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HEADER OXYGEN STORAGE/TRANSPORT 06-DEC-98 1HBR TITLE R-STATE FORM OF CHICKEN HEMOGLOBIN D COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROTEIN (HEMOGLOBIN D); COMPND 3 CHAIN: A, C; COMPND 4 SYNONYM: HB D; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: PROTEIN (HEMOGLOBIN D); COMPND 7 CHAIN: B, D; COMPND 8 SYNONYM: HB D SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: GALLUS GALLUS; SOURCE 3 ORGANISM_COMMON: CHICKEN; SOURCE 4 TISSUE: BLOOD; SOURCE 5 CELL: ERYTHROCYTES; SOURCE 6 CELLULAR_LOCATION: CYTOPLASM; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: GALLUS GALLUS; SOURCE 9 ORGANISM_COMMON: CHICKEN; SOURCE 10 TISSUE: BLOOD; SOURCE 11 CELL: ERYTHROCYTES; SOURCE 12 CELLULAR_LOCATION: CYTOPLASM KEYWDS HEMOGLOBIN D (R-STATE) 1, HEMOGLOBIN, AVIAN, HIGH KEYWDS 2 COOPERATIITY, OXYGEN TRANSPORT EXPDTA X-RAY DIFFRACTION AUTHOR E.KNAPP,M.A.OLIVEIRA,Q.XIE,S.R.ERNST,A.F.RIGGS,M.L.HACKERT REVDAT 2 15-MAR-00 1HBR 1 COMPND HEADER REMARK REVDAT 1 26-MAR-99 1HBR 0 JRNL AUTH J.E.KNAPP,M.A.OLIVEIRA,Q.XIE,S.R.ERNST,A.F.RIGGS, JRNL AUTH 2 M.L.HACKERT JRNL TITL THE STRUCTURAL AND FUNCTIONAL ANALYSIS OF THE JRNL TITL 2 HEMOGLOBIN D COMPONENT FROM CHICKEN. JRNL REF J.BIOL.CHEM. V. 274 6411 1999 JRNL REFN ASTM JBCHA3 US ISSN 0021-9258 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH B.SHAANAN REMARK 1 TITL STRUCTURE OF HUMAN OXYHAEMOGLOBIN AT 2.1 A REMARK 1 TITL 2 RESOLUTION REMARK 1 REF J.MOL.BIOL. V. 171 31 1983 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 REMARK 1 REFERENCE 2 REMARK 1 AUTH J.B.DODGSON,J.D.ENGEL REMARK 1 TITL THE NUCLEOTIDE SEQUENCE OF THE ADULT CHICKEN REMARK 1 TITL 2 ALPHA-GLOBIN GENES REMARK 1 REF J.BIOL.CHEM. V. 258 4623 1983 REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258 REMARK 1 REFERENCE 3 REMARK 1 AUTH M.DOLAN,J.B.DODGSON,J.D.ENGEL REMARK 1 TITL ANALYSIS OF THE ADULT CHICKEN BETA-GLOBIN GENE REMARK 1 REF J.BIOL.CHEM. V. 258 3983 1983 REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258 REMARK 2 REMARK 2 RESOLUTION. 2.30 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.851 REMARK 3 AUTHORS : BRUNGER 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)) : 0.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 10000000.000 REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0010 REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.1 REMARK 3 NUMBER OF REFLECTIONS : 29702 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) : 0.222 REMARK 3 FREE R VALUE : 0.257 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.900 REMARK 3 FREE R VALUE TEST SET COUNT : 2949 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005 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) (%) : 96.90 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4343 REMARK 3 BIN R VALUE (WORKING SET) : 0.2920 REMARK 3 BIN FREE R VALUE : 0.3630 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.90 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 