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HEADER OXYGEN STORAGE/TRANSPORT 11-OCT-04 1XQ5 TITLE MET-PERCH HEMOGLOBIN AT 1.9A COMPND MOL_ID: 1; COMPND 2 MOLECULE: HEMOGLOBIN ALPHA-1 CHAIN; COMPND 3 CHAIN: A, C; COMPND 4 MOL_ID: 2; COMPND 5 MOLECULE: HEMOGLOBIN BETA-2 CHAIN; COMPND 6 CHAIN: B, D SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: PERCA FLAVESCENS; SOURCE 3 ORGANISM_COMMON: YELLOW PERCH; SOURCE 4 MOL_ID: 2; SOURCE 5 ORGANISM_SCIENTIFIC: PERCA FLAVESCENS; SOURCE 6 ORGANISM_COMMON: YELLOW PERCH KEYWDS FISH HEMOGLOBIN, RAPID OXIDATION, STRUCTURAL GENOMICS, KEYWDS 2 PROTEIN STRUCTURE INITIATIVE, PSI, CESG, CENTER FOR KEYWDS 3 EUKARYOTIC STRUCTURAL GENOMICS EXPDTA X-RAY DIFFRACTION AUTHOR CENTER FOR EUKARYOTIC STRUCTURAL GENOMICS (CESG) REVDAT 2 01-FEB-05 1XQ5 1 KEYWDS REMARK REVDAT 1 16-NOV-04 1XQ5 0 JRNL AUTH CENTER FOR EUKARYOTIC STRUCTURAL GENOMICS (CESG) JRNL TITL MET-PERCH HEMOGLOBIN AT 1.9A JRNL REF TO BE PUBLISHED JRNL REFN REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 1.90 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.2.0005 REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 69.01 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 96.3 REMARK 3 NUMBER OF REFLECTIONS : 43714 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 + TEST SET) : 0.246 REMARK 3 R VALUE (WORKING SET) : 0.243 REMARK 3 FREE R VALUE : 0.297 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100 REMARK 3 FREE R VALUE TEST SET COUNT : 2327 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH : 1.90 REMARK 3 BIN RESOLUTION RANGE LOW : 1.95 REMARK 3 REFLECTION IN BIN (WORKING SET) : 3128 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.99 REMARK 3 BIN R VALUE (WORKING SET) : 0.2530 REMARK 3 BIN FREE R VALUE SET COUNT : 168 REMARK 3 BIN FREE R VALUE : 0.3220 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 ALL ATOMS : 4867 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.05 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 1.54000 REMARK 3 B22 (A**2) : -1.58000 REMARK 3 B33 (A**2) : 0.04000 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 OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.213 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.194 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.141 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.633 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.927 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.893 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4777 ; 0.018 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): 1 ; 0.001 ; 0.020 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6533 ; 1.809 ; 2.068 REMARK 3 BOND ANGLES OTHERS (DEGREES): 2 ; 0.807 ; 3.000 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 572 ; 6.887 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 184 ;41.365 ;24.022 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 773 ;18.947 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;16.963 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 712 ; 0.138 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3565 ; 0.007 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 1 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2545 ; 0.244 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 1 ; 0.311 