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HEADER OXYGEN TRANSPORT 30-MAY-99 1QPW TITLE CRYSTAL STRUCTURE DETERMINATION OF PORCINE HEMOGLOBIN AT TITLE 2 1.8A RESOLUTION COMPND MOL_ID: 1; COMPND 2 MOLECULE: PORICINE HEMOGLOBIN (ALPHA SUBUNIT); COMPND 3 CHAIN: A, C; COMPND 4 MOL_ID: 2; COMPND 5 MOLECULE: PORICINE HEMOGLOBIN (BETA SUBUNIT); COMPND 6 CHAIN: B, D SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SUS SCROFA; SOURCE 3 ORGANISM_COMMON: PIG; SOURCE 4 OTHER_DETAILS: TAIWANESE PIG FROM SLAUGHTERHOUSE; SOURCE 5 MOL_ID: 2; SOURCE 6 ORGANISM_SCIENTIFIC: SUS SCROFA; SOURCE 7 ORGANISM_COMMON: PIG; SOURCE 8 OTHER_DETAILS: TAIWANESE PIG FROM SLAUGHTERHOUSE KEYWDS X-RAY STUDY, PORCINE HEMOGLOBIN, ARTIFICIAL HUMAN BLOOD, KEYWDS 2 OXYGEN TRANSPORT EXPDTA X-RAY DIFFRACTION AUTHOR T.-H.LU,K.PANNEERSELVAM,Y.-C.LIAW,P.KAN,C.-J.LEE REVDAT 3 01-APR-03 1QPW 1 JRNL REVDAT 2 06-MAR-00 1QPW 1 JRNL REVDAT 1 04-JUN-99 1QPW 0 JRNL AUTH T.H.LU,K.PANNEERSELVAM,Y.C.LIAW,P.KAN,C.J.LEE JRNL TITL STRUCTURE DETERMINATION OF PORCINE HAEMOGLOBIN. JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 56 304 2000 JRNL REFN ASTM ABCRE6 DK ISSN 0907-4449 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH D.S.KATZ,S.P.WHITE,W.HUANG,R.KUMAR,D.W.CHRISTIANSON REMARK 1 TITL STRUCTURE DETERMINATION OF AQUOMET PORCINE REMARK 1 TITL 2 HEMOGLOBIN AT 2.8A RESOLUTION REMARK 1 REF J.MOL.BIOL. V. 244 541 1994 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 REMARK 2 REMARK 2 RESOLUTION. 1.80 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.1 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) : 8.00 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) (%) : 98.2 REMARK 3 NUMBER OF REFLECTIONS : 36820 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : NULL REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM SELECTION OF 10% OF REMARK 3 THE OBSERVED REFLECTIONS REMARK 3 R VALUE (WORKING SET) : 0.207 REMARK 3 FREE R VALUE : 0.251 REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : 3682 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 : 4398 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 176 REMARK 3 SOLVENT ATOMS : 574 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) : 0.017 REMARK 3 BOND ANGLES (DEGREES) : 3.00 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 20.60 REMARK 3 IMPROPER ANGLES (DEGREES) : 1.80 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: NULL REMARK 4 REMARK 4 1QPW 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 RCSB009125. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 10-AUG-1991 REMARK 200 TEMPERATURE (KELVIN) : 293.0 REMARK 200 PH : 6.80 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 RU300 REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : R-AXIS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36820 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800 REMARK 200 RESOLUTION RANGE LOW (A) : 8.