476 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.017 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 4331 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 172 REMARK 3 SOLVENT ATOMS : 147 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 28.00 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.10 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.00000 REMARK 3 B22 (A**2) : 0.00000 REMARK 3 B33 (A**2) : 0.00000 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) : 0.27 REMARK 3 ESD FROM SIGMAA (A) : 0.35 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) : 0.34 REMARK 3 ESD FROM C-V SIGMAA (A) : 0.51 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.008 REMARK 3 BOND ANGLES (DEGREES) : 1.60 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.40 REMARK 3 IMPROPER ANGLES (DEGREES) : 1.59 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) : 10.790; 1.500 REMARK 3 MAIN-CHAIN ANGLE (A**2) : 13.120; 2.000 REMARK 3 SIDE-CHAIN BOND (A**2) : 12.100; 2.000 REMARK 3 SIDE-CHAIN ANGLE (A**2) : 14.290; 2.500 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 : PARHCSDX.PRO REMARK 3 PARAMETER FILE 2 : PARAM19X.HEME2 REMARK 3 PARAMETER FILE 3 : PARAM19.SOL REMARK 3 PARAMETER FILE 4 : NULL REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO REMARK 3 TOPOLOGY FILE 2 : TOPH19X.HEME REMARK 3 TOPOLOGY FILE 3 : TOPH19.SOL REMARK 3 TOPOLOGY FILE 4 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1HBR COMPLIES WITH FORMAT V. 3.0, 1-DEC-2006 REMARK 4 REMARK 4 THIS IS THE REMEDIATED VERSION OF THIS PDB ENTRY. REMARK 4 REMEDIATED DATA FILE REVISION 3.101 (2007-05-31) REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB . REMARK 100 THE RCSB ID CODE IS RCSB000227. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : MAR-1994 REMARK 200 TEMPERATURE (KELVIN) : 298.0 REMARK 200 PH : 7.00 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : N REMARK 200 RADIATION SOURCE : NULL 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) : 1.54 REMARK 200 MONOCHROMATOR : GRAPHITE REMARK 200 OPTICS : NO MIRRORS REMARK 200 REMARK 200 DETECTOR TYPE : MULTIWIRE REMARK 200 DETECTOR MANUFACTURER : SDMW REMARK 200 INTENSITY-INTEGRATION SOFTWARE : UCSD REMARK 200 DATA SCALING SOFTWARE : UCSD REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29702 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300 REMARK 200 RESOLUTION RANGE LOW (A) : 10.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1 REMARK 200 DATA REDUNDANCY : 9.600 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 8.10000 REMARK 200 FOR THE DATA SET : 15.5000 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) : 2.50 REMARK 200 COMPLETENESS FOR SHELL (%) : 97.7 REMARK 200 DATA REDUNDANCY IN SHELL : 3.60 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 23.90000 REMARK 200 FOR SHELL : 2.300 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 1HHO REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 52.70 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.0 