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HEADER OXYGEN STORAGE/TRANSPORT 01-AUG-00 1FHJ TITLE CRYSTAL STRUCTURE OF AQUOMET HEMOGLOBIN-I OF THE MANED WOLF TITLE 2 (CHRYSOCYON BRACHYURUS) AT 2.0 RESOLUTION. COMPND MOL_ID: 1; COMPND 2 MOLECULE: HEMOGLOBIN (ALPHA CHAIN); COMPND 3 CHAIN: A, C; COMPND 4 MOL_ID: 2; COMPND 5 MOLECULE: HEMOGLOBIN (BETA CHAIN); COMPND 6 CHAIN: B, D SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: CHRYSOCYON BRACHYURUS; SOURCE 3 ORGANISM_COMMON: MANED WOLF; SOURCE 4 MOL_ID: 2; SOURCE 5 ORGANISM_SCIENTIFIC: CHRYSOCYON BRACHYURUS; SOURCE 6 ORGANISM_COMMON: MANED WOLF KEYWDS MANED WOLF, HEMOGLOBIN, METAHEMOGLOBIN, X-RAY DIFFRACTION EXPDTA X-RAY DIFFRACTION AUTHOR V.FADEL,W.F.DE AZEVEDO REVDAT 2 13-JAN-04 1FHJ 1 JRNL REVDAT 1 01-AUG-01 1FHJ 0 JRNL AUTH V.FADEL,F.CANDURI,J.R.OLIVIERI,A.L.SMARRA, JRNL AUTH 2 M.F.COLOMBO,G.O.BONILLA-RODRIGUEZ,W.F.DE AZEVEDO JRNL TITL CRYSTAL STRUCTURE OF HEMOGLOBIN FROM THE MANED JRNL TITL 2 WOLF (CHRYSOCYON BRACHYURUS) USING SYNCHROTRON JRNL TITL 3 RADIATION. JRNL REF PROTEIN PEPT.LETT. V. 10 551 2003 JRNL REFN ASTM PPELEN NE ISSN 0929-8665 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH A.L.SMARRA,V.FADEL,M.DELLAMANO,J.R.OLIVIERI, REMARK 1 AUTH 2 W.F.DE AZEVEDO JR.,G.O.BONILLA-RODRIGUEZ REMARK 1 TITL CRYSTALLIZATION, PRELIMINARY X-RAY DIFFRACTION REMARK 1 TITL 2 ANALYSIS AND PATTERSON SEARCH OF OXYHEMOGLOBIN I REMARK 1 TITL 3 FROM THE WOLF (CHRYSOCYON BRACHIURUS) REMARK 1 REF ACTA CRYSTALLOGR., SECT.D V. 55 1618 1999 REMARK 1 REFN ASTM ABCRE6 DK ISSN 0907-4449 REMARK 2 REMARK 2 RESOLUTION. 1.80 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 93.5 REMARK 3 NUMBER OF REFLECTIONS : 50039 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : NULL REMARK 3 FREE R VALUE TEST SET SELECTION : FIXED RANDOMLY FOR X-PLOR REMARK 3 REFINEMENT AND FIXED THE REMARK 3 SAME REFLECTIONS FOR THE REMARK 3 REFMAC REFINEMENT. REMARK 3 R VALUE (WORKING SET) : 0.194 REMARK 3 FREE R VALUE : 0.246 REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : 10 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : NULL REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL REMARK 3 BIN R VALUE (WORKING SET) : NULL REMARK 3 BIN FREE R VALUE : NULL REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 4420 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 172 REMARK 3 SOLVENT ATOMS : 308 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 CROSS-VALIDATED ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL REMARK 3 ESD FROM C-V SIGMAA (A) : NULL REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.013 REMARK 3 BOND ANGLES (DEGREES) : 1.71 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.17 REMARK 3 IMPROPER ANGLES (DEGREES) : 1.93 REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : 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 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 : NULL REMARK 3 TOPOLOGY FILE 1 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REFMAC WAS ALSO USED FOR REFINEMENT. REMARK 3 THE SIMULLATED ANNEALING METHOD (X-PLOR) AND MAXIMUM REMARK 3 LIKELIHOOD METHOD (REFMAC) WAS EMPLOYED. DATA WAS USED TO 1.8 REMARK 3 ANGSTROMS, BUT WITH LOW COMPLETENESS. REMARK 4 REMARK 4 1FHJ 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 3.100 (2007-03-17) REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB . REMARK 100 THE RCSB ID CODE IS RCSB011592. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 27-AUG-1998 REMARK 200 TEMPERATURE (KELVIN) : 300.0 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : LNLS REMARK 200 BEAMLINE : D03B-MX1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.37 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL 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 : 50240 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.864 REMARK 200 RESOLUTION RANGE LOW (A) : 72.548 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 93.1 REMARK 200 DATA REDUNDANCY : 2.620 REMARK 200 R MERGE (I) : 0.05000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 9.4000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.86 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.90 REMARK 200 COMPLETENESS FOR SHELL (%) : 78.7 REMARK 200 DATA REDUNDANCY IN SHELL : 2.38 REMARK 200 R MERGE FOR SHELL (I) : 0.58300 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 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: HUMAN OXYHEMOGLOBIN PDB ID 1HHO REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 51.44 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.53 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 1500 30%, VAPOR DIFFUSION, REMARK 280 TEMPERATURE 295K 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 1/2-X,-Y,1/2+Z REMARK 290 3555 -X,1/2+Y,1/2-Z REMARK 290 4555 1/2+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 27.09200 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 66.72500 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 43.86250 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 66.72500 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.09200 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 43.86250 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 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 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 PRO A 50 C PRO A 50 O 0.086 REMARK 500 THR B 4 CB THR B 4 CG2 0.075 REMARK 500 MET B 55 SD MET B 55 CE -0.143 REMARK 500 GLY C 51 C GLY C 51 O -0.072 REMARK 500 LYS D 120 CB LYS D 120 CG 