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3340 ; 0.316 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): 2 ; 0.341 ; 0.200 REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 233 ; 0.175 ; 0.200 REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 53 ; 0.260 ; 0.200 REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 5 ; 0.169 ; 0.200 REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2934 ; 1.780 ; 2.000 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1 ; 0.080 ; 2.000 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4603 ; 3.036 ; 4.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2126 ; 5.027 ; 6.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1922 ; 6.581 ; 8.000 REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 2 REMARK 3 REMARK 3 NCS GROUP NUMBER : 1 REMARK 3 CHAIN NAMES : A C REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 A 1 A 142 2 REMARK 3 1 C 1 C 142 2 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 TIGHT POSITIONAL 1 A (A): 564 ; 0.08 ; 0.05 REMARK 3 MEDIUM POSITIONAL 1 A (A): 532 ; 0.53 ; 0.50 REMARK 3 TIGHT THERMAL 1 A (A**2): 564 ; 0.38 ; 0.50 REMARK 3 MEDIUM THERMAL 1 A (A**2): 532 ; 1.72 ; 2.00 REMARK 3 REMARK 3 NCS GROUP NUMBER : 2 REMARK 3 CHAIN NAMES : B D REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 B 16 B 129 2 REMARK 3 1 D 16 D 129 2 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 TIGHT POSITIONAL 2 B (A): 456 ; 0.07 ; 0.05 REMARK 3 MEDIUM POSITIONAL 2 B (A): 413 ; 0.37 ; 0.50 REMARK 3 TIGHT THERMAL 2 B (A**2): 456 ; 0.34 ; 0.50 REMARK 3 MEDIUM THERMAL 2 B (A**2): 413 ; 1.79 ; 2.00 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 0 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : BABINET MODEL WITH MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.20 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE REMARK 3 RIDING POSITIONS REMARK 4 REMARK 4 1XQ5 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 (2007-05-29) REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB . REMARK 100 THE RCSB ID CODE IS RCSB030635. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 31-JUL-2004 REMARK 200 TEMPERATURE (KELVIN) : 110.0 REMARK 200 PH : 7.00 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 19-BM REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97934 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : APS-1 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 43714 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.898 REMARK 200 RESOLUTION RANGE LOW (A) : 69.007 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -1.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 96.3 REMARK 200 DATA REDUNDANCY : 6.500 REMARK 200 R MERGE (I) : 0.08400 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 15.0960 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97 REMARK 200 COMPLETENESS FOR SHELL (%) : 96.1 REMARK 200 DATA REDUNDANCY IN SHELL : 5.90 REMARK 200 R MERGE FOR SHELL (I) : 0.52100 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 4.027 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: PDB ENTRY 1OUU REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 46.00 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.16 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4K, HEPES, PH 7.0, BATCH, REMARK 280 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 