HEADER OXYGEN STORAGE/TRANSPORT 20-AUG-04 1X9F TITLE HEMOGLOBIN DODECAMER FROM LUMBRICUS ERYTHROCRUORIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: GLOBIN IV, EXTRACELLULAR; COMPND 3 CHAIN: A, E, I; COMPND 4 SYNONYM: ERYTHROCRUORIN, GLOBIN A; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: GLOBIN II, EXTRACELLULAR; COMPND 7 CHAIN: B, F, J; COMPND 8 SYNONYM: ERYTHROCRUORIN; GLOBIN AIII; GLOBIN B; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: GLOBIN III, EXTRACELLULAR; COMPND 11 CHAIN: C, G, K; COMPND 12 SYNONYM: ERYTHROCRUORIN; GLOBIN C; COMPND 13 MOL_ID: 4; COMPND 14 MOLECULE: HEMOGLOBIN CHAIN D1; COMPND 15 CHAIN: D, H, L SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: LUMBRICUS TERRESTRIS; SOURCE 3 ORGANISM_COMMON: COMMON EARTHWORM; SOURCE 4 ORGAN: BLOOD; SOURCE 5 MOL_ID: 2; SOURCE 6 ORGANISM_SCIENTIFIC: LUMBRICUS TERRESTRIS; SOURCE 7 ORGANISM_COMMON: COMMON EARTHWORM; SOURCE 8 ORGAN: BLOOD; SOURCE 9 MOL_ID: 3; SOURCE 10 ORGANISM_SCIENTIFIC: LUMBRICUS TERRESTRIS; SOURCE 11 ORGANISM_COMMON: COMMON EARTHWORM; SOURCE 12 ORGAN: BLOOD; SOURCE 13 MOL_ID: 4; SOURCE 14 ORGANISM_SCIENTIFIC: LUMBRICUS TERRESTRIS; SOURCE 15 ORGANISM_COMMON: COMMON EARTHWORM; SOURCE 16 ORGAN: BLOOD KEYWDS CRYSTAL; DODECAMER; ALLOSTERIC EXPDTA X-RAY DIFFRACTION AUTHOR K.STRAND,J.E.KNAPP,B.BHYRAVBHATLA,W.E.ROYER JR. REVDAT 1 30-NOV-04 1X9F 0 JRNL AUTH K.STRAND,J.E.KNAPP,B.BHYRAVBHATLA,W.E.ROYER JR. JRNL TITL CRYSTAL STRUCTURE OF THE HEMOGLOBIN DODECAMER FROM JRNL TITL 2 LUMBRICUS ERYTHROCRUORIN: ALLOSTERIC CORE OF GIANT JRNL TITL 3 ANNELID RESPIRATORY COMPLEXES JRNL REF J.MOL.BIOL. V. 344 119 2004 JRNL REFN ASTM JMOBAK UK ISSN 0022-2836 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 2.60 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.2 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) : 2.60 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 105.41 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 88.7 REMARK 3 NUMBER OF REFLECTIONS : 63085 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) : 0.215 REMARK 3 R VALUE (WORKING SET) : 0.213 REMARK 3 FREE R VALUE : 0.246 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 3337 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH : 2.60 REMARK 3 BIN RESOLUTION RANGE LOW : 2.67 REMARK 3 REFLECTION IN BIN (WORKING SET) : 4470 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 86.63 REMARK 3 BIN R VALUE (WORKING SET) : 0.3060 REMARK 3 BIN FREE R VALUE SET COUNT : 255 REMARK 3 BIN FREE R VALUE : 0.3110 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 ALL ATOMS : 14847 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.32 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -1.45000 REMARK 3 B22 (A**2) : -0.87000 REMARK 3 B33 (A**2) : 2.32000 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): 0.524 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.329 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.204 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.526 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.916 