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,1/2+Y,-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 40.25500 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT REMARK 300 WHICH CONSISTS OF 4 CHAIN(S). SEE REMARK 350 FOR REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S). REMARK 350 REMARK 350 GENERATING THE BIOMOLECULE 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 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 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 TYR B 145 REMARK 465 HIS B 146 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 LYS A 8 CD CE NZ REMARK 470 GLN A 11 CG CD OE1 NE2 REMARK 470 GLU A 15 CG CD OE1 OE2 REMARK 470 SER A 19 OG REMARK 470 ARG A 56 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 60 CB CG CD CE NZ REMARK 470 LYS A 71 CD CE NZ REMARK 470 GLN A 78 CB CG CD OE1 NE2 REMARK 470 GLU A 82 CG CD OE1 OE2 REMARK 470 TYR A 89 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LYS A 115 CG CD CE NZ REMARK 470 ARG A 141 CG CD NE CZ NH1 NH2 REMARK 470 HIS B 2 ND1 CD2 CE1 NE2 REMARK 470 GLN B 9 CB CG CD OE1 NE2 REMARK 470 LYS B 76 CD CE NZ REMARK 470 ASN B 77 CG OD1 ND2 REMARK 470 LYS B 82 CG CD CE NZ REMARK 470 GLN B 87 CG CD OE1 NE2 REMARK 470 ARG B 143 CG CD NE CZ NH1 NH2 REMARK 470 LYS B 144 CA C O CB CG CD CE REMARK 470 LYS B 144 NZ REMARK 470 MET C 1 SD CE REMARK 470 LYS C 8 CG CD CE NZ REMARK 470 ARG C 56 NE CZ NH1 NH2 REMARK 470 LYS C 71 CG CD CE NZ REMARK 470 GLN C 78 CG CD OE1 NE2 REMARK 470 GLU C 82 CG CD OE1 OE2 REMARK 470 LYS C 115 CG CD CE NZ REMARK 470 GLU C 138 CB CG CD OE1 OE2 REMARK 470 ARG C 141 CA C O CB CG CD NE REMARK 470 ARG C 141 CZ NH1 NH2 REMARK 470 ASN D 77 CG OD1 ND2 REMARK 470 LYS D 82 CG CD CE NZ REMARK 470 GLN D 87 CG CD OE1 NE2 REMARK 470 LYS D 95 CG CD CE NZ REMARK 470 ARG D 143 CG CD NE CZ NH1 NH2 REMARK 470 LYS D 144 CG CD CE NZ REMARK 470 TYR D 145 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 HIS D 146 CG ND1 CD2 CE1 NE2 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 REMARK 500 O HOH A 143 O HOH A 144 1.24 REMARK 500 O HOH B 148 O HOH B 149 1.25 REMARK 500 O HOH D 148 O HOH D 149 1.25 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS 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,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3) REMARK 500 REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 ARG B 143 C LYS B 144 N -0.099 REMARK 500 GLU C 5 CB GLU C 5 CG 0.078 REMARK 500 MET C 80 SD MET C 80 CE 0.052 REMARK 500 TYR C 140 CB TYR C 140 CG -0.048 REMARK 500 TYR C 140 C ARG C 141 N -0.099 REMARK 500 HIS D 2 N HIS D 2 CA -0.063 REMARK 500 LYS D 144 N LYS D 144 CA 0.076 REMARK 500 LYS D 144 C LYS D 144 O 0.051 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: ENGH AND HUBER, 1991 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 ASP A 47 N - CA - C ANGL. DEV. =-13.3 DEGREES REMARK 500 ASN A 75 N - CA - C ANGL. DEV. = -8.3 DEGREES REMARK 500 TYR A 117 N - CA - C ANGL. DEV. = -8.0 DEGREES