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HEADER OXYGEN STORAGE/TRANSPORT 04-OCT-05 2B7H TITLE HEMOGLOBIN FROM CERDOCYON THOUS, A CANIDAE FROM BRAZIL, AT TITLE 2 2.2 ANGSTROMS 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: DUSICYON THOUS; SOURCE 3 MOL_ID: 2; SOURCE 4 ORGANISM_SCIENTIFIC: DUSICYON THOUS KEYWDS HEMOGLOBIN, AQUOMET, X-RAY CRYSTALLOGRAPHY, CERDOCYON THOUS EXPDTA X-RAY DIFFRACTION AUTHOR G.F.ESTEVES,V.C.SILVA,C.BLOCH JR.,F.J.MEDRANO, AUTHOR 2 J.A.R.G.BARBOSA,S.M.FREITAS REVDAT 1 12-SEP-06 2B7H 0 JRNL AUTH G.F.ESTEVES,V.C.SILVA,C.BLOCH JR.,F.J.MEDRANO, JRNL AUTH 2 J.A.R.G.BARBOSA,S.M.FREITAS JRNL TITL CRYSTAL STRUCTURE AND BIOPHYSICAL CHARACTERIZATION JRNL TITL 2 OF THE CERDOCYON THOUS, A CANIDAE FROM BRAZIL. JRNL REF TO BE PUBLISHED JRNL REFN REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 2.20 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 : ENGH & HUBER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 3 NUMBER OF REFLECTIONS : 28633 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) : 0.169 REMARK 3 R VALUE (WORKING SET) : 0.165 REMARK 3 FREE R VALUE : 0.233 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100 REMARK 3 FREE R VALUE TEST SET COUNT : 1530 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH : 2.20 REMARK 3 BIN RESOLUTION RANGE LOW : 2.26 REMARK 3 REFLECTION IN BIN (WORKING SET) : 2039 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.26 REMARK 3 BIN R VALUE (WORKING SET) : 0.1680 REMARK 3 BIN FREE R VALUE SET COUNT : 108 REMARK 3 BIN FREE R VALUE : 0.2740 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 ALL ATOMS : 5037 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 26.91 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.57 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -1.00000 REMARK 3 B22 (A**2) : -0.15000 REMARK 3 B33 (A**2) : 1.15000 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): 0.283 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.218 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.142 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.249 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.953 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.911 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4716 ; 0.015 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6468 ; 1.399 ; 2.065 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 571 ; 5.525 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 182 ;36.130 ;24.341 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 729 ;14.431 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 10 ;12.223 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 705 ; 0.092 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3548 ; 0.006 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 3065 ; 0.216 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3314 ; 0.312 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 588 ; 0.161 ; 0.200 REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 2 ; 0.025 ; 0.200 REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 58 ; 0.151 ; 0.200 REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 15 ; 0.156 ; 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): 2886 ; 0.707 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4576 ; 1.196 ; 2.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2061 ; 2.048 ; 3.