HEADER OXYGEN TRANSPORT 18-SEP-92 1CMY
TITLE THE MUTATION BETA99 ASP-TYR STABILIZES Y-A NEW, COMPOSITE QUATERNARY
TITLE 2 STATE OF HUMAN HEMOGLOBIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEMOGLOBIN YPSILANTI (CARBONMONOXY) (ALPHA CHAIN);
COMPND 3 CHAIN: A, C;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: HEMOGLOBIN YPSILANTI (CARBONMONOXY) (BETA CHAIN);
COMPND 7 CHAIN: B, D;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 7 ORGANISM_COMMON: HUMAN;
SOURCE 8 ORGANISM_TAXID: 9606
KEYWDS OXYGEN TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR F.R.SMITH,E.E.LATTMAN,C.W.CARTER JUNIOR
REVDAT 4 07-FEB-24 1CMY 1 REMARK SEQADV LINK
REVDAT 3 24-FEB-09 1CMY 1 VERSN
REVDAT 2 01-APR-03 1CMY 1 JRNL
REVDAT 1 31-OCT-93 1CMY 0
JRNL AUTH F.R.SMITH,E.E.LATTMAN,C.W.CARTER JR.
JRNL TITL THE MUTATION BETA 99 ASP-TYR STABILIZES Y--A NEW, COMPOSITE
JRNL TITL 2 QUATERNARY STATE OF HUMAN HEMOGLOBIN.
JRNL REF PROTEINS V. 10 81 1991
JRNL REFN ISSN 0887-3585
JRNL PMID 1896430
JRNL DOI 10.1002/PROT.340100202
REMARK 2
REMARK 2 RESOLUTION. 3.00 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) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : NULL
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : NULL
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : 0.269
REMARK 3 R VALUE (WORKING SET) : NULL
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
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) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4392
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 172
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) : 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) : 0.008 ; 0.020
REMARK 3 ANGLE DISTANCE (A) : 0.021 ; 0.030
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : 0.027 ; 0.050
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : 0.007 ; 0.020
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : 0.113 ; 0.150
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : 0.210 ; 0.500
REMARK 3 MULTIPLE TORSION (A) : 0.279 ; 0.500
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : 0.250 ; 0.500
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : 1.300 ; 3.000
REMARK 3 STAGGERED (DEGREES) : 23.000; 15.000
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
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 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1CMY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000172402.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : NULL
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
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) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.91
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 96.40000
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 48.20000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 48.20000
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 96.40000
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: 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 OD1 ASN B 139 OH TYR D 145 1.70
REMARK 500 OH TYR B 145 OD1 ASN D 139 1.89
REMARK 500 O PHE C 36 OG1 THR C 39 2.08