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.888 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 14987 ; 0.009 ; 0.021 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 20434 ; 1.875 ; 1.983 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1731 ; 4.236 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 720 ;38.027 ;23.417 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2481 ;17.110 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 111 ;22.066 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2121 ; 0.083 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 11538 ; 0.005 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 8104 ; 0.297 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 10257 ; 0.304 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 529 ; 0.131 ; 0.200 REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 12 ; 0.201 ; 0.200 REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 71 ; 0.287 ; 0.200 REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 11 ; 0.201 ; 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): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL 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 : 0 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : 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 1X9F 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 RCSB030105. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : NULL REMARK 200 TEMPERATURE (KELVIN) : NULL REMARK 200 PH : 6.80 REMARK 200 NUMBER OF CRYSTALS USED : NULL REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : N; Y REMARK 200 RADIATION SOURCE : ROTATING ANODE; APS REMARK 200 BEAMLINE : NULL; 14-BM-C REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU200H REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418; 1.0000 REMARK 200 MONOCHROMATOR : YALE MIRRORS; BEAMLINE OPTICS REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE; CCD REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IIC; ADSC REMARK 200 QUANTUM 4 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : R-AXIS REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 74920 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600 REMARK 200 RESOLUTION RANGE LOW (A) : 105.410 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : NULL REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : NULL REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: CNS REMARK 200 STARTING MODEL: 3.8 STRUCTURE OF THE WHOLE MOLECULE REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 57.60 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.92 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 2.8M NA PHOSPHATE, PH 6.8, VAPOR REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 281.0K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,1/2+Z REMARK 290 3555 -X,Y,1/2-Z REMARK 290 4555 X,-Y,-Z REMARK 290 5555 1/2+X,1/2+Y,Z REMARK 290 6555 1/2-X,1/2-Y,1/2+Z REMARK 290 7555 1/2-X,1/2+Y,1/2-Z REMARK 290 8555 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 