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1884 ; 2.996 ; 4.500 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 : 0 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 4 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 NUMBER OF COMPONENTS GROUP : 2 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 1 A 141 REMARK 3 RESIDUE RANGE : A 200 A 200 REMARK 3 ORIGIN FOR THE GROUP (A): -14.7250 -6.8243 -4.3671 REMARK 3 T TENSOR REMARK 3 T11: -0.0976 T22: -0.1415 REMARK 3 T33: -0.1875 T12: 0.0092 REMARK 3 T13: 0.0074 T23: 0.0019 REMARK 3 L TENSOR REMARK 3 L11: 3.0878 L22: 1.2604 REMARK 3 L33: 1.4903 L12: 0.0346 REMARK 3 L13: 0.0893 L23: 0.2159 REMARK 3 S TENSOR REMARK 3 S11: -0.0242 S12: 0.0197 S13: -0.0627 REMARK 3 S21: 0.0231 S22: 0.0349 S23: 0.0420 REMARK 3 S31: 0.1783 S32: 0.1128 S33: -0.0107 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 NUMBER OF COMPONENTS GROUP : 2 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : B 2 B 145 REMARK 3 RESIDUE RANGE : B 200 B 200 REMARK 3 ORIGIN FOR THE GROUP (A): -31.6549 9.3321 -0.0934 REMARK 3 T TENSOR REMARK 3 T11: -0.0672 T22: -0.1102 REMARK 3 T33: -0.0144 T12: 0.0291 REMARK 3 T13: -0.0393 T23: 0.0067 REMARK 3 L TENSOR REMARK 3 L11: 4.0680 L22: 1.8756 REMARK 3 L33: 2.2526 L12: -0.2974 REMARK 3 L13: -1.2965 L23: -0.1522 REMARK 3 S TENSOR REMARK 3 S11: 0.0621 S12: -0.0077 S13: 0.6078 REMARK 3 S21: 0.1159 S22: 0.0630 S23: -0.0500 REMARK 3 S31: -0.3672 S32: -0.2119 S33: -0.1251 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 NUMBER OF COMPONENTS GROUP : 2 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : C 1 C 141 REMARK 3 RESIDUE RANGE : C 200 C 200 REMARK 3 ORIGIN FOR THE GROUP (A): -27.9532 -11.6629 23.8805 REMARK 3 T TENSOR REMARK 3 T11: -0.1076 T22: -0.1571 REMARK 3 T33: -0.1444 T12: -0.0177 REMARK 3 T13: 0.0376 T23: 0.0152 REMARK 3 L TENSOR REMARK 3 L11: 3.3970 L22: 1.7903 REMARK 3 L33: 1.5880 L12: 0.3197 REMARK 3 L13: 0.4970 L23: 0.4025 REMARK 3 S TENSOR REMARK 3 S11: -0.0199 S12: -0.0320 S13: -0.2864 REMARK 3 S21: -0.1146 S22: -0.0218 S23: -0.1375 REMARK 3 S31: 0.1674 S32: -0.0991 S33: 0.0417 REMARK 3 REMARK 3 TLS GROUP : 4 REMARK 3 NUMBER OF COMPONENTS GROUP : 2 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : D 1 D 145 REMARK 3 RESIDUE RANGE : D 200 D 200 REMARK 3 ORIGIN FOR THE GROUP (A): -11.2152 5.1936 25.1298 REMARK 3 T TENSOR REMARK 3 T11: -0.1160 T22: -0.1212 REMARK 3 T33: -0.1331 T12: -0.0116 REMARK 3 T13: -0.0279 T23: -0.0061 REMARK 3 L TENSOR REMARK 3 L11: 2.7702 L22: 1.9285 REMARK 3 L33: 2.5942 L12: 0.1424 REMARK 3 L13: -1.1426 L23: 0.8494 REMARK 3 S TENSOR REMARK 3 S11: 0.0295 S12: 0.0123 S13: 0.2906 REMARK 3 S21: -0.1109 S22: 0.0139 S23: -0.0652 REMARK 3 S31: -0.2953 S32: 0.1211 S33: -0.0433 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: SIMULATED ANNEALING WAS PERFORMED REMARK 3 WITH THE CNS SOFTWARE IN THE FIRST CYCLE OR REFINEMENT. USED REMARK 3 TLS REFINEMENT. TYR 145 FROM THE B AND D MOLECULES PRESENTED REMARK 3 WEAK DENSITY FOR AN ALTERNATE CONFORMATION THAT WAS NOT REMARK 3 MODELED. REMARK 4 REMARK 4 2B7H 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 RCSB034770. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 19-MAR-2004 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 7.80 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) : 1.4270 REMARK 200 MONOCHROMATOR : SI CRYSTAL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30219 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200 REMARK 200 RESOLUTION RANGE LOW (A) : 40.