0.077 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 LEU A 2 CA - C - N ANGL. DEV. =-11.0 DEGREES REMARK 500 ASP A 47 N - CA - C ANGL. DEV. =-16.0 DEGREES REMARK 500 PRO A 50 CB - CA - C ANGL. DEV. = 14.1 DEGREES REMARK 500 PRO A 50 CA - C - N ANGL. DEV. = 15.7 DEGREES REMARK 500 GLY A 51 CA - C - N ANGL. DEV. = 12.0 DEGREES REMARK 500 SER B 49 N - CA - C ANGL. DEV. = 11.6 DEGREES REMARK 500 ASP C 47 N - CA - C ANGL. DEV. =-15.0 DEGREES REMARK 500 PRO C 50 CA - C - N ANGL. DEV. = 10.9 DEGREES REMARK 500 ASP D 79 N - CA - C ANGL. DEV. = 10.2 DEGREES 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 41 DISTANCE = 6.60 ANGSTROMS REMARK 525 HOH 66 DISTANCE = 9.32 ANGSTROMS REMARK 525 HOH 71 DISTANCE = 5.84 ANGSTROMS REMARK 525 HOH 85 DISTANCE = 6.30 ANGSTROMS REMARK 525 HOH 88 DISTANCE = 6.91 ANGSTROMS REMARK 525 HOH 90 DISTANCE = 9.40 ANGSTROMS REMARK 525 HOH 91 DISTANCE = 5.12 ANGSTROMS REMARK 525 HOH 93 DISTANCE = 8.01 ANGSTROMS REMARK 525 HOH 95 DISTANCE = 8.74 ANGSTROMS REMARK 525 HOH 102 DISTANCE = 5.02 ANGSTROMS REMARK 525 HOH 108 DISTANCE = 11.99 ANGSTROMS REMARK 525 HOH 111 DISTANCE = 8.37 ANGSTROMS REMARK 525 HOH 112 DISTANCE = 11.38 ANGSTROMS REMARK 525 HOH 118 DISTANCE = 12.83 ANGSTROMS REMARK 525 HOH 119 DISTANCE = 8.72 ANGSTROMS REMARK 525 HOH 120 DISTANCE = 7.52 ANGSTROMS REMARK 525 HOH 124 DISTANCE = 7.95 ANGSTROMS REMARK 525 HOH 127 DISTANCE = 8.94 ANGSTROMS REMARK 525 HOH 131 DISTANCE = 6.98 ANGSTROMS REMARK 525 HOH 144 DISTANCE = 8.46 ANGSTROMS REMARK 525 HOH 145 DISTANCE = 7.54 ANGSTROMS REMARK 525 HOH 153 DISTANCE = 10.15 ANGSTROMS REMARK 525 HOH 156 DISTANCE = 7.14 ANGSTROMS REMARK 525 HOH 159 DISTANCE = 5.07 ANGSTROMS REMARK 525 HOH 186 DISTANCE = 5.79 ANGSTROMS REMARK 525 HOH 190 DISTANCE = 6.83 ANGSTROMS REMARK 525 HOH 191 DISTANCE = 7.45 ANGSTROMS REMARK 525 HOH 197 DISTANCE = 5.00 ANGSTROMS REMARK 525 HOH 202 DISTANCE = 5.60 ANGSTROMS REMARK 525 HOH 207 DISTANCE = 5.20 ANGSTROMS REMARK 525 HOH 208 DISTANCE = 8.28 ANGSTROMS REMARK 525 HOH 214 DISTANCE = 5.74 ANGSTROMS REMARK 525 HOH 216 DISTANCE = 5.63 ANGSTROMS REMARK 525 HOH 217 DISTANCE = 5.46 ANGSTROMS REMARK 525 HOH 219 DISTANCE = 8.91 ANGSTROMS REMARK 525 HOH 220 DISTANCE = 5.13 ANGSTROMS REMARK 525 HOH 222 DISTANCE = 5.79 ANGSTROMS REMARK 525 HOH 223 DISTANCE = 5.60 ANGSTROMS REMARK 525 HOH 227 DISTANCE = 5.67 ANGSTROMS REMARK 525 HOH 234 DISTANCE = 5.44 ANGSTROMS REMARK 525 HOH 235 DISTANCE = 10.51 ANGSTROMS REMARK 525 HOH 237 DISTANCE = 6.60 ANGSTROMS REMARK 525 HOH 238 DISTANCE = 8.11 ANGSTROMS REMARK 525 HOH 239 DISTANCE = 6.61 ANGSTROMS REMARK 525 HOH 241 DISTANCE = 5.03 ANGSTROMS REMARK 525 HOH 246 DISTANCE = 5.25 ANGSTROMS REMARK 525 HOH 250 DISTANCE = 6.73 ANGSTROMS REMARK 525 HOH 253 DISTANCE = 7.31 ANGSTROMS REMARK 525 HOH 