28.65100 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 60.88950 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 42.49300 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 60.88950 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 28.65100 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 42.49300 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: 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 OE1 GLU D 125 O HOH 275 2.05 REMARK 500 FE HEM B 148 O HOH 379 2.10 REMARK 500 FE HEM C 143 O HOH 380 2.14 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 48 C - N - CA ANGL. DEV. = 14.1 DEGREES REMARK 500 VAL A 68 CB - CA - C ANGL. DEV. = 11.0 DEGREES REMARK 500 LEU A 87 CA - CB - CG ANGL. DEV. = 12.0 DEGREES REMARK 500 LEU A 133 CB - CG - CD2 ANGL. DEV. =-13.5 DEGREES REMARK 500 LEU B 141 N - CA - C ANGL. DEV. = 12.2 DEGREES REMARK 500 ASP C 8 CB - CA - C ANGL. DEV. = 10.6 DEGREES REMARK 500 ILE C 67 CG1 - CB - CG2 ANGL. DEV. =-15.1 DEGREES REMARK 500 LEU C 133 CB - CG - CD2 ANGL. DEV. =-10.7 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 ASP A 48 62.92 121.92 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 LYS A 47 ASP A 48 -49.52 REMARK 500 LEU B 141 GLY B 142 78.06 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 274 DISTANCE = 7.65 ANGSTROMS REMARK 525 HOH 299 DISTANCE = 9.39 ANGSTROMS REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: PERCH HEMOGLOBIN RELATED DB: TARGETDB REMARK 900 RELATED ID: PERCH RELATED DB: TARGETDB REMARK 900 RELATED ID: HEMOGLOBIN RELATED DB: TARGETDB REMARK 999 REMARK 999 SEQUENCE REMARK 999 THE SEQUENCE OF THE PROTEIN WAS NOT DEPOSITED REMARK 999 INTO ANY SEQUENCE DATABASE. SEQRES 1 A 142 SER LEU SER SER LYS ASP LYS ASP THR VAL LYS ALA LEU SEQRES 2 A 142 TRP GLY LYS ILE ALA ASP LYS ALA GLU GLU ILE GLY SER SEQRES 3 A 142 ASP ALA LEU SER ARG MET LEU ALA VAL TYR PRO GLN THR SEQRES 4 A 142 LYS THR TYR PHE SER HIS TRP LYS ASP LEU SER PRO GLY SEQRES 5 A 142 SER ALA PRO VAL ASN LYS HIS GLY LYS THR ILE MET GLY SEQRES 6 A 142 GLY ILE VAL ASP ALA VAL ALA SER ILE ASP ASP LEU ASN SEQRES 7 A 142 ALA GLY LEU LEU ALA LEU SER GLU LEU HIS ALA PHE THR SEQRES 8 A 142 LEU ARG VAL ASP PRO ALA ASN PHE LYS ILE LEU SER HIS SEQRES 9 A 142 CYS ILE LEU VAL LEU LEU ALA VAL LYS PHE PRO LYS ASP SEQRES 10 A 142 PHE THR PRO GLU VAL HIS ILE SER TYR ASP LYS PHE PHE SEQRES 11 A 142 SER ALA LEU ALA ARG ALA LEU ALA GLU LYS TYR ARG SEQRES 1 B 146 VAL VAL TRP THR ASP PHE GLU ARG ALA THR ILE ALA ASP SEQRES 2 B 146 ILE PHE SER LYS LEU ASP TYR GLU ALA VAL GLY GLY ALA SEQRES 3 B 146 THR LEU ALA ARG CYS LEU ILE VAL TYR PRO TRP THR GLN SEQRES 4 B 146 ARG TYR PHE GLY ASN PHE GLY ASN LEU TYR ASN ALA ALA SEQRES 5 B 146 ALA ILE MET GLY ASN PRO MET ILE ALA LYS HIS GLY THR SEQRES 6 B 146 THR ILE LEU HIS GLY LEU ASP ARG ALA VAL LYS ASN MET SEQRES 7 B 146 ASP ASN ILE LYS ALA THR TYR ALA GLU LEU SER VAL LEU SEQRES 8 B 146 HIS SER GLU LYS LEU HIS VAL ASP PRO ASP ASN PHE LYS SEQRES 9 B 146 LEU LEU SER ASP CYS LEU THR ILE VAL VAL ALA ALA GLN SEQRES 10 B 146 LEU GLY LYS ALA PHE SER GLY GLU VAL GLN ALA ALA PHE SEQRES 11 B 146 GLN LYS PHE LEU SER VAL VAL VAL SER ALA LEU GLY LYS SEQRES 12 B 146 GLN TYR HIS SEQRES 1 C 142 SER LEU SER SER LYS ASP LYS ASP THR VAL LYS ALA LEU SEQRES 2 C 142 TRP GLY LYS ILE ALA ASP LYS ALA GLU GLU ILE GLY SER