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 8.000 REMARK 200 R MERGE (I) : 0.07200 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 29.1000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 7.80 REMARK 200 R MERGE FOR SHELL (I) : 0.30600 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 7.000 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: MOLREP REMARK 200 STARTING MODEL: PDB ENTRY 1FHJ REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 46.50 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 16 % POLYETHYLENEGLYCOL (PEG), 0.1 REMARK 280 M HEPES NA, PH 7.8, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE REMARK 280 293K 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 26.36550 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 65.14250 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 42.11850 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 65.14250 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.36550 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 42.11850 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 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 VAL B 1 REMARK 465 HIS B 146 REMARK 465 HIS D 146 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 FE HEM B 200 O HOH 2 1.98 REMARK 500 SG CYS B 93 CE2 TYR B 145 1.99 REMARK 500 FE HEM D 200 O HOH 4 2.01 REMARK 500 FE HEM A 200 O HOH 1 2.03 REMARK 500 FE HEM C 200 O HOH 3 2.03 REMARK 500 SG CYS B 93 CD2 TYR B 145 2.06 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 ILE A 17 CG1 ILE A 17 CD1 -0.109 REMARK 500 CYS D 93 CB CYS D 93 SG 0.121 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. = -9.0 DEGREES REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1FHJ RELATED DB: PDB REMARK 900 USED AS THE MODEL FOR THE MOLECULAR REPLACEMENT. REMARK 999 REMARK 999 SEQUENCE REMARK 999 THE SEQUENCE OF THE PROTEIN HAS NOT BEEN DEPOSITED REMARK 999 INTO ANY SEQUENCE DATABASE. DBREF 2B7H A 1 141 UNP P60523 HBA_CHRBR 1 141 DBREF 2B7H B 1 146 UNP P60526 HBB_CHRBR 1 146 DBREF 2B7H C 1 141 UNP P60523 HBA_CHRBR 1 141 DBREF 2B7H D 1 146 UNP P60526 HBB_CHRBR 1 146 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 ALA 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 SER 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 ALA 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 SER 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 SO4 501 5 HET SO4 502 5 HET HEM A 200 43 HET HEM B 200 43 HET HEM C 200 43 HET HEM D 200 43 HETNAM SO4 SULFATE ION HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE HETSYN HEM HEME FORMUL 5 SO4 2(O4 S 2-) FORMUL 7 HEM 4(C34 H32 FE N4 O4) FORMUL 11 HOH *443(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 LEU A 80 1 6 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 SER A 138 ARG A 141 5 4 HELIX 10 10 THR B 4 ALA B 16 1 13 HELIX 11 11 GLU B 22 TYR B 35 1 14 HELIX 12 12 PRO B 36 GLY B 46 5 11 HELIX 13 13 THR B 50 SER B 56 1 7 HELIX 14 14 ASN B 57 LYS B 76 1 20 HELIX 15 15 ASN B 80 LYS B 95 1 16 HELIX 16 16 PRO B 100 GLY B 119 1 20 HELIX 17 17 LYS B 120 PHE B 122 5 3 HELIX 18 18 THR B 123 HIS B 143 1 21 HELIX 19 19 SER C 3 GLY C 18 1 16 HELIX 20 20 HIS C 20 PHE C 36 1 17 HELIX 21 21 PRO C 37 PHE C 43 5 7 HELIX 22 22 SER C 52 ALA C 71 1 20 HELIX 23 23 HIS C 72 ASP C 74 5 3 HELIX 24 24 ASP C 75 LEU C 80 1 6 HELIX 25 25 LEU C 80 LYS C 90 1 11 HELIX 26 26 PRO C 95 HIS C 113 1 19 HELIX 27 27 THR C 118 THR C 137 1 20 HELIX 28 28 SER C 138 ARG C 141 5 4 HELIX 29 29 THR D 4 ALA D 16 1 13 HELIX 30 30 GLU D 22 TYR D 35 1 14 HELIX 31 31 PRO D 36 GLY D 46 5 11 HELIX 32 32 THR D 50 SER D 56 1 7 HELIX 33 33 ASN D 57 ASN D 77 1 21 HELIX 34 34 ASN D 80 LYS D 95 1 16 HELIX 35 35 PRO D 100 GLY D 119 1 20 HELIX 36 36 LYS D 120 PHE D 122 5 3 HELIX 37 37 THR D 123 HIS D 143 1 21 LINK NE2 HIS A 87 FE HEM A 200 LINK NE2 HIS C 87 FE HEM C 200 LINK NE2 HIS B 92 FE HEM B 200 LINK NE2 HIS D 92 FE HEM D 200 CRYST1 52.731 84.237 130.285 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 0.018964 0.000000 0.000000 0.00000 SCALE2 0.000000 0.011871 0.000000 0.00000 SCALE3 0.000000 0.000000 0.007675 0.00000