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 101.44300 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 101.44300 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 69.61250 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 86.03550 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 69.61250 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 86.03550 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 101.44300 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 69.61250 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 86.03550 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 101.44300 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 69.61250 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 86.03550 REMARK 290 SMTRY3 8 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 12CHAIN(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, E, F, G, H, I, REMARK 350 J, K, L 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 ALA A 1 REMARK 465 ASP A 2 REMARK 465 ASP A 3 REMARK 465 GLU A 4 REMARK 465 ASP C 1 REMARK 465 GLU C 2 REMARK 465 ASN C 152 REMARK 465 ALA C 153 REMARK 465 ALA E 1 REMARK 465 ASP E 2 REMARK 465 ASP E 3 REMARK 465 GLU E 4 REMARK 465 ASP G 1 REMARK 465 GLU G 2 REMARK 465 ASN G 152 REMARK 465 ALA G 153 REMARK 465 ALA I 1 REMARK 465 ASP I 2 REMARK 465 ASP I 3 REMARK 465 GLU I 4 REMARK 465 ASP K 1 REMARK 465 GLU K 2 REMARK 465 ASN K 152 REMARK 465 ALA K 153 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 CB HIS C 3 O HOH 416 0.92 REMARK 500 CA HIS C 3 O HOH 416 1.33 REMARK 500 CG HIS C 3 O HOH 416 1.73 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 A 31 C ARG A 31 O 0.090 REMARK 500 VAL A 32 N VAL A 32 CA 0.062 REMARK 500 VAL A 32 CA VAL A 32 C 0.054 REMARK 500 ARG A 31 C VAL A 32 N 0.066 REMARK 500 GLY A 64 N GLY A 64 CA 0.054 REMARK 500 LYS A 78 CE LYS A 78 NZ 0.076 REMARK 500 ILE A 81 CG1 ILE A 81 CD1 0.052 REMARK 500 LYS B 1 CE LYS B 1 NZ 0.064 REMARK 500 HIS C 3 CA HIS C 3 CB 0.146 REMARK 500 HIS C 3 CB HIS C 3 CG 0.134 REMARK 500 TRP D 32 CB TRP D 32 CG -0.050 REMARK 500 TRP D 128 CB TRP D 128 CG -0.059 REMARK 500 ARG E 31 C ARG E 31 O 0.073 REMARK 500 VAL E 32 N VAL E 32 CA 0.094 REMARK 500 LYS E 78 CE LYS E 78 NZ 0.067 REMARK 500 HIS G 3 CB HIS G 3 CG 0.052 REMARK 500 ILE G 74 CG1 ILE G 74 CD1 0.065 REMARK 500 TRP H 128 CB TRP H 128 CG -0.048 REMARK 500 THR I 28 CB THR I 28 OG1 0.076 REMARK 500 ARG I 31 C ARG I 31 O 0.092 REMARK 500 VAL I 32 N VAL I 32 CA 0.065 REMARK 500 LYS I 78 CE LYS I 78 NZ 0.114 REMARK 500 HIS K 3 CB HIS K 3 CG 0.052 REMARK 500 ILE K 74 CG1 ILE K 74 CD1 0.054 REMARK 500 TRP L 128 CB TRP L 128 CG -0.047 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 PHE A 27 N - CA - C ANGL. DEV. = -8.7 DEGREES REMARK 500 HIS C 3 CB - CA - C ANGL. DEV. = 9.5 DEGREES REMARK 500 HIS C 3 N - CA - CB ANGL. DEV. = 10.0 DEGREES REMARK 500 HIS C 3 CA - CB - CG ANGL. DEV. = 17.9 DEGREES REMARK 500 HIS C 3 N - CA - C ANGL. DEV. =-45.3 DEGREES REMARK 500 LYS E 57 N - CA - C ANGL. DEV. = 8.1 DEGREES REMARK 500 THR I 28 OG1 - CB - CG2 ANGL. DEV. = -9.1 DEGREES REMARK 500 LEU I 150 N - CA - C ANGL. DEV. = 8.2 DEGREES DBREF 1X9F A 1 151 UNP P13579 GLB4_LUMTE 1 151 DBREF 1X9F E 1 151 UNP P13579 GLB4_LUMTE 1 151 DBREF 1X9F I 1 151 UNP P13579 GLB4_LUMTE 1 151 DBREF 1X9F B 1 145 UNP P02218 GLB2_LUMTE 1 145 DBREF 1X9F F 1 145 UNP P02218 GLB2_LUMTE 1 145 DBREF 1X9F J 1 145 UNP P02218 GLB2_LUMTE 1 145 DBREF 1X9F C 1 153 UNP P11069 GLB3_LUMTE 18 170 DBREF 1X9F G 1 153 UNP P11069 GLB3_LUMTE 18 170 DBREF 1X9F K 1 153 UNP P11069 GLB3_LUMTE 18 170 DBREF 1X9F D 1 140 UNP O61233 O61233_LUMTE 19 158 DBREF 1X9F H 1 140 UNP O61233 O61233_LUMTE 19 158 DBREF 1X9F L 1 140 UNP O61233 O61233_LUMTE 19 158 SEQADV 1X9F LYS A 78 UNP P13579 ASP 78 CONFLICT SEQADV 1X9F LYS E 78 UNP P13579 ASP 78 CONFLICT SEQADV 1X9F LYS I 78 UNP P13579 ASP 78 CONFLICT SEQADV 1X9F ASP B 66 UNP P02218 GLU 66 CONFLICT SEQADV 1X9F ASP F 66 UNP P02218 GLU 66 CONFLICT SEQADV 1X9F ASP J 66 UNP P02218 GLU 66 CONFLICT SEQADV 1X9F GLU C 49 UNP P11069 ASP 66 CONFLICT SEQADV 1X9F GLU G 49 UNP P11069 ASP 66 CONFLICT SEQADV 1X9F GLU K 49 UNP P11069 ASP 66 CONFLICT SEQRES 1 A 151 ALA ASP ASP GLU ASP CYS CYS SER TYR GLU ASP ARG ARG SEQRES 2 A 151 GLU ILE ARG HIS ILE TRP ASP ASP VAL TRP SER SER SER SEQRES 3 A 151 PHE THR ASP ARG ARG VAL ALA ILE VAL ARG ALA VAL PHE SEQRES 4 A 151 ASP ASP LEU PHE LYS HIS TYR PRO THR SER LYS ALA LEU SEQRES 5 A 151 PHE GLU ARG VAL LYS ILE ASP GLU PRO GLU SER GLY GLU SEQRES 6 A 151 PHE LYS SER HIS LEU VAL ARG VAL ALA ASN GLY LEU LYS SEQRES 7 A 151 LEU LEU ILE ASN LEU LEU ASP ASP THR LEU VAL LEU GLN SEQRES 8 A 151 SER HIS LEU GLY HIS LEU ALA ASP GLN HIS ILE GLN ARG SEQRES 9 A 151 LYS GLY VAL THR LYS GLU TYR PHE ARG GLY ILE GLY GLU SEQRES 10 A 151 ALA PHE ALA ARG VAL LEU PRO GLN VAL LEU SER CYS PHE SEQRES 11 A 151 ASN VAL ASP ALA TRP ASN ARG CYS PHE HIS ARG LEU VAL SEQRES 12 A 151 ALA ARG ILE ALA LYS ASP LEU PRO SEQRES 1 B 145 LYS LYS GLN CYS GLY VAL LEU GLU GLY LEU LYS VAL LYS SEQRES 2 B 145 SER GLU TRP GLY ARG ALA TYR GLY SER GLY HIS ASP ARG SEQRES 3 B 145 GLU ALA PHE SER GLN ALA ILE TRP ARG ALA THR PHE ALA SEQRES 4 B 145 GLN VAL PRO GLU SER ARG SER LEU PHE LYS ARG VAL HIS SEQRES 5 B 145 GLY ASP ASP THR SER HIS PRO ALA PHE ILE ALA HIS ALA SEQRES 6 B 145 ASP ARG VAL LEU GLY GLY LEU ASP ILE ALA ILE SER THR SEQRES 7 B 145 LEU ASP GLN PRO ALA THR LEU LYS GLU GLU LEU ASP HIS SEQRES 8 B 145 LEU GLN VAL GLN HIS GLU GLY ARG LYS ILE PRO ASP ASN SEQRES 9 B 145 TYR PHE ASP ALA PHE LYS THR ALA ILE LEU HIS VAL VAL SEQRES 10 B 145 ALA ALA GLN LEU GLY ARG CYS TYR ASP ARG GLU ALA TRP SEQRES 11 B 145 ASP ALA CYS ILE ASP HIS ILE GLU ASP GLY ILE LYS GLY SEQRES 12 B 145 HIS HIS SEQRES 1 C 153 ASP GLU HIS GLU HIS CYS CYS SER GLU GLU ASP HIS ARG SEQRES 2 C 153 ILE VAL GLN LYS GLN TRP ASP ILE LEU TRP ARG ASP THR SEQRES 3 C 153 GLU SER SER LYS ILE LYS ILE GLY PHE GLY ARG LEU LEU SEQRES 4 C 153 LEU THR LYS LEU ALA LYS ASP ILE PRO GLU VAL ASN ASP SEQRES 5 C 153 LEU PHE LYS ARG VAL ASP ILE GLU HIS ALA GLU GLY PRO SEQRES 6 C 153 LYS PHE SER ALA HIS ALA LEU ARG ILE LEU ASN GLY LEU SEQRES 7 C 