HEADER OXYGEN STORAGE/TRANSPORT 17-DEC-02 1NGK TITLE CRYSTALLOGRAPHIC STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS TITLE 2 HEMOGLOBIN O COMPND MOL_ID: 1; COMPND 2 MOLECULE: HEMOGLOBIN-LIKE PROTEIN HBO; COMPND 3 CHAIN: A, B, C, D, E, F, G, H, I, J, K, L; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS; SOURCE 3 ORGANISM_COMMON: BACTERIA; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_COMMON: BACTERIA KEYWDS TRUNCATED HEMOGLOBIN EXPDTA X-RAY DIFFRACTION AUTHOR M.MILANI,P.-Y.SAVARD,H.OULLET,P.ASCENZI,M.GUERTIN, AUTHOR 2 M.BOLOGNESI REVDAT 1 20-MAY-03 1NGK 0 JRNL AUTH M.MILANI,P.-Y.SAVARD,H.OULLET,P.ASCENZI,M.GUERTIN, JRNL AUTH 2 M.BOLOGNESI JRNL TITL A TYRCD1/TRPG8 HYDROGEN BOND NETWORK AND A JRNL TITL 2 TYRB10-TYRCD1 COVALENT LINK SHAPE THE HEME DISTAL JRNL TITL 3 SITE OF MYCOBACTERIUM TUBERCULOSIS HEMOGLOBIN O JRNL REF PROC.NATL.ACAD.SCI.USA V. 100 5766 2003 JRNL REFN ASTM PNASA6 US ISSN 0027-8424 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 2.11 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.1.19 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) : 2.11 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7 REMARK 3 NUMBER OF REFLECTIONS : 131238 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) : 0.188 REMARK 3 R VALUE (WORKING SET) : 0.186 REMARK 3 FREE R VALUE : 0.226 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 6934 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH : 2.11 REMARK 3 BIN RESOLUTION RANGE LOW : 2.17 REMARK 3 REFLECTION IN BIN (WORKING SET) : 9483 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 BIN R VALUE (WORKING SET) : 0.2190 REMARK 3 BIN FREE R VALUE SET COUNT : 508 REMARK 3 BIN FREE R VALUE : 0.2750 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 ALL ATOMS : 15104 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.36 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.09000 REMARK 3 B22 (A**2) : 0.09000 REMARK 3 B33 (A**2) : -0.19000 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): 0.181 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.163 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.945 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.924 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 13599 ; 0.010 ; 0.021 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 18590 ; 1.250 ; 2.066 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1561 ; 4.565 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1810 ; 0.086 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 10808 ; 0.011 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 1473 ; 0.145 ; 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): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 35 ; 0.139 ; 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): 7796 ; 1.070 ; 2.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 12457 ; 1.985 ; 4.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 5803 ; 2.531 ; 4.500 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 6133 ; 3.608 ; 6.000 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 : 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 : BABINET MODEL WITH MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.40 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1NGK 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 RCSB017850. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 07-AUG-2001; 21-FEB-2002; 21- REMARK 200 FEB-2002; 21-FEB-2002 REMARK 200 TEMPERATURE (KELVIN) : 100; 100; 100; 100 REMARK 200 PH : 7.25 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y; Y; Y; Y REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG; ESRF; REMARK 200 ESRF; ESRF REMARK 200 BEAMLINE : BW7B; ID29; ID29; ID29 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M REMARK 200 WAVELENGTH OR RANGE (A) : 0.8456; 1.7387; 1.7404; 0.9801 REMARK 200 MONOCHROMATOR : TRIANGULAR MONOCHROMATOR; REMARK 200 CHANNEL - CUT SI MONOCHROMATOR REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE; CCD; CCD; CCD REMARK 200 DETECTOR MANUFACTURER : MAR IP 345 MM; MARRESEARCH; REMARK 200 MARRESEARCH; MARRESEARCH REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA) REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 131238 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.110 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7 REMARK 200 DATA REDUNDANCY : 3.000 REMARK 200 R MERGE (I) : 0.08100 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 16.0000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.11 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.15 REMARK 200 COMPLETENESS FOR SHELL (%) : 97.5 REMARK 200 DATA REDUNDANCY IN SHELL : 1.50 REMARK 200 R MERGE FOR SHELL (I) : 0.48900 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 2.800 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; MAD REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD REMARK 200 SOFTWARE USED: SOLVE REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 56.38 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.84 