REMARK 500 OE2 GLU D 7 NZ LYS D 132 2.12
REMARK 500 NH2 ARG C 31 O PHE D 122 2.17
REMARK 500 OD2 ASP C 47 OG SER C 49 2.17
REMARK 500 O LEU B 32 NE2 GLN B 39 2.19
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 CA LYS A 16 OE2 GLU D 90 4567 0.76
REMARK 500 CE LYS C 90 CA SER D 44 2664 1.03
REMARK 500 CE LYS C 90 C SER D 44 2664 1.19
REMARK 500 NZ LYS C 90 CB SER D 44 2664 1.25
REMARK 500 O GLY A 15 OE1 GLU D 90 4567 1.29
REMARK 500 CD LYS C 90 O SER D 44 2664 1.38
REMARK 500 N LYS A 16 OE2 GLU D 90 4567 1.38
REMARK 500 CE LYS C 90 CB SER D 44 2664 1.47
REMARK 500 NZ LYS C 90 OG SER D 44 2664 1.50
REMARK 500 O GLY A 15 CD GLU D 90 4567 1.50
REMARK 500 CE LYS C 90 O SER D 44 2664 1.58
REMARK 500 NE2 HIS A 20 O GLY D 83 4567 1.61
REMARK 500 C LYS A 16 OE2 GLU D 90 4567 1.70
REMARK 500 C GLY A 15 CD GLU D 90 4567 1.84
REMARK 500 NZ LYS B 95 O2D HEM A 142 2664 1.91
REMARK 500 CD LYS C 90 C SER D 44 2664 1.98
REMARK 500 CA LYS A 16 CD GLU D 90 4567 1.98
REMARK 500 N LYS A 16 CD GLU D 90 4567 2.02
REMARK 500 C GLY A 15 OE2 GLU D 90 4567 2.03
REMARK 500 CG LYS C 90 O SER D 44 2664 2.04
REMARK 500 CB ASN D 19 ND2 ASN D 19 4557 2.05
REMARK 500 NZ LYS A 61 NZ LYS B 95 3565 2.06
REMARK 500 OD2 ASP B 47 NE2 HIS C 20 6666 2.08
REMARK 500 NZ LYS C 90 CA SER D 44 2664 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 C 141 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 THR D 50 N - CA - CB ANGL. DEV. = 12.8 DEGREES
REMARK 500 HIS D 77 CA - CB - CG ANGL. DEV. = 13.9 DEGREES
REMARK 500 ASP D 79 CB - CG - OD1 ANGL. DEV. = -7.3 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 LEU A 2 102.67 85.58
REMARK 500 PHE A 43 61.18 -119.51
REMARK 500 HIS A 50 -72.93 -24.16
REMARK 500 HIS A 72 18.16 132.96
REMARK 500 ASP A 75 44.79 -162.20
REMARK 500 HIS A 89 -72.39 -77.38
REMARK 500 HIS B 2 -63.75 -136.69
REMARK 500 LEU B 3 108.45 42.46
REMARK 500 ALA B 76 53.40 -117.88
REMARK 500 HIS B 77 28.75 -175.52
REMARK 500 CYS B 93 -84.89 -71.87
REMARK 500 ASP B 94 53.58 -103.45
REMARK 500 LYS B 95 -39.31 -155.72
REMARK 500 PHE B 122 70.98 -106.23
REMARK 500 LEU C 2 104.32 86.05
REMARK 500 PHE C 43 60.17 -115.78
REMARK 500 HIS C 50 -78.98 -23.24
REMARK 500 HIS C 72 18.84 132.47
REMARK 500 ASP C 75 48.72 -161.82
REMARK 500 HIS D 2 -66.55 -131.98
REMARK 500 LEU D 3 104.97 46.61
REMARK 500 ALA D 76 50.07 -116.30
REMARK 500 HIS D 77 36.74 -178.89
REMARK 500 CYS D 93 -78.86 -76.30
REMARK 500 ASP D 94 50.89 -103.17
REMARK 500 LYS D 95 -34.96 -154.70
REMARK 500 PRO D 100 -28.44 -39.77
REMARK 500 PHE D 122 71.53 -105.73
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 92.2
REMARK 620 3 HEM A 142 NB 91.5 90.6
REMARK 620 4 HEM A 142 NC 88.2 179.5 89.8
REMARK 620 5 HEM A 142 ND 87.4 89.6 178.9 90.0
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 84.5
REMARK 620 3 HEM B 147 NB 92.1 90.7
REMARK 620 4 HEM B 147 NC 91.6 176.1 90.0
REMARK 620 5 HEM B 147 ND 84.6 89.8 176.6 89.3
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 84.0
REMARK 620 3 HEM C 142 NB 92.3 89.7
REMARK 620 4 HEM C 142 NC 89.3 173.2 89.3
REMARK 620 5 HEM C 142 ND 80.0 89.3 172.3 90.8
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 93.4