153 ASP LEU ALA ILE ASN LEU LEU ASP ASP PRO PRO ALA LEU SEQRES 8 C 153 ASP ALA ALA LEU ASP HIS LEU ALA HIS GLN HIS GLU VAL SEQRES 9 C 153 ARG GLU GLY VAL GLN LYS ALA HIS PHE LYS LYS PHE GLY SEQRES 10 C 153 GLU ILE LEU ALA THR GLY LEU PRO GLN VAL LEU ASP ASP SEQRES 11 C 153 TYR ASP ALA LEU ALA TRP LYS SER CYS LEU LYS GLY ILE SEQRES 12 C 153 LEU THR LYS ILE SER SER ARG LEU ASN ALA SEQRES 1 D 140 GLU CYS LEU VAL THR GLU SER LEU LYS VAL LYS LEU GLN SEQRES 2 D 140 TRP ALA SER ALA PHE GLY HIS ALA HIS GLU ARG VAL ALA SEQRES 3 D 140 PHE GLY LEU GLU LEU TRP ARG ASP ILE ILE ASP ASP HIS SEQRES 4 D 140 PRO GLU ILE LYS ALA PRO PHE SER ARG VAL ARG GLY ASP SEQRES 5 D 140 ASN ILE TYR SER PRO GLU PHE GLY ALA HIS SER GLN ARG SEQRES 6 D 140 VAL LEU SER GLY LEU ASP ILE THR ILE SER MET LEU ASP SEQRES 7 D 140 THR PRO ASP MET LEU ALA ALA GLN LEU ALA HIS LEU LYS SEQRES 8 D 140 VAL GLN HIS VAL GLU ARG ASN LEU LYS PRO GLU PHE PHE SEQRES 9 D 140 ASP ILE PHE LEU LYS HIS LEU LEU HIS VAL LEU GLY ASP SEQRES 10 D 140 ARG LEU GLY THR HIS PHE ASP PHE GLY ALA TRP HIS ASP SEQRES 11 D 140 CYS VAL ASP GLN ILE ILE ASP GLY ILE LYS SEQRES 1 E 151 ALA ASP ASP GLU ASP CYS CYS SER TYR GLU ASP ARG ARG SEQRES 2 E 151 GLU ILE ARG HIS ILE TRP ASP ASP VAL TRP SER SER SER SEQRES 3 E 151 PHE THR ASP ARG ARG VAL ALA ILE VAL ARG ALA VAL PHE SEQRES 4 E 151 ASP ASP LEU PHE LYS HIS TYR PRO THR SER LYS ALA LEU SEQRES 5 E 151 PHE GLU ARG VAL LYS ILE ASP GLU PRO GLU SER GLY GLU SEQRES 6 E 151 PHE LYS SER HIS LEU VAL ARG VAL ALA ASN GLY LEU LYS SEQRES 7 E 151 LEU LEU ILE ASN LEU LEU ASP ASP THR LEU VAL LEU GLN SEQRES 8 E 151 SER HIS LEU GLY HIS LEU ALA ASP GLN HIS ILE GLN ARG SEQRES 9 E 151 LYS GLY VAL THR LYS GLU TYR PHE ARG GLY ILE GLY GLU SEQRES 10 E 151 ALA PHE ALA ARG VAL LEU PRO GLN VAL LEU SER CYS PHE SEQRES 11 E 151 ASN VAL ASP ALA TRP ASN ARG CYS PHE HIS ARG LEU VAL SEQRES 12 E 151 ALA ARG ILE ALA LYS ASP LEU PRO SEQRES 1 F 145 LYS LYS GLN CYS GLY VAL LEU GLU GLY LEU LYS VAL LYS SEQRES 2 F 145 SER GLU TRP GLY ARG ALA TYR GLY SER GLY HIS ASP ARG SEQRES 3 F 145 GLU ALA PHE SER GLN ALA ILE TRP ARG ALA THR PHE ALA SEQRES 4 F 145 GLN VAL PRO GLU SER ARG SER LEU PHE LYS ARG VAL HIS SEQRES 5 F 145 GLY ASP ASP THR SER HIS PRO ALA PHE ILE ALA HIS ALA SEQRES 6 F 145 ASP ARG VAL LEU GLY GLY LEU ASP ILE ALA ILE SER THR SEQRES 7 F 145 LEU ASP GLN PRO ALA THR LEU LYS GLU GLU LEU ASP HIS SEQRES 8 F 145 LEU GLN VAL GLN HIS GLU GLY ARG LYS ILE PRO ASP ASN SEQRES 9 F 145 TYR PHE ASP ALA PHE LYS THR ALA ILE LEU HIS VAL VAL SEQRES 10 F 145 ALA ALA GLN LEU GLY ARG CYS TYR ASP ARG GLU ALA TRP SEQRES 11 F 145 ASP ALA CYS ILE ASP HIS ILE GLU ASP GLY ILE LYS GLY SEQRES 12 F 145 HIS HIS SEQRES 1 G 153 ASP GLU HIS GLU HIS CYS CYS SER GLU GLU ASP HIS ARG SEQRES 2 G 153 ILE VAL GLN LYS GLN TRP ASP ILE LEU TRP ARG ASP THR SEQRES 3 G 153 GLU SER SER LYS ILE LYS ILE GLY PHE GLY ARG LEU LEU SEQRES 4 G 153 LEU THR LYS LEU ALA LYS ASP ILE PRO GLU VAL ASN ASP SEQRES 5 G 153 LEU PHE LYS ARG VAL ASP ILE GLU HIS ALA GLU GLY PRO SEQRES 6 G 153 LYS PHE SER ALA HIS ALA LEU ARG ILE LEU ASN GLY LEU