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 78.0 REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : 0.05800 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 1.0000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 8.00 REMARK 200 COMPLETENESS FOR SHELL (%) : 78.0 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.05800 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: NULL REMARK 200 SOFTWARE USED: X-PLOR REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 45.80 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 2.8M OF PHOSPHATE SOLUTION, PH 6.8, REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 296K 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 34.05000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 57.42500 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.13500 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 57.42500 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 34.05000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 36.13500 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 HIS C 87 NE2 HIS C 87 CD2 -0.138 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 6 DISTANCE = 6.24 ANGSTROMS REMARK 525 HOH 35 DISTANCE = 5.57 ANGSTROMS REMARK 525 HOH 66 DISTANCE = 6.02 ANGSTROMS REMARK 525 HOH 67 DISTANCE = 5.51 ANGSTROMS REMARK 525 HOH 88 DISTANCE = 5.95 ANGSTROMS REMARK 525 HOH 93 DISTANCE = 5.37 ANGSTROMS REMARK 525 HOH 104 DISTANCE = 5.22 ANGSTROMS REMARK 525 HOH 119 DISTANCE = 6.78 ANGSTROMS REMARK 525 HOH 120 DISTANCE = 5.80 ANGSTROMS REMARK 525 HOH 137 DISTANCE = 8.30 ANGSTROMS REMARK 525 HOH 139 DISTANCE = 5.37 ANGSTROMS REMARK 525 HOH 148 DISTANCE = 7.94 ANGSTROMS REMARK 525 HOH 168 DISTANCE = 7.11 ANGSTROMS REMARK 525 HOH 171 DISTANCE = 10.88 ANGSTROMS REMARK 525 HOH 203 DISTANCE = 5.02 ANGSTROMS REMARK 525 HOH 228 DISTANCE = 5.13 ANGSTROMS REMARK 525 HOH 238 DISTANCE = 5.17 ANGSTROMS REMARK 525 HOH 242 DISTANCE = 7.96 ANGSTROMS REMARK 525 HOH 245 DISTANCE = 7.52 ANGSTROMS REMARK 525 HOH 246 DISTANCE = 6.14 ANGSTROMS REMARK 525 HOH 249 DISTANCE = 7.92 ANGSTROMS REMARK 525 HOH 256 DISTANCE = 5.02 ANGSTROMS REMARK 525 HOH 264 DISTANCE = 9.26 ANGSTROMS REMARK 525 HOH 265 DISTANCE = 6.76 ANGSTROMS REMARK 525 HOH 286 DISTANCE = 8.03 ANGSTROMS REMARK 525 HOH 291 DISTANCE = 10.20 ANGSTROMS REMARK 525 HOH 292 DISTANCE = 7.36 ANGSTROMS REMARK 525 HOH 296 DISTANCE = 5.67 ANGSTROMS REMARK 525 HOH 299 DISTANCE = 5.65 ANGSTROMS REMARK 525 HOH 301 DISTANCE = 6.92 ANGSTROMS REMARK 525 HOH 304 DISTANCE = 6.18 ANGSTROMS REMARK 525 HOH 308 DISTANCE = 7.41 ANGSTROMS REMARK 525 HOH 310 DISTANCE = 10.47 ANGSTROMS REMARK 525 HOH 321 DISTANCE = 5.35 ANGSTROMS REMARK 525 HOH 327 DISTANCE = 7.86 ANGSTROMS REMARK 525 HOH 330 DISTANCE = 5.78 ANGSTROMS REMARK 525 HOH 331 DISTANCE = 7.73 ANGSTROMS REMARK 525 HOH 341 DISTANCE = 5.38 ANGSTROMS REMARK 525 HOH 343 DISTANCE = 5.98 ANGSTROMS REMARK 525 HOH 349 DISTANCE = 6.14 ANGSTROMS REMARK 525 HOH 362 DISTANCE = 6.39 ANGSTROMS REMARK 525 HOH 364 DISTANCE = 11.36 ANGSTROMS REMARK 525 HOH 368 DISTANCE = 8.25 ANGSTROMS REMARK 525 HOH 372 DISTANCE = 6.06 ANGSTROMS REMARK 525 HOH 373 DISTANCE = 7.34 ANGSTROMS REMARK 525 HOH 376 DISTANCE = 6.89 ANGSTROMS REMARK 525 HOH 379 DISTANCE = 8.14 ANGSTROMS REMARK 525 HOH 380 DISTANCE = 6.09 ANGSTROMS REMARK 525 HOH 382 DISTANCE = 5.98 ANGSTROMS REMARK 525 HOH 386 DISTANCE = 7.30 ANGSTROMS REMARK 525 HOH 389 DISTANCE = 7.43 ANGSTROMS REMARK 525 HOH 391 DISTANCE = 7.14 ANGSTROMS REMARK 525 HOH 392 