REMARK 500 TYR A 140 N - CA - C ANGL. DEV. = 9.4 DEGREES REMARK 500 ARG A 141 N - CA - C ANGL. DEV. =-10.1 DEGREES REMARK 500 VAL B 1 CB - CA - C ANGL. DEV. = 8.1 DEGREES REMARK 500 LEU B 96 N - CA - C ANGL. DEV. = 9.1 DEGREES REMARK 500 ASP C 47 N - CA - C ANGL. DEV. =-12.2 DEGREES REMARK 500 TYR C 117 N - CA - C ANGL. DEV. = -8.0 DEGREES REMARK 500 TYR C 140 CB - CA - C ANGL. DEV. = -8.3 DEGREES REMARK 500 VAL D 1 N - CA - C ANGL. DEV. = 12.2 DEGREES REMARK 500 HIS D 2 N - CA - C ANGL. DEV. =-11.0 DEGREES REMARK 500 LEU D 96 N - CA - C ANGL. DEV. = 9.0 DEGREES REMARK 500 LYS D 144 N - CA - C ANGL. DEV. = 10.9 DEGREES REMARK 500 TYR D 145 N - CA - C ANGL. DEV. = -9.2 DEGREES REMARK 500 HIS D 146 N - CA - C ANGL. DEV. = -8.8 DEGREES REMARK 500 HIS D 146 C - N - CA ANGL. DEV. = 8.4 DEGREES 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 M RES CSSEQI PSI PHI REMARK 500 TYR C 140 -85.95 101.98 REMARK 525 REMARK 525 SOLVENT REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH 53 DISTANCE = 8.76 ANGSTROMS REMARK 525 HOH 113 DISTANCE = 6.33 ANGSTROMS REMARK 525 HOH 117 DISTANCE = 7.42 ANGSTROMS REMARK 525 HOH 120 DISTANCE = 5.81 ANGSTROMS DBREF 1HBR A 1 141 UNP P02001 HBAD_CHICK 1 141 DBREF 1HBR B 1 146 UNP P02112 HBB_CHICK 1 146 DBREF 1HBR C 1 141 UNP P02001 HBAD_CHICK 1 141 DBREF 1HBR D 1 146 UNP P02112 HBB_CHICK 1 146 SEQRES 1 A 141 MET LEU THR ALA GLU ASP LYS LYS LEU ILE GLN GLN ALA SEQRES 2 A 141 TRP GLU LYS ALA ALA SER HIS GLN GLU GLU PHE GLY ALA SEQRES 3 A 141 GLU ALA LEU THR ARG MET PHE THR THR TYR PRO GLN THR SEQRES 4 A 141 LYS THR TYR PHE PRO HIS PHE ASP LEU SER PRO GLY SER SEQRES 5 A 141 ASP GLN VAL ARG GLY HIS GLY LYS LYS VAL LEU GLY ALA SEQRES 6 A 141 LEU GLY ASN ALA VAL LYS ASN VAL ASP ASN LEU SER GLN SEQRES 7 A 141 ALA MET ALA GLU LEU SER ASN LEU HIS ALA TYR ASN LEU SEQRES 8 A 141 ARG VAL ASP PRO VAL ASN PHE LYS LEU LEU SER GLN CYS SEQRES 9 A 141 ILE GLN VAL VAL LEU ALA VAL HIS MET GLY LYS ASP TYR SEQRES 10 A 141 THR PRO GLU VAL HIS ALA ALA PHE ASP LYS PHE LEU SER SEQRES 11 A 141 ALA VAL SER ALA VAL LEU ALA GLU LYS TYR ARG SEQRES 1 B 146 VAL HIS TRP THR ALA GLU GLU LYS GLN LEU ILE THR GLY SEQRES 2 B 146 LEU TRP GLY LYS VAL ASN VAL ALA GLU CYS GLY ALA GLU SEQRES 3 B 146 ALA LEU ALA ARG LEU LEU ILE VAL TYR PRO TRP THR GLN SEQRES 4 B 146 ARG PHE PHE ALA SER PHE GLY ASN LEU SER SER PRO THR SEQRES 5 B 146 ALA ILE LEU GLY ASN PRO MET VAL ARG ALA HIS GLY LYS SEQRES 6 B 146 LYS VAL LEU THR SER PHE GLY ASP ALA VAL LYS ASN LEU SEQRES 7 B 146 ASP ASN ILE LYS ASN THR PHE SER GLN 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 ASP ILE LEU ILE ILE VAL LEU ALA ALA HIS SEQRES 10 B 146 PHE SER LYS ASP PHE THR PRO GLU CYS GLN ALA ALA TRP SEQRES 11 B 146 GLN LYS LEU VAL ARG VAL VAL ALA HIS ALA LEU ALA ARG SEQRES 12 B 146 LYS TYR HIS SEQRES 1 C 141 MET LEU THR ALA GLU ASP LYS LYS LEU ILE GLN GLN ALA SEQRES 2 C 141 TRP GLU LYS ALA ALA SER HIS GLN GLU GLU PHE GLY ALA SEQRES 3 C 141 GLU ALA LEU THR ARG MET PHE THR THR TYR PRO GLN THR SEQRES 4 C 141 