SEQRES 7 G 153 ASP LEU ALA ILE ASN LEU LEU ASP ASP PRO PRO ALA LEU SEQRES 8 G 153 ASP ALA ALA LEU ASP HIS LEU ALA HIS GLN HIS GLU VAL SEQRES 9 G 153 ARG GLU GLY VAL GLN LYS ALA HIS PHE LYS LYS PHE GLY SEQRES 10 G 153 GLU ILE LEU ALA THR GLY LEU PRO GLN VAL LEU ASP ASP SEQRES 11 G 153 TYR ASP ALA LEU ALA TRP LYS SER CYS LEU LYS GLY ILE SEQRES 12 G 153 LEU THR LYS ILE SER SER ARG LEU ASN ALA SEQRES 1 H 140 GLU CYS LEU VAL THR GLU SER LEU LYS VAL LYS LEU GLN SEQRES 2 H 140 TRP ALA SER ALA PHE GLY HIS ALA HIS GLU ARG VAL ALA SEQRES 3 H 140 PHE GLY LEU GLU LEU TRP ARG ASP ILE ILE ASP ASP HIS SEQRES 4 H 140 PRO GLU ILE LYS ALA PRO PHE SER ARG VAL ARG GLY ASP SEQRES 5 H 140 ASN ILE TYR SER PRO GLU PHE GLY ALA HIS SER GLN ARG SEQRES 6 H 140 VAL LEU SER GLY LEU ASP ILE THR ILE SER MET LEU ASP SEQRES 7 H 140 THR PRO ASP MET LEU ALA ALA GLN LEU ALA HIS LEU LYS SEQRES 8 H 140 VAL GLN HIS VAL GLU ARG ASN LEU LYS PRO GLU PHE PHE SEQRES 9 H 140 ASP ILE PHE LEU LYS HIS LEU LEU HIS VAL LEU GLY ASP SEQRES 10 H 140 ARG LEU GLY THR HIS PHE ASP PHE GLY ALA TRP HIS ASP SEQRES 11 H 140 CYS VAL ASP GLN ILE ILE ASP GLY ILE LYS SEQRES 1 I 151 ALA ASP ASP GLU ASP CYS CYS SER TYR GLU ASP ARG ARG SEQRES 2 I 151 GLU ILE ARG HIS ILE TRP ASP ASP VAL TRP SER SER SER SEQRES 3 I 151 PHE THR ASP ARG ARG VAL ALA ILE VAL ARG ALA VAL PHE SEQRES 4 I 151 ASP ASP LEU PHE LYS HIS TYR PRO THR SER LYS ALA LEU SEQRES 5 I 151 PHE GLU ARG VAL LYS ILE ASP GLU PRO GLU SER GLY GLU SEQRES 6 I 151 PHE LYS SER HIS LEU VAL ARG VAL ALA ASN GLY LEU LYS SEQRES 7 I 151 LEU LEU ILE ASN LEU LEU ASP ASP THR LEU VAL LEU GLN SEQRES 8 I 151 SER HIS LEU GLY HIS LEU ALA ASP GLN HIS ILE GLN ARG SEQRES 9 I 151 LYS GLY VAL THR LYS GLU TYR PHE ARG GLY ILE GLY GLU SEQRES 10 I 151 ALA PHE ALA ARG VAL LEU PRO GLN VAL LEU SER CYS PHE SEQRES 11 I 151 ASN VAL ASP ALA TRP ASN ARG CYS PHE HIS ARG LEU VAL SEQRES 12 I 151 ALA ARG ILE ALA LYS ASP LEU PRO SEQRES 1 J 145 LYS LYS GLN CYS GLY VAL LEU GLU GLY LEU LYS VAL LYS SEQRES 2 J 145 SER GLU TRP GLY ARG ALA TYR GLY SER GLY HIS ASP ARG SEQRES 3 J 145 GLU ALA PHE SER GLN ALA ILE TRP ARG ALA THR PHE ALA SEQRES 4 J 145 GLN VAL PRO GLU SER ARG SER LEU PHE LYS ARG VAL HIS SEQRES 5 J 145 GLY ASP ASP THR SER HIS PRO ALA PHE ILE ALA HIS ALA SEQRES 6 J 145 ASP ARG VAL LEU GLY GLY LEU ASP ILE ALA ILE SER THR SEQRES 7 J 145 LEU ASP GLN PRO ALA THR LEU LYS GLU GLU LEU ASP HIS SEQRES 8 J 145 LEU GLN VAL GLN HIS GLU GLY ARG LYS ILE PRO ASP ASN SEQRES 9 J 145 TYR PHE ASP ALA PHE LYS THR ALA ILE LEU HIS VAL VAL SEQRES 10 J 145 ALA ALA GLN LEU GLY ARG CYS TYR ASP ARG GLU ALA TRP SEQRES 11 J 145 ASP ALA CYS ILE ASP HIS ILE GLU ASP GLY ILE LYS GLY SEQRES 12 J 145 HIS HIS SEQRES 1 K 153 ASP GLU HIS GLU HIS CYS CYS SER GLU GLU ASP HIS ARG SEQRES 2 K 153 ILE VAL GLN LYS GLN TRP ASP ILE LEU TRP ARG ASP THR SEQRES 3 K 153 GLU SER SER LYS ILE LYS ILE GLY PHE GLY ARG LEU LEU SEQRES 4 K 153 LEU THR LYS LEU ALA LYS ASP ILE PRO GLU VAL ASN ASP SEQRES 5 K 153 LEU PHE LYS ARG VAL ASP ILE GLU HIS ALA GLU GLY PRO SEQRES 6 K 153 LYS PHE SER ALA HIS ALA LEU ARG ILE LEU ASN