REMARK 620 3 HEM D 147 NB 101.4 90.0
REMARK 620 4 HEM D 147 NC 84.2 177.5 90.0
REMARK 620 5 HEM D 147 ND 76.5 90.5 177.8 89.4
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
DBREF 1CMY A 1 141 UNP P69905 HBA_HUMAN 1 141
DBREF 1CMY B 1 146 UNP P68871 HBB_HUMAN 1 146
DBREF 1CMY C 1 141 UNP P69905 HBA_HUMAN 1 141
DBREF 1CMY D 1 146 UNP P68871 HBB_HUMAN 1 146
SEQADV 1CMY TYR B 99 UNP P68871 ASP 99 CONFLICT
SEQADV 1CMY TYR D 99 UNP P68871 ASP 99 CONFLICT
SEQRES 1 A 141 VAL 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 TYR 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 TYR 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 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 TYR 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)
HELIX 1 AA SER A 3 GLY A 18 1 16
HELIX 2 AB HIS A 20 SER A 35 1 16
HELIX 3 AC PHE A 36 TYR A 42 1 7
HELIX 4 AD SER A 52 ALA A 71 1 20
HELIX 5 AE LEU A 80 ALA A 88 1 9
HELIX 6 AG ASP A 94 HIS A 112 1 19
HELIX 7 AH THR A 118 SER A 138 1 21
HELIX 8 BA THR B 4 VAL B 18 1 15
HELIX 9 BB ASN B 19 VAL B 34 1 16
HELIX 10 BC TYR B 35 PHE B 41 1 7
HELIX 11 BD THR B 50 GLY B 56 1 7
HELIX 12 BE ASN B 57 ALA B 76 1 20
HELIX 13 BF PHE B 85 CYS B 93 1 9
HELIX 14 BG TYR B 99 HIS B 117 1 19
HELIX 15 BH THR B 123 HIS B 143 1 21
HELIX 16 CA SER C 3 GLY C 18 1 16
HELIX 17 CB HIS C 20 SER C 35 1 16
HELIX 18 CC PHE C 36 TYR C 42 1 7
HELIX 19 CD SER C 52 ALA C 71 1 20
HELIX 20 CE LEU C 80 ALA C 88 1 9
HELIX 21 CG ASP C 94 HIS C 112 1 19
HELIX 22 CH THR C 118 SER C 138 1 21
HELIX 23 DA THR D 4 VAL D 18 1 15
HELIX 24 DB ASN D 19 VAL D 34 1 16
HELIX 25 DC TYR D 35 PHE D 41 1 7
HELIX 26 DD THR D 50 GLY D 56 1 7
HELIX 27 DE ASN D 57 ALA D 76 1 20
HELIX 28 DF PHE D 85 CYS D 93 1 9
HELIX 29 DG TYR D 99 HIS D 117 1 19
HELIX 30 DH THR D 123 HIS D 143 1 21
LINK NE2 HIS A 87 FE HEM A 142 1555 1555 2.02
LINK NE2 HIS B 92 FE HEM B 147 1555 1555 2.03
LINK NE2 HIS C 87 FE HEM C 142 1555 1555 2.09
LINK NE2 HIS D 92 FE HEM D 147 1555 1555 1.99
SITE 1 AC1 16 TYR A 42 PHE A 43 HIS A 45 PHE A 46
SITE 2 AC1 16 HIS A 58 LYS A 61 VAL A 62 ALA A 65
SITE 3 AC1 16 HIS A 87 LEU A 91 VAL A 93 ASN A 97
SITE 4 AC1 16 PHE A 98 LEU A 101 VAL A 132 LYS B 95
SITE 1 AC2 12 THR B 38 PHE B 41 PHE B 42 HIS B 63
SITE 2 AC2 12 LYS B 66 PHE B 71 HIS B 92 VAL B 98
SITE 3 AC2 12 ASN B 102 LEU B 106 VAL B 137 LEU B 141
SITE 1 AC3 14 TYR C 42 PHE C 43 HIS C 45 PHE C 46
SITE 2 AC3 14 HIS C 58 LYS C 61 LEU C 83 HIS C 87
SITE 3 AC3 14 LEU C 91 VAL C 93 ASN C 97 PHE C 98
SITE 4 AC3 14 LEU C 101 VAL C 132
SITE 1 AC4 15 THR D 38 PHE D 41 PHE D 42 HIS D 63
SITE 2 AC4 15 LYS D 66 VAL D 67 PHE D 71 LEU D 88
SITE 3 AC4 15 LEU D 91 HIS D 92 LEU D 96 VAL D 98
SITE 4 AC4 15 ASN D 102 LEU D 106 LEU D 141
CRYST1 93.100 93.100 144.600 90.00 90.00 120.00 P 32 2 1 12
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 0.010741 0.006201 0.000000 0.00000
SCALE2 0.000000 0.012403 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006916 0.00000
MTRIX1 1 0.033590 0.987120 0.156400 -75.69865 1
MTRIX2 1 0.986080 -0.058230 0.155740 36.84016 1
MTRIX3 1 0.162840 0.148990 -0.975340 260.36945 1
(ATOM LINES ARE NOT SHOWN.)
END