DISTANCE = 8.05 ANGSTROMS REMARK 525 HOH 395 DISTANCE = 7.65 ANGSTROMS REMARK 525 HOH 402 DISTANCE = 10.79 ANGSTROMS REMARK 525 HOH 409 DISTANCE = 7.18 ANGSTROMS REMARK 525 HOH 412 DISTANCE = 9.90 ANGSTROMS REMARK 525 HOH 424 DISTANCE = 5.90 ANGSTROMS REMARK 525 HOH 427 DISTANCE = 7.14 ANGSTROMS REMARK 525 HOH 429 DISTANCE = 8.44 ANGSTROMS REMARK 525 HOH 437 DISTANCE = 5.96 ANGSTROMS REMARK 525 HOH 441 DISTANCE = 7.26 ANGSTROMS REMARK 525 HOH 444 DISTANCE = 7.83 ANGSTROMS REMARK 525 HOH 445 DISTANCE = 10.97 ANGSTROMS REMARK 525 HOH 450 DISTANCE = 8.66 ANGSTROMS REMARK 525 HOH 460 DISTANCE = 10.70 ANGSTROMS REMARK 525 HOH 469 DISTANCE = 11.00 ANGSTROMS REMARK 525 HOH 473 DISTANCE = 6.40 ANGSTROMS REMARK 525 HOH 474 DISTANCE = 7.51 ANGSTROMS REMARK 525 HOH 475 DISTANCE = 7.21 ANGSTROMS REMARK 525 HOH 481 DISTANCE = 5.25 ANGSTROMS REMARK 525 HOH 490 DISTANCE = 8.46 ANGSTROMS REMARK 525 HOH 492 DISTANCE = 6.38 ANGSTROMS REMARK 525 HOH 493 DISTANCE = 7.55 ANGSTROMS REMARK 525 HOH 496 DISTANCE = 9.50 ANGSTROMS REMARK 525 HOH 497 DISTANCE = 6.60 ANGSTROMS REMARK 525 HOH 521 DISTANCE = 8.77 ANGSTROMS REMARK 525 HOH 522 DISTANCE = 5.62 ANGSTROMS REMARK 525 HOH 523 DISTANCE = 6.04 ANGSTROMS REMARK 525 HOH 525 DISTANCE = 6.06 ANGSTROMS REMARK 525 HOH 529 DISTANCE = 9.15 ANGSTROMS REMARK 525 HOH 530 DISTANCE = 6.93 ANGSTROMS REMARK 525 HOH 532 DISTANCE = 8.02 ANGSTROMS REMARK 525 HOH 538 DISTANCE = 6.26 ANGSTROMS REMARK 525 HOH 540 DISTANCE = 7.04 ANGSTROMS REMARK 525 HOH 549 DISTANCE = 9.84 ANGSTROMS REMARK 525 HOH 553 DISTANCE = 8.88 ANGSTROMS REMARK 525 HOH 557 DISTANCE = 6.50 ANGSTROMS REMARK 525 HOH 558 DISTANCE = 9.48 ANGSTROMS REMARK 525 HOH 561 DISTANCE = 5.67 ANGSTROMS REMARK 525 HOH 562 DISTANCE = 6.44 ANGSTROMS REMARK 525 HOH 564 DISTANCE = 7.33 ANGSTROMS REMARK 525 HOH 566 DISTANCE = 5.92 ANGSTROMS REMARK 525 HOH 572 DISTANCE = 8.95 ANGSTROMS DBREF 1QPW A 1 141 UNP P01965 HBA_PIG 1 141 DBREF 1QPW B 1 146 UNP P02067 HBB_PIG 1 146 DBREF 1QPW C 1 141 UNP P01965 HBA_PIG 1 141 DBREF 1QPW D 1 146 UNP P02067 HBB_PIG 1 146 SEQADV 1QPW ASP B 125 UNP P01965 ASN 125 CONFLICT SEQADV 1QPW ASP D 125 UNP P02067 ASN 125 CONFLICT SEQRES 1 A 141 VAL LEU SER ALA ALA ASP LYS ALA ASN VAL LYS ALA ALA SEQRES 2 A 141 TRP GLY LYS VAL GLY GLY GLN ALA GLY ALA HIS GLY ALA SEQRES 3 A 141 GLU ALA LEU GLU ARG MET PHE LEU GLY PHE PRO THR THR SEQRES 4 A 141 LYS THR TYR PHE PRO HIS PHE ASN LEU SER HIS GLY SER SEQRES 5 A 141 ASP GLN VAL LYS ALA HIS GLY GLN LYS VAL ALA ASP ALA SEQRES 6 A 141 LEU THR LYS ALA VAL GLY HIS LEU ASP ASP LEU PRO GLY 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 HIS PRO ASP ASP PHE SEQRES 10 A 141 ASN PRO SER VAL HIS ALA SER LEU ASP LYS PHE LEU ALA SEQRES 11 A 141 ASN VAL SER THR VAL LEU THR SER LYS TYR ARG SEQRES 1 B 146 VAL HIS LEU SER ALA GLU GLU LYS GLU ALA VAL LEU 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 VAL VAL TYR PRO TRP THR GLN SEQRES 4 B 146 ARG PHE PHE GLU SER PHE GLY ASP LEU SER ASN ALA 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 GLN SER PHE SER ASP GLY LEU LYS HIS 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 GLN LEU HIS VAL ASP PRO GLU ASN PHE ARG SEQRES 9 B 146 LEU LEU GLY ASN VAL ILE VAL VAL VAL LEU ALA ARG ARG SEQRES 