GLY LEU SEQRES 7 K 153 ASP LEU ALA ILE ASN LEU LEU ASP ASP PRO PRO ALA LEU SEQRES 8 K 153 ASP ALA ALA LEU ASP HIS LEU ALA HIS GLN HIS GLU VAL SEQRES 9 K 153 ARG GLU GLY VAL GLN LYS ALA HIS PHE LYS LYS PHE GLY SEQRES 10 K 153 GLU ILE LEU ALA THR GLY LEU PRO GLN VAL LEU ASP ASP SEQRES 11 K 153 TYR ASP ALA LEU ALA TRP LYS SER CYS LEU LYS GLY ILE SEQRES 12 K 153 LEU THR LYS ILE SER SER ARG LEU ASN ALA SEQRES 1 L 140 GLU CYS LEU VAL THR GLU SER LEU LYS VAL LYS LEU GLN SEQRES 2 L 140 TRP ALA SER ALA PHE GLY HIS ALA HIS GLU ARG VAL ALA SEQRES 3 L 140 PHE GLY LEU GLU LEU TRP ARG ASP ILE ILE ASP ASP HIS SEQRES 4 L 140 PRO GLU ILE LYS ALA PRO PHE SER ARG VAL ARG GLY ASP SEQRES 5 L 140 ASN ILE TYR SER PRO GLU PHE GLY ALA HIS SER GLN ARG SEQRES 6 L 140 VAL LEU SER GLY LEU ASP ILE THR ILE SER MET LEU ASP SEQRES 7 L 140 THR PRO ASP MET LEU ALA ALA GLN LEU ALA HIS LEU LYS SEQRES 8 L 140 VAL GLN HIS VAL GLU ARG ASN LEU LYS PRO GLU PHE PHE SEQRES 9 L 140 ASP ILE PHE LEU LYS HIS LEU LEU HIS VAL LEU GLY ASP SEQRES 10 L 140 ARG LEU GLY THR HIS PHE ASP PHE GLY ALA TRP HIS ASP SEQRES 11 L 140 CYS VAL ASP GLN ILE ILE ASP GLY ILE LYS HET PO4 1 5 HET PO4 2 5 HET PO4 3 5 HET HEM A 160 43 HET CMO 1161 2 HET HEM B 160 43 HET CMO 1162 2 HET HEM C 160 43 HET CMO 1163 2 HET HEM D 160 43 HET CMO 1164 2 HET HEM E 160 43 HET CMO 2161 2 HET HEM F 160 43 HET CMO 2162 2 HET HEM G 160 43 HET CMO 2163 2 HET HEM H 160 43 HET CMO 2164 2 HET HEM I 160 43 HET CMO 3161 2 HET HEM J 160 43 HET CMO 3162 2 HET HEM K 160 43 HET CMO 3163 2 HET HEM L 160 43 HET CMO 3164 2 HETNAM PO4 PHOSPHATE ION HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE HETNAM CMO CARBON MONOXIDE HETSYN HEM HEME FORMUL 13 PO4 3(O4 P 3-) FORMUL 16 HEM 12(C34 H32 FE N4 O4) FORMUL 17 CMO 12(C O) FORMUL 40 HOH *264(H2 O) HELIX 1 1 SER A 8 TRP A 23 1 16 HELIX 2 2 THR A 28 TYR A 46 1 19 HELIX 3 3 PRO A 47 GLU A 54 5 8 HELIX 4 4 GLY A 64 ASN A 82 1 19 HELIX 5 5 ASP A 86 GLN A 103 1 18 HELIX 6 6 THR A 108 LEU A 127 1 20 HELIX 7 7 ASN A 131 ALA A 147 1 17 HELIX 8 8 GLY B 5 GLY B 21 1 17 HELIX 9 9 SER B 22 VAL B 41 1 20 HELIX 10 10 PRO B 42 HIS B 52 5 11 HELIX 11 11 HIS B 58 THR B 78 1 21 HELIX 12 12 GLN B 81 GLU B 97 1 17 HELIX 13 13 PRO B 102 GLY B 122 1 21 HELIX 14 14 ASP B 126 GLY B 143 1 18 HELIX 15 15 SER C 8 ILE C 21 1 14 HELIX 16 16 LEU C 22 ARG C 24 5 3 HELIX 17 17 GLU C 27 ILE C 47 1 21 HELIX 18 18 GLU C 49 PHE C 54 1 6 HELIX 19 19 LYS C 55 ALA C 62 5 8 HELIX 20 20 GLY C 64 LEU C 84 1 21 HELIX 21 21 ASP C 87 VAL C 104 1 18 HELIX 22 22 GLN C 109 LEU C 128 1 20 HELIX 23 23 ASP C 132 SER C 149 1 18 HELIX 24 24 LEU D 3 GLY D 19 1 17 HELIX 25 25 HIS D 20 HIS D 39 1 20 HELIX 26 26 PRO D 40 ARG D 50 5 11 HELIX 27 27 SER D 56 MET D 76 1 21 HELIX 28 28 THR D 79 GLU D 96 1 18 HELIX 29 29 LYS D 100 GLY D 120 1 21 HELIX 30 30 THR D 121 PHE D 123 5 3 HELIX 31 31 ASP D 124 LYS D 140 1 17 HELIX 32 32 SER E 8 TRP E 23 1 16 HELIX 33 33 THR E 28 TYR E 46 1 19 HELIX 34 34 PRO E 47 GLU E 54 5 8 HELIX 35 35 GLY E 64 ASN E 82 1 19 HELIX 36 36 ASP E 86 GLN E 103 1 18 HELIX 37 37 THR E 108 LEU E 127 