SEQRES 3 C 142 ASP ALA LEU SER ARG MET LEU ALA VAL TYR PRO GLN THR SEQRES 4 C 142 LYS THR TYR PHE SER HIS TRP LYS ASP LEU SER PRO GLY SEQRES 5 C 142 SER ALA PRO VAL ASN LYS HIS GLY LYS THR ILE MET GLY SEQRES 6 C 142 GLY ILE VAL ASP ALA VAL ALA SER ILE ASP ASP LEU ASN SEQRES 7 C 142 ALA GLY LEU LEU ALA LEU SER GLU LEU HIS ALA PHE THR SEQRES 8 C 142 LEU ARG VAL ASP PRO ALA ASN PHE LYS ILE LEU SER HIS SEQRES 9 C 142 CYS ILE LEU VAL LEU LEU ALA VAL LYS PHE PRO LYS ASP SEQRES 10 C 142 PHE THR PRO GLU VAL HIS ILE SER TYR ASP LYS PHE PHE SEQRES 11 C 142 SER ALA LEU ALA ARG ALA LEU ALA GLU LYS TYR ARG SEQRES 1 D 146 VAL VAL TRP THR ASP PHE GLU ARG ALA THR ILE ALA ASP SEQRES 2 D 146 ILE PHE SER LYS LEU ASP TYR GLU ALA VAL GLY GLY ALA SEQRES 3 D 146 THR LEU ALA ARG CYS LEU ILE VAL TYR PRO TRP THR GLN SEQRES 4 D 146 ARG TYR PHE GLY ASN PHE GLY ASN LEU TYR ASN ALA ALA SEQRES 5 D 146 ALA ILE MET GLY ASN PRO MET ILE ALA LYS HIS GLY THR SEQRES 6 D 146 THR ILE LEU HIS GLY LEU ASP ARG ALA VAL LYS ASN MET SEQRES 7 D 146 ASP ASN ILE LYS ALA THR TYR ALA GLU LEU SER VAL LEU SEQRES 8 D 146 HIS SER GLU LYS LEU HIS VAL ASP PRO ASP ASN PHE LYS SEQRES 9 D 146 LEU LEU SER ASP CYS LEU THR ILE VAL VAL ALA ALA GLN SEQRES 10 D 146 LEU GLY LYS ALA PHE SER GLY GLU VAL GLN ALA ALA PHE SEQRES 11 D 146 GLN LYS PHE LEU SER VAL VAL VAL SER ALA LEU GLY LYS SEQRES 12 D 146 GLN TYR HIS HET ACE A 0 3 HET ACE C 0 3 HET HEM A 143 43 HET HEM B 148 43 HET HEM C 143 43 HET HEM D 148 43 HETNAM ACE ACETYL GROUP HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE HETSYN HEM HEME FORMUL 5 ACE 2(C2 H4 O) FORMUL 7 HEM 4(C34 H32 FE N4 O4) FORMUL 11 HOH *219(H2 O) HELIX 1 1 SER A 3 ILE A 17 1 15 HELIX 2 2 LYS A 20 TYR A 36 1 17 HELIX 3 3 PRO A 37 SER A 44 5 8 HELIX 4 4 SER A 53 SER A 73 1 21 HELIX 5 5 ASP A 76 LEU A 81 1 6 HELIX 6 6 LEU A 81 THR A 91 1 11 HELIX 7 7 PRO A 96 PHE A 114 1 19 HELIX 8 8 PRO A 115 PHE A 118 5 4 HELIX 9 9 THR A 119 GLU A 139 1 21 HELIX 10 10 LYS A 140 ARG A 142 5 3 HELIX 11 11 THR B 4 LEU B 18 1 15 HELIX 12 12 ASP B 19 TYR B 35 1 17 HELIX 13 13 PRO B 36 GLY B 43 5 8 HELIX 14 14 ASN B 50 GLY B 56 1 7 HELIX 15 15 ASN B 57 LYS B 76 1 20 HELIX 16 16 ASN B 80 TYR B 85 1 6 HELIX 17 17 TYR B 85 SER B 93 1 9 HELIX 18 18 PRO B 100 GLY B 119 1 20 HELIX 19 19 LYS B 120 PHE B 122 5 3 HELIX 20 20 SER B 123 GLY B 142 1 20 HELIX 21 21 SER C 3 ILE C 17 1 15 HELIX 22 22 LYS C 20 TYR C 36 1 17 HELIX 23 23 PRO C 37 SER C 44 5 8 HELIX 24 24 SER C 53 SER C 73 1 21 HELIX 25 25 ASP C 76 LEU C 81 1 6 HELIX 26 26 LEU C 81 PHE C 90 1 10 HELIX 27 27 ASP C 95 ALA C 97 5 3 HELIX 28 28 ASN C 98 PHE C 114 1 17 HELIX 29 29 PRO C 115 PHE C 118 5 4 HELIX 30 30 THR C 119 GLU C 139 1 21 HELIX 31 31 THR D 4 LEU D 18 1 15 HELIX 32 32 ASP D 19 TYR D 35 1 17 HELIX 33 33 PRO D 36 GLY D 43 5 8 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 ASN D 80 TYR D 85 1 6 HELIX 37 37 TYR D 85 SER D 93 1 9 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 SER D 123 GLY D 142 1 20 LINK FE HEM A 143 NE2 HIS A 88 LINK FE HEM B 148 NE2 HIS B 92 LINK FE HEM C 143 NE2 HIS C 88 LINK FE HEM D 148 NE2 HIS D 92 LINK C ACE A 0 N SER A 1 LINK C ACE C 0 N SER C 1 CRYST1 57.302 84.986 121.779 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 0.017451 0.000000 0.000000 0.00000 SCALE2 0.000000 0.011767 0.000000 0.00000 SCALE3 0.000000 0.000000 0.008212 0.00000