, STABILIZATION, CHAPERONE, CYTOPLASM,
KEYWDS 2 POLYMORPHISM, ACETYLATION, DISEASE MUTATION, GLYCATION,
KEYWDS 3 GLYCOPROTEIN, HEME, IRON, METAL-BINDING, OXYGEN TRANSPORT,
KEYWDS 4 PHOSPHOPROTEIN, TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR L.FENG,P.D.JEFFREY,Y.SHI
REVDAT 3 21-FEB-24 3IA3 1 REMARK
REVDAT 2 27-OCT-09 3IA3 1 JRNL
REVDAT 1 28-JUL-09 3IA3 0
JRNL AUTH D.A.GELL,L.FENG,S.ZHOU,P.D.JEFFREY,K.BENDAK,A.GOW,M.J.WEISS,
JRNL AUTH 2 Y.SHI,J.P.MACKAY
JRNL TITL A CIS-PROLINE IN ALPHA-HEMOGLOBIN STABILIZING PROTEIN
JRNL TITL 2 DIRECTS THE STRUCTURAL REORGANIZATION OF ALPHA-HEMOGLOBIN.
JRNL REF J.BIOL.CHEM. V. 284 29462 2009
JRNL REFN ISSN 0021-9258
JRNL PMID 19706593
JRNL DOI 10.1074/JBC.M109.027045
REMARK 2
REMARK 2 RESOLUTION. 3.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.2
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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 21.25
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2259220.540
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 84.7
REMARK 3 NUMBER OF REFLECTIONS : 8538
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) : 0.230
REMARK 3 FREE R VALUE : 0.293
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 439
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.014
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) : 3.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.40
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 54.90
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 852
REMARK 3 BIN R VALUE (WORKING SET) : 0.2870
REMARK 3 BIN FREE R VALUE : 0.3840
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.20
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 37
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.063
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3520
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 86
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 82.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -15.96000
REMARK 3 B22 (A**2) : -15.96000
REMARK 3 B33 (A**2) : 31.91000
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) : 0.40
REMARK 3 ESD FROM SIGMAA (A) : 0.46
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.51
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.58
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 19.30
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.810
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 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.30
REMARK 3 BSOL : 49.83
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 : DNA-RNA_REP.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : HEM.PARAM
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : DNA-RNA.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : HEM.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED
REMARK 4
REMARK 4 3IA3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-JUL-09.
REMARK 100 THE DEPOSITION ID IS D_1000054154.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-NOV-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CHESS
REMARK 200 BEAMLINE : A1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.918
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 8764
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 85.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05800
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) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 51.1
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.45300
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: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.17
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES, PH 6.5, 4% ACETONITRILE AND
REMARK 280 14.5% (W/V) PEG3000, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
REMARK 290 7555 Y,X,-Z+1/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+2/3
REMARK 290 10555 -Y,-X,-Z+5/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 146.55333
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 293.10667