10 B 146 LEU GLY HIS ASP PHE ASN PRO ASP VAL GLN ALA ALA PHE 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 ALA ALA ASP LYS ALA ASN VAL LYS ALA ALA SEQRES 2 C 141 TRP GLY LYS VAL GLY GLY GLN ALA GLY ALA HIS GLY ALA SEQRES 3 C 141 GLU ALA LEU GLU ARG MET PHE LEU GLY PHE PRO THR THR SEQRES 4 C 141 LYS THR TYR PHE PRO HIS PHE ASN LEU SER HIS GLY SER SEQRES 5 C 141 ASP GLN VAL LYS ALA HIS GLY GLN LYS VAL ALA ASP ALA SEQRES 6 C 141 LEU THR LYS ALA VAL GLY HIS LEU ASP ASP LEU PRO GLY 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 HIS PRO ASP ASP PHE SEQRES 10 C 141 ASN PRO SER VAL HIS ALA SER LEU ASP LYS PHE LEU ALA SEQRES 11 C 141 ASN VAL SER THR VAL LEU THR SER LYS TYR ARG SEQRES 1 D 146 VAL HIS LEU SER ALA GLU GLU LYS GLU ALA VAL LEU 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 VAL VAL TYR PRO TRP THR GLN SEQRES 4 D 146 ARG PHE PHE GLU SER PHE GLY ASP LEU SER ASN ALA 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 GLN SER PHE SER ASP GLY LEU LYS HIS 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 GLN LEU HIS VAL ASP PRO GLU ASN PHE ARG SEQRES 9 D 146 LEU LEU GLY ASN VAL ILE VAL VAL VAL LEU ALA ARG ARG SEQRES 10 D 146 LEU GLY HIS ASP PHE ASN PRO ASP VAL GLN ALA ALA PHE 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 650 43 HET HEM 750 43 HET OXY 751 2 HET HEM 850 43 HET OXY 851 2 HET HEM 950 43 HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE HETNAM OXY OXYGEN MOLECULE HETSYN HEM HEME FORMUL 5 HEM 4(C34 H32 FE N4 O4) FORMUL 7 OXY 2(O2) FORMUL 11 HOH *574(H2 O) HELIX 1 1 SER A 3 LYS A 16 1 14 HELIX 2 2 VAL A 17 GLY A 19 5 3 HELIX 3 3 GLN A 20 PHE A 36 1 17 HELIX 4 4 THR A 38 PHE A 43 5 6 HELIX 5 5 SER A 52 GLY A 71 1 20 HELIX 6 6 HIS A 72 ASP A 74 5 3 HELIX 7 7 ASP A 75 ALA A 88 1 14 HELIX 8 8 ASP A 94 HIS A 113 1 20 HELIX 9 9 PRO A 114 PHE A 117 5 4 HELIX 10 10 ASN A 118 THR A 137 1 20 HELIX 11 11 SER B 4 GLY B 16 1 13 HELIX 12 12 ASN B 19 TYR B 35 1 17 HELIX 13 13 PRO B 36 GLU B 43 5 8 HELIX 14 14 PHE B 42 GLY B 46 5 5 HELIX 15 15 ASN B 50 MET B 55 1 6 HELIX 16 16 ASN B 57 LEU B 75 1 19 HELIX 17 17 HIS B 77 ASP B 79 5 3 HELIX 18 18 ASN B 80 GLN B 95 1 16 HELIX 19 19 PRO B 100 GLY B 119 1 20 HELIX 20 20 HIS B 120 PHE B 122 5 3 HELIX 21 21 ASN B 123 ALA B 142 1 20 HELIX 22 22 SER C 3 GLY C 18 1 16 HELIX 23 23 GLN C 20 PHE C 36 1 17 HELIX 24 24 PRO C 37 PHE C 43 5 7 HELIX 25 25 SER C 52 HIS C 72 1 21 HELIX 26 26 ASP C 75 LEU C 80 1 6 HELIX 27 27 LEU C 80 HIS C 89 1 10 HELIX 28 28 ASP C 94 HIS C 113 1 20 HELIX 29 29 ASN C 118 SER C 138 1 21 HELIX 30 30 SER D 4 GLY D 16 1 13 HELIX 31 31 ASN D 19 TYR D 35 1 17 HELIX 32 32 PRO D 36 GLU D 43 5 8 HELIX 33 33 PHE D 42 GLY D 46 5 5 HELIX 34 34 ASN D 50 GLY D 56 1 7 HELIX 35 35 ASN D 57 LYS D 76 1 20 HELIX 36 36 HIS D 77 ASP D 79 5 3 HELIX 37 37 ASN D 80 ASP D 94 1 15 HELIX 38 38 PRO D 100 GLY D 119 1 20 HELIX 39 39 HIS D 120 PHE D 122 5 3 HELIX 40 40 ASN D 123 ALA D 142 1 20 LINK FE HEM 650 O HOH 573 LINK FE HEM 750 O1 OXY 751 LINK FE HEM 850 O1 OXY 851 LINK FE HEM 950 O HOH 574 CRYST1 68.100 72.270 114.850 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 0.014684 0.000000 0.000000 0.00000 SCALE2 0.000000 0.013837 0.000000 0.00000 SCALE3 0.000000 0.000000 0.008707 0.00000