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULPHATE, PH 7.25, VAPOR REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 277K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41 2 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 1/2-X,1/2-Y,1/2+Z REMARK 290 3555 -Y,1/2+X,1/4+Z REMARK 290 4555 1/2+Y,-X,3/4+Z REMARK 290 5555 1/2-X,Y,3/4-Z REMARK 290 6555 X,1/2-Y,1/4-Z REMARK 290 7555 1/2+Y,1/2+X,1/2-Z REMARK 290 8555 -Y,-X,-Z REMARK 290 9555 1/2+X,1/2+Y,1/2+Z REMARK 290 10555 1-X,1-Y,1+Z REMARK 290 11555 1/2-Y,1+X,3/4+Z REMARK 290 12555 1+Y,1/2-X,5/4+Z REMARK 290 13555 1-X,1/2+Y,5/4-Z REMARK 290 14555 1/2+X,1-Y,3/4-Z REMARK 290 15555 1+Y,1+X,1-Z REMARK 290 16555 1/2-Y,1/2-X,1/2-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 93.51700 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 93.51700 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 137.43050 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 93.51700 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 68.71525 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 93.51700 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 206.14575 REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 93.51700 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 206.14575 REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 93.51700 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 68.71525 REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 93.51700 REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 93.51700 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 137.43050 REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 9 1.000000 0.000000 0.000000 93.51700 REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 93.51700 REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 137.43050 REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 187.03400 REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 187.03400 REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 274.86100 REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 93.51700 REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 187.03400 REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 206.14575 REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 187.03400 REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 93.51700 REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 343.57625 REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 187.03400 REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 93.51700 REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 343.57625 REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 93.51700 REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 187.03400 REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 206.14575 REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 187.03400 REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 187.03400 REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 274.86100 REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 93.51700 REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 93.51700 REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 137.43050 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 MET A 1 REMARK 465 PRO A 2 REMARK 465 MET B 1 REMARK 465 MET C 1 REMARK 465 PRO C 2 REMARK 465 MET D 1 REMARK 465 PRO D 2 REMARK 465 MET E 1 REMARK 465 MET F 1 REMARK 465 PRO F 2 REMARK 465 MET G 1 REMARK 465 MET H 1 REMARK 465 MET I 1 REMARK 465 MET J 1 REMARK 465 MET K 1 REMARK 465 MET L 1 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 OD1 ASP B 40 O HOH 1501 1.81 REMARK 500 OH TYR I 23 CE2 TYR I 36 2.17 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 K 69 C ARG K 70 N 0.076 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 PRO A 37 CA - N - CD ANGL. DEV. =-17.3 DEGREES REMARK 500 GLU A 38 N - CA - C ANGL. DEV. = 16.5 DEGREES REMARK 500 GLU A 38 CA - C - N ANGL. DEV. = 10.3 DEGREES REMARK 500 PRO B 37 CA - N - CD ANGL. DEV. =-17.7 DEGREES REMARK 500 PRO B 37 CA - N - CD ANGL. DEV. =-11.9 DEGREES REMARK 500 PRO B 37 N - CA - C ANGL. DEV. = 10.7 DEGREES REMARK 500 PRO B 37 C - N - CD ANGL. DEV. =-10.6 DEGREES REMARK 500 GLU B 38 N - CA - C ANGL. DEV. = 13.6 DEGREES REMARK 500 GLU B 38 C - N - CA ANGL. DEV. = 9.6 DEGREES REMARK 500 GLU B 38 CA - C - N ANGL. DEV. = 9.3 DEGREES REMARK 500 ASP B 39 C - N - CA ANGL. DEV. = -9.6 DEGREES REMARK 500 PRO C 37 CA - N - CD ANGL. DEV. = -8.8 DEGREES REMARK 500 PRO C 37 CB - CA - C ANGL. DEV. = 9.0 DEGREES REMARK 500 GLU C 38 N - CA - C ANGL. DEV. = 15.9 DEGREES REMARK 500 GLU C 38 CA - C - N ANGL. DEV. = 9.0 DEGREES REMARK 500 PRO D 37 CA - N - CD ANGL. DEV. = -8.7 DEGREES REMARK 500 PRO D 37 CB - CA - C ANGL. DEV. = 9.1 DEGREES REMARK 500 GLU D 38 N - CA - C ANGL. DEV. = 16.0 DEGREES REMARK 500 GLU D 38 CA - C - N ANGL. DEV. = 8.9 DEGREES REMARK 500 PRO E 2 CA - N - CD ANGL. DEV. =-15.4 DEGREES REMARK 500 PRO E 37 CA - N - CD ANGL. DEV. =-10.9 DEGREES REMARK 500 PRO E 37 CA - N - CD ANGL. DEV. =-15.0 DEGREES REMARK 500