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 219.83000
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 366.38333
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 73.27667
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 146.55333
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 293.10667
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 366.38333
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 219.83000
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 73.27667
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 300 REMARK: HETERODIMER OF ALPHA-HEMOGLOBIN STABILIZING PROTEIN AND
REMARK 300 ALPHA-HEMOGLOBIN WITH HEME, TWO COPIES IN THE ASYMMETRIC UNIT.
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: 2880 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11900 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2900 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11830 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 GLY B -3
REMARK 465 SER B -2
REMARK 465 HIS B -1
REMARK 465 MET B 0
REMARK 465 VAL B 1
REMARK 465 THR B 137
REMARK 465 SER B 138
REMARK 465 LYS B 139
REMARK 465 TYR B 140
REMARK 465 ARG B 141
REMARK 465 MET C 1
REMARK 465 GLY D -3
REMARK 465 SER D -2
REMARK 465 HIS D -1
REMARK 465 MET D 0
REMARK 465 VAL D 1
REMARK 465 THR D 137
REMARK 465 SER D 138
REMARK 465 LYS D 139
REMARK 465 TYR D 140
REMARK 465 ARG D 141
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 CD1 TYR D 42 CD1 TYR D 42 12545 1.83
REMARK 500 CD2 TYR B 42 CD2 TYR B 42 12545 2.08
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 LEU A 4 -157.09 165.85
REMARK 500 ARG A 53 23.05 -69.53
REMARK 500 PRO A 60 6.09 -50.35
REMARK 500 LYS B 16 -73.68 -66.30
REMARK 500 THR B 41 -32.59 -39.20
REMARK 500 TYR B 42 -114.06 -119.74
REMARK 500 PHE B 43 65.76 75.61
REMARK 500 PHE B 46 5.77 57.74
REMARK 500 ASP B 47 59.42 38.29
REMARK 500 SER B 52 20.22 -73.10
REMARK 500 ALA B 79 -51.29 -28.80
REMARK 500 PRO B 95 -13.42 -48.31
REMARK 500 LEU B 113 79.10 -118.24
REMARK 500 SER B 131 65.65 -102.81
REMARK 500 LEU C 4 -157.37 166.91
REMARK 500 ASN C 46 -7.67 -51.11
REMARK 500 PHE C 47 -60.81 -91.66
REMARK 500 ARG C 53 22.37 -69.93
REMARK 500 PRO C 60 5.91 -49.94
REMARK 500 THR D 41 -31.10 -38.91
REMARK 500 TYR D 42 -103.77 -119.60
REMARK 500 PHE D 43 69.64 66.04
REMARK 500 PHE D 46 2.56 53.27
REMARK 500 ASP D 47 60.73 39.58
REMARK 500 SER D 52 20.52 -77.35
REMARK 500 SER D 131 66.37 -104.69
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 B 201 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 58 NE2
REMARK 620 2 HEM B 201 NA 95.2
REMARK 620 3 HEM B 201 NB 92.6 87.0
REMARK 620 4 HEM B 201 NC 84.4 177.0 90.0
REMARK 620 5 HEM B 201 ND 88.3 90.6 177.5 92.4
REMARK 620 6 HIS B 87 NE2 174.5 87.7 92.2 92.9 87.0
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 58 NE2
REMARK 620 2 HEM D 201 NA 96.7
REMARK 620 3 HEM D 201 NB 95.4 87.5
REMARK 620 4 HEM D 201 NC 83.6 177.2 89.8
REMARK 620 5 HEM D 201 ND 85.5 90.4 177.8 92.3
REMARK 620 6 HIS D 87 NE2 171.3 86.8 92.7 93.3 86.5
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 HEM B 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM D 201
DBREF 3IA3 A 1 91 UNP Q9NZD4 AHSP_HUMAN 1 91
DBREF 3IA3 B 0 141 UNP P69905 HBA_HUMAN 1 142
DBREF 3IA3 C 1 91 UNP Q9NZD4 AHSP_HUMAN 1 91
DBREF 3IA3 D 0 141 UNP P69905 HBA_HUMAN 1 142
SEQADV 3IA3 GLY B -3 UNP P69905 EXPRESSION TAG
SEQADV 3IA3 SER B -2 UNP P69905 EXPRESSION TAG
SEQADV 3IA3 HIS B -1 UNP P69905 EXPRESSION TAG
SEQADV 3IA3 GLY D -3 UNP P69905 EXPRESSION TAG
SEQADV 3IA3 SER D -2 UNP P69905 EXPRESSION TAG
SEQADV 3IA3 HIS D -1 UNP P69905 EXPRESSION TAG
SEQRES 1 A 91 MET ALA LEU LEU LYS ALA ASN LYS ASP LEU ILE SER ALA
SEQRES 2 A 91 GLY LEU LYS GLU PHE SER VAL LEU LEU ASN GLN GLN VAL
SEQRES 3 A 91 PHE ASN ASP PRO LEU VAL SER GLU GLU ASP MET VAL THR
SEQRES 4 A 91 VAL VAL GLU ASP TRP MET ASN PHE TYR ILE ASN TYR TYR
SEQRES 5 A 91 ARG GLN GLN VAL THR GLY GLU PRO GLN GLU ARG ASP LYS