LYS THR TYR PHE PRO HIS PHE ASP LEU SER PRO GLY SER SEQRES 5 C 141 ASP GLN VAL ARG GLY HIS GLY LYS LYS VAL LEU GLY ALA SEQRES 6 C 141 LEU GLY ASN ALA VAL LYS ASN VAL ASP ASN LEU SER GLN SEQRES 7 C 141 ALA MET ALA GLU LEU SER ASN LEU HIS ALA TYR ASN LEU SEQRES 8 C 141 ARG VAL ASP PRO VAL ASN PHE LYS LEU LEU SER GLN CYS SEQRES 9 C 141 ILE GLN VAL VAL LEU ALA VAL HIS MET GLY LYS ASP TYR SEQRES 10 C 141 THR PRO GLU VAL HIS ALA ALA PHE ASP LYS PHE LEU SER SEQRES 11 C 141 ALA VAL SER ALA VAL LEU ALA GLU LYS TYR ARG SEQRES 1 D 146 VAL HIS TRP THR ALA GLU GLU LYS GLN LEU ILE THR GLY SEQRES 2 D 146 LEU TRP GLY LYS VAL ASN VAL ALA GLU CYS GLY ALA GLU SEQRES 3 D 146 ALA LEU ALA ARG LEU LEU ILE VAL TYR PRO TRP THR GLN SEQRES 4 D 146 ARG PHE PHE ALA SER PHE GLY ASN LEU SER SER PRO THR SEQRES 5 D 146 ALA ILE LEU GLY ASN PRO MET VAL ARG ALA HIS GLY LYS SEQRES 6 D 146 LYS VAL LEU THR SER PHE GLY ASP ALA VAL LYS ASN LEU SEQRES 7 D 146 ASP ASN ILE LYS ASN THR PHE SER GLN 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 ASP ILE LEU ILE ILE VAL LEU ALA ALA HIS SEQRES 10 D 146 PHE SER LYS ASP PHE THR PRO GLU CYS GLN ALA ALA TRP SEQRES 11 D 146 GLN LYS LEU VAL ARG VAL VAL ALA HIS ALA LEU ALA ARG 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 *147(H2 O) HELIX 1 1 GLU A 5 SER A 19 1 15 HELIX 2 2 GLN A 21 THR A 35 1 15 HELIX 3 3 PRO A 37 TYR A 42 5 6 HELIX 4 4 ASP A 53 LYS A 71 1 19 HELIX 5 5 LEU A 76 ALA A 79 1 4 HELIX 6 6 ALA A 81 ALA A 88 1 8 HELIX 7 7 PRO A 95 ASP A 116 5 22 HELIX 8 8 PRO A 119 LEU A 136 1 18 HELIX 9 9 ALA B 5 LYS B 17 1 13 HELIX 10 10 VAL B 20 VAL B 34 1 15 HELIX 11 11 PRO B 36 PHE B 45 5 10 HELIX 12 12 PRO B 51 GLY B 56 1 6 HELIX 13 13 PRO B 58 VAL B 75 1 18 HELIX 14 14 ILE B 81 CYS B 93 1 13 HELIX 15 15 PRO B 100 ASP B 121 1 22 HELIX 16 16 PRO B 124 LEU B 141 1 18 HELIX 17 17 ALA C 4 SER C 19 1 16 HELIX 18 18 GLN C 21 THR C 35 1 15 HELIX 19 19 PRO C 37 TYR C 42 5 6 HELIX 20 20 ASP C 53 LYS C 71 1 19 HELIX 21 21 LEU C 76 ALA C 79 1 4 HELIX 22 22 ALA C 81 ALA C 88 1 8 HELIX 23 23 PRO C 95 ASP C 116 5 22 HELIX 24 24 PRO C 119 ALA C 137 1 19 HELIX 25 25 ALA D 5 LYS D 17 1 13 HELIX 26 26 VAL D 20 VAL D 34 1 15 HELIX 27 27 PRO D 36 PHE D 45 5 10 HELIX 28 28 PRO D 51 GLY D 56 1 6 HELIX 29 29 PRO D 58 VAL D 75 1 18 HELIX 30 30 LEU D 78 THR D 84 5 7 HELIX 31 31 SER D 86 CYS D 93 1 8 HELIX 32 32 PRO D 100 ASP D 121 1 22 HELIX 33 33 PRO D 124 ARG D 143 1 20 LINK FE HEM A 142 O HOH A 143 LINK FE HEM C 142 O HOH C 145 LINK FE HEM B 147 O HOH B 148 LINK FE HEM D 147 O HOH D 148 LINK FE HEM D 147 NE2 HIS D 92 LINK FE HEM B 147 NE2 HIS B 92 LINK FE HEM C 142 NE2 HIS C 87 LINK FE HEM A 142 NE2 HIS A 87 CRYST1 53.960 80.510 82.110 90.00 104.50 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 0.018532 0.000000 0.004793 0.00000 SCALE2 0.000000 0.012421 0.000000 0.00000 SCALE3 0.000000 0.000000 0.012579 0.00000 MTRIX1 1 0.883125 -0.046056 0.466871 -6.74100 1 MTRIX2 1 -0.046909 -0.998851 -0.009803 1.13000 1 MTRIX3 1 0.466786 -0.013243 -0.884271 27.20400 1