254 DISTANCE = 8.67 ANGSTROMS REMARK 525 HOH 257 DISTANCE = 8.58 ANGSTROMS REMARK 525 HOH 258 DISTANCE = 7.90 ANGSTROMS REMARK 525 HOH 259 DISTANCE = 5.49 ANGSTROMS REMARK 525 HOH 261 DISTANCE = 6.23 ANGSTROMS REMARK 525 HOH 262 DISTANCE = 5.31 ANGSTROMS REMARK 525 HOH 263 DISTANCE = 6.41 ANGSTROMS REMARK 525 HOH 264 DISTANCE = 6.23 ANGSTROMS REMARK 525 HOH 267 DISTANCE = 5.36 ANGSTROMS REMARK 525 HOH 268 DISTANCE = 9.63 ANGSTROMS REMARK 525 HOH 274 DISTANCE = 7.65 ANGSTROMS REMARK 525 HOH 276 DISTANCE = 5.29 ANGSTROMS REMARK 525 HOH 277 DISTANCE = 11.30 ANGSTROMS REMARK 525 HOH 281 DISTANCE = 5.14 ANGSTROMS REMARK 525 HOH 284 DISTANCE = 5.62 ANGSTROMS REMARK 525 HOH 285 DISTANCE = 5.30 ANGSTROMS REMARK 525 HOH 286 DISTANCE = 5.51 ANGSTROMS REMARK 525 HOH 293 DISTANCE = 5.89 ANGSTROMS REMARK 525 HOH 294 DISTANCE = 5.11 ANGSTROMS REMARK 525 HOH 295 DISTANCE = 5.15 ANGSTROMS REMARK 525 HOH 297 DISTANCE = 5.86 ANGSTROMS REMARK 525 HOH 298 DISTANCE = 5.50 ANGSTROMS REMARK 525 HOH 299 DISTANCE = 5.41 ANGSTROMS REMARK 525 HOH 300 DISTANCE = 9.74 ANGSTROMS REMARK 525 HOH 301 DISTANCE = 8.49 ANGSTROMS REMARK 525 HOH 304 DISTANCE = 5.86 ANGSTROMS REMARK 525 HOH 305 DISTANCE = 5.51 ANGSTROMS REMARK 525 HOH 306 DISTANCE = 6.29 ANGSTROMS REMARK 525 HOH 307 DISTANCE = 6.31 ANGSTROMS DBREF 1FHJ A 1 141 UNP P01952 HBA_CANFAX 1 141 DBREF 1FHJ B 1 146 UNP P02056 HBB_CANFAX 1 146 DBREF 1FHJ C 1 141 UNP P01952 HBA_CANFAX 1 141 DBREF 1FHJ D 1 146 UNP P02056 HBB_CANFAX 1 146 SEQADV 1FHJ THR A 130 UNP P01952 ALA 130 SEE REMARK 999 SEQADV 1FHJ THR C 130 UNP P01952 ALA 130 SEE REMARK 999 SEQRES 1 A 141 VAL LEU SER PRO ALA ASP LYS THR ASN ILE LYS SER THR SEQRES 2 A 141 TRP ASP LYS ILE GLY GLY HIS ALA GLY ASP TYR GLY GLY SEQRES 3 A 141 GLU ALA LEU ASP ARG THR PHE GLN SER PHE PRO THR THR SEQRES 4 A 141 LYS THR TYR PHE PRO HIS PHE ASP LEU SER PRO GLY SER SEQRES 5 A 141 ALA GLN VAL LYS ALA HIS GLY LYS LYS VAL ALA ASP ALA SEQRES 6 A 141 LEU THR THR ALA VAL ALA HIS LEU ASP ASP LEU PRO GLY SEQRES 7 A 141 ALA LEU SER ALA LEU SER ASP LEU HIS ALA TYR 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 CYS HIS HIS PRO THR GLU PHE SEQRES 10 A 141 THR PRO ALA VAL HIS ALA SER LEU ASP LYS PHE PHE THR SEQRES 11 A 141 ALA VAL SER THR VAL LEU THR SER LYS TYR ARG SEQRES 1 B 146 VAL HIS LEU THR ALA GLU GLU LYS SER LEU VAL SER GLY 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 ILE VAL TYR PRO TRP THR GLN SEQRES 4 B 146 ARG PHE PHE ASP SER PHE GLY ASP LEU SER THR PRO ASP SEQRES 5 B 146 ALA VAL MET SER ASN ALA LYS VAL LYS ALA HIS GLY LYS SEQRES 6 B 146 LYS VAL LEU ASN SER PHE SER ASP GLY LEU LYS ASN LEU SEQRES 7 B 146 ASP ASN LEU LYS GLY THR PHE ALA LYS LEU SER GLU LEU SEQRES 8 B 146 HIS CYS ASP LYS LEU HIS VAL ASP PRO GLU ASN PHE LYS 