1 20 HELIX 38 38 ASN E 131 ALA E 147 1 17 HELIX 39 39 GLY F 5 GLY F 21 1 17 HELIX 40 40 SER F 22 VAL F 41 1 20 HELIX 41 41 PRO F 42 HIS F 52 5 11 HELIX 42 42 HIS F 58 THR F 78 1 21 HELIX 43 43 GLN F 81 GLU F 97 1 17 HELIX 44 44 PRO F 102 GLY F 122 1 21 HELIX 45 45 ASP F 126 GLY F 143 1 18 HELIX 46 46 SER G 8 ILE G 21 1 14 HELIX 47 47 LEU G 22 ARG G 24 5 3 HELIX 48 48 GLU G 27 ILE G 47 1 21 HELIX 49 49 GLU G 49 PHE G 54 1 6 HELIX 50 50 LYS G 55 ALA G 62 5 8 HELIX 51 51 GLY G 64 LEU G 84 1 21 HELIX 52 52 ASP G 87 VAL G 104 1 18 HELIX 53 53 GLN G 109 LEU G 124 1 16 HELIX 54 54 ASP G 132 SER G 149 1 18 HELIX 55 55 LEU H 3 GLY H 19 1 17 HELIX 56 56 HIS H 20 HIS H 39 1 20 HELIX 57 57 PRO H 40 ARG H 50 5 11 HELIX 58 58 SER H 56 MET H 76 1 21 HELIX 59 59 THR H 79 VAL H 95 1 17 HELIX 60 60 PRO H 101 GLY H 120 1 20 HELIX 61 61 THR H 121 PHE H 123 5 3 HELIX 62 62 ASP H 124 LYS H 140 1 17 HELIX 63 63 SER I 8 TRP I 23 1 16 HELIX 64 64 THR I 28 TYR I 46 1 19 HELIX 65 65 PRO I 47 GLU I 54 5 8 HELIX 66 66 GLY I 64 ASN I 82 1 19 HELIX 67 67 ASP I 86 GLN I 103 1 18 HELIX 68 68 THR I 108 LEU I 127 1 20 HELIX 69 69 ASN I 131 ALA I 147 1 17 HELIX 70 70 GLY J 5 GLY J 21 1 17 HELIX 71 71 SER J 22 VAL J 41 1 20 HELIX 72 72 PRO J 42 HIS J 52 5 11 HELIX 73 73 HIS J 58 THR J 78 1 21 HELIX 74 74 GLN J 81 GLU J 97 1 17 HELIX 75 75 PRO J 102 GLY J 122 1 21 HELIX 76 76 ASP J 126 GLY J 143 1 18 HELIX 77 77 SER K 8 ILE K 21 1 14 HELIX 78 78 LEU K 22 ARG K 24 5 3 HELIX 79 79 GLU K 27 ILE K 47 1 21 HELIX 80 80 GLU K 49 PHE K 54 1 6 HELIX 81 81 ASP K 58 ALA K 62 5 5 HELIX 82 82 GLY K 64 ASN K 83 1 20 HELIX 83 83 ASP K 87 VAL K 104 1 18 HELIX 84 84 GLN K 109 LEU K 128 1 20 HELIX 85 85 ASP K 132 SER K 149 1 18 HELIX 86 86 LEU L 3 GLY L 19 1 17 HELIX 87 87 HIS L 20 HIS L 39 1 20 HELIX 88 88 PRO L 40 ARG L 50 5 11 HELIX 89 89 SER L 56 MET L 76 1 21 HELIX 90 90 THR L 79 GLU L 96 1 18 HELIX 91 91 PRO L 101 GLY L 120 1 20 HELIX 92 92 THR L 121 PHE L 123 5 3 HELIX 93 93 ASP L 124 LYS L 140 1 17 SSBOND 1 CYS A 6 CYS G 6 SSBOND 2 CYS A 7 CYS A 138 SSBOND 3 CYS A 129 CYS B 124 SSBOND 4 CYS B 4 CYS B 133 SSBOND 5 CYS C 6 CYS I 6 SSBOND 6 CYS C 7 CYS C 139 SSBOND 7 CYS D 2 CYS D 131 SSBOND 8 CYS E 6 CYS K 6 SSBOND 9 CYS E 7 CYS E 138 SSBOND 10 CYS F 4 CYS F 133 SSBOND 11 CYS G 7 CYS G 139 SSBOND 12 CYS H 2 CYS H 131 SSBOND 13 CYS I 7 CYS I 138 SSBOND 14 CYS I 129 CYS J 124 SSBOND 15 CYS J 4 CYS J 133 SSBOND 16 CYS K 7 CYS K 139 SSBOND 17 CYS L 2 CYS L 131 LINK NE2 HIS A 101 FE HEM A 160 LINK NE2 HIS E 101 FE HEM E 160 LINK NE2 HIS I 101 FE HEM I 160 LINK NE2 HIS B 96 FE HEM B 160 LINK NE2 HIS F 96 FE HEM F 160 LINK NE2 HIS J 96 FE HEM J 160 LINK NE2 HIS C 102 FE HEM C 160 LINK NE2 HIS G 102 FE HEM G 160 LINK NE2 HIS K 102 FE HEM K 160 LINK NE2 HIS D 94 FE HEM D 160 LINK NE2 HIS H 94 FE HEM H 160 LINK NE2 HIS L 94 FE HEM L 160 CRYST1 139.225 172.071 202.886 90.00 90.00 90.00 C 2 2 21 24 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 0.007183 0.000000 0.000000 0.00000 SCALE2 0.000000 0.005812 0.000000 0.00000 SCALE3 0.000000 0.000000 0.004929 0.00000