SEQRES 6 A 91 ALA LEU GLN GLU LEU ARG GLN GLU LEU ASN THR LEU ALA
SEQRES 7 A 91 ASN PRO PHE LEU ALA LYS TYR ARG ASP PHE LEU LYS SER
SEQRES 1 B 145 GLY SER HIS MET VAL LEU SER PRO ALA ASP LYS THR ASN
SEQRES 2 B 145 VAL LYS ALA ALA TRP GLY LYS VAL GLY ALA HIS ALA GLY
SEQRES 3 B 145 GLU TYR GLY ALA GLU ALA LEU GLU ARG MET PHE LEU SER
SEQRES 4 B 145 PHE PRO THR THR LYS THR TYR PHE PRO HIS PHE ASP LEU
SEQRES 5 B 145 SER HIS GLY SER ALA GLN VAL LYS GLY HIS GLY LYS LYS
SEQRES 6 B 145 VAL ALA ASP ALA LEU THR ASN ALA VAL ALA HIS VAL ASP
SEQRES 7 B 145 ASP MET PRO ASN ALA LEU SER ALA LEU SER ASP LEU HIS
SEQRES 8 B 145 ALA HIS LYS LEU ARG VAL ASP PRO VAL ASN PHE LYS LEU
SEQRES 9 B 145 LEU SER HIS CYS LEU LEU VAL THR LEU ALA ALA HIS LEU
SEQRES 10 B 145 PRO ALA GLU PHE THR PRO ALA VAL HIS ALA SER LEU ASP
SEQRES 11 B 145 LYS PHE LEU ALA SER VAL SER THR VAL LEU THR SER LYS
SEQRES 12 B 145 TYR ARG
SEQRES 1 C 91 MET ALA LEU LEU LYS ALA ASN LYS ASP LEU ILE SER ALA
SEQRES 2 C 91 GLY LEU LYS GLU PHE SER VAL LEU LEU ASN GLN GLN VAL
SEQRES 3 C 91 PHE ASN ASP PRO LEU VAL SER GLU GLU ASP MET VAL THR
SEQRES 4 C 91 VAL VAL GLU ASP TRP MET ASN PHE TYR ILE ASN TYR TYR
SEQRES 5 C 91 ARG GLN GLN VAL THR GLY GLU PRO GLN GLU ARG ASP LYS
SEQRES 6 C 91 ALA LEU GLN GLU LEU ARG GLN GLU LEU ASN THR LEU ALA
SEQRES 7 C 91 ASN PRO PHE LEU ALA LYS TYR ARG ASP PHE LEU LYS SER
SEQRES 1 D 145 GLY SER HIS MET VAL LEU SER PRO ALA ASP LYS THR ASN
SEQRES 2 D 145 VAL LYS ALA ALA TRP GLY LYS VAL GLY ALA HIS ALA GLY
SEQRES 3 D 145 GLU TYR GLY ALA GLU ALA LEU GLU ARG MET PHE LEU SER
SEQRES 4 D 145 PHE PRO THR THR LYS THR TYR PHE PRO HIS PHE ASP LEU
SEQRES 5 D 145 SER HIS GLY SER ALA GLN VAL LYS GLY HIS GLY LYS LYS
SEQRES 6 D 145 VAL ALA ASP ALA LEU THR ASN ALA VAL ALA HIS VAL ASP
SEQRES 7 D 145 ASP MET PRO ASN ALA LEU SER ALA LEU SER ASP LEU HIS
SEQRES 8 D 145 ALA HIS LYS LEU ARG VAL ASP PRO VAL ASN PHE LYS LEU
SEQRES 9 D 145 LEU SER HIS CYS LEU LEU VAL THR LEU ALA ALA HIS LEU
SEQRES 10 D 145 PRO ALA GLU PHE THR PRO ALA VAL HIS ALA SER LEU ASP
SEQRES 11 D 145 LYS PHE LEU ALA SER VAL SER THR VAL LEU THR SER LYS
SEQRES 12 D 145 TYR ARG
HET HEM B 201 43
HET HEM D 201 43
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETSYN HEM HEME
FORMUL 5 HEM 2(C34 H32 FE N4 O4)
HELIX 1 1 LYS A 5 GLN A 24 1 20
HELIX 2 2 SER A 33 ARG A 53 1 21
HELIX 3 3 GLU A 62 SER A 91 1 30
HELIX 4 4 SER B 3 GLY B 18 1 16
HELIX 5 5 TYR B 24 PHE B 36 1 13
HELIX 6 6 PRO B 37 LYS B 40 5 4
HELIX 7 7 PRO B 44 GLY B 51 5 8
HELIX 8 8 SER B 52 HIS B 72 1 21
HELIX 9 9 ASN B 78 LYS B 90 1 13
HELIX 10 10 ASP B 94 LEU B 113 1 20
HELIX 11 11 THR B 118 LEU B 129 1 12
HELIX 12 12 LYS C 5 GLN C 24 1 20
HELIX 13 13 SER C 33 ARG C 53 1 21
HELIX 14 14 GLU C 62 SER C 91 1 30
HELIX 15 15 SER D 3 GLY D 18 1 16
HELIX 16 16 HIS D 20 GLU D 23 5 4
HELIX 17 17 TYR D 24 PHE D 36 1 13
HELIX 18 18 PRO D 37 LYS D 40 5 4
HELIX 19 19 ASP D 47 GLY D 51 5 5
HELIX 20 20 SER D 52 HIS D 72 1 21
HELIX 21 21 ASN D 78 LYS D 90 1 13
HELIX 22 22 ASP D 94 LEU D 113 1 20
HELIX 23 23 THR D 118 ALA D 130 1 13
LINK NE2 HIS B 58 FE HEM B 201 1555 1555 2.20
LINK NE2 HIS B 87 FE HEM B 201 1555 1555 2.00
LINK NE2 HIS D 58 FE HEM D 201 1555 1555 2.19
LINK NE2 HIS D 87 FE HEM D 201 1555 1555 2.00
CISPEP 1 ASP A 29 PRO A 30 0 -0.08
CISPEP 2 ASP C 29 PRO C 30 0 -0.04
SITE 1 AC1 17 PHE B 43 HIS B 45 PHE B 46 HIS B 58
SITE 2 AC1 17 LYS B 61 VAL B 62 ALA B 65 LEU B 83
SITE 3 AC1 17 HIS B 87 VAL B 93 ASN B 97 PHE B 98
SITE 4 AC1 17 LEU B 101 SER B 102 PRO D 77 ASN D 78
SITE 5 AC1 17 ALA D 79
SITE 1 AC2 18 MET B 76 PRO B 77 ASN B 78 ALA B 79
SITE 2 AC2 18 PHE D 43 HIS D 45 PHE D 46 HIS D 58
SITE 3 AC2 18 LYS D 61 VAL D 62 ALA D 65 LEU D 83
SITE 4 AC2 18 HIS D 87 VAL D 93 ASN D 97 PHE D 98
SITE 5 AC2 18 LEU D 101 SER D 102
CRYST1 65.230 65.230 439.660 90.00 90.00 120.00 P 61 2 2 24
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 0.015330 0.008851 0.000000 0.00000
SCALE2 0.000000 0.017702 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002274 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