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 GLN 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 ILE LYS SER THR SEQRES 2 C 141 TRP ASP LYS ILE GLY GLY HIS ALA GLY ASP TYR GLY GLY SEQRES 3 C 141 GLU ALA LEU ASP ARG THR PHE GLN SER PHE PRO THR THR SEQRES 4 C 141 LYS THR TYR PHE PRO HIS PHE ASP LEU SER PRO GLY SER SEQRES 5 C 141 ALA GLN VAL LYS ALA HIS GLY LYS LYS VAL ALA ASP ALA SEQRES 6 C 141 LEU THR THR ALA VAL ALA HIS LEU ASP ASP LEU PRO GLY SEQRES 7 C 141 ALA LEU SER ALA LEU SER ASP LEU HIS ALA TYR 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 CYS HIS HIS PRO THR GLU PHE SEQRES 10 C 141 THR PRO ALA VAL HIS ALA SER LEU ASP LYS PHE PHE THR SEQRES 11 C 141 ALA VAL SER THR VAL LEU THR SER LYS TYR ARG SEQRES 1 D 146 VAL HIS LEU THR ALA GLU GLU LYS SER LEU VAL SER GLY 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 ILE VAL TYR PRO TRP THR GLN SEQRES 4 D 146 ARG PHE PHE ASP SER PHE GLY ASP LEU SER THR PRO ASP SEQRES 5 D 146 ALA VAL MET SER ASN ALA LYS VAL LYS ALA HIS GLY LYS SEQRES 6 D 146 LYS VAL LEU ASN SER PHE SER ASP GLY LEU LYS ASN LEU SEQRES 7 D 146 ASP ASN LEU LYS GLY THR PHE ALA LYS LEU SER GLU LEU SEQRES 8 D 146 HIS CYS ASP LYS LEU HIS VAL ASP PRO GLU ASN PHE LYS 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 GLN 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 *308(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 SER A 81 1 7 HELIX 6 6 LEU A 80 LYS A 90 1 11 HELIX 7 7 PRO A 95 HIS A 113 1 19 HELIX 8 8 THR A 118 THR A 137 1 20 HELIX 9 9 THR B 4 GLY B 16 1 13 HELIX 10 10 ASN B 19 TYR B 35 1 17 HELIX 11 11 PRO B 36 ASP B 43 5 8 HELIX 12 12 PHE B 42 GLY B 46 5 5 HELIX 13 13 THR B 50 ASN B 57 1 8 HELIX 14 14 ASN B 57 ASN B 77 1 21 HELIX 15 15 ASN B 80 PHE B 85 1 6 HELIX 16 16 PHE B 85 LYS B 95 1 11 HELIX 17 17 PRO B 100 GLY B 119 1 20 HELIX 18 18 LYS B 120 PHE B 122 5 3 HELIX 19 19 THR B 123 ALA B 142 1 20 HELIX 20 20 HIS B 143 HIS B 146 5 4 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 HIS C 72 1 21 HELIX 25 25 ASP C 75 SER C 81 1 7 HELIX 26 26 LEU C 80 LYS C 90 1 11 HELIX 27 27 PRO C 95 HIS C 113 1 19 HELIX 28 28 THR C 118 SER C 138 1 21 HELIX 29 29 LYS C 139 ARG C 141 5 3 HELIX 30 30 THR D 4 GLY D 16 1 13 HELIX 31 31 ASN D 19 TYR D 35 1 17 HELIX 32 32 PRO D 36 ASP D 43 5 8 HELIX 33 33 PHE D 42 GLY D 46 5 5 HELIX 34 34 THR D 50 ASN D 57 1 8 HELIX 35 35 ASN D 57 ASN D 77 1 21 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 HELIX 41 41 HIS D 143 HIS D 146 5 4 LINK NE2 HIS A 87 FE HEM A 142 LINK NE2 HIS B 92 FE HEM B 147 LINK NE2 HIS C 87 FE HEM C 142 LINK NE2 HIS D 92 FE HEM D 147 CRYST1 54.184 87.725 133.450 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 0.018460 0.000000 0.000000 0.00000 SCALE2 0.000000 0.011400 0.000000 0.00000 SCALE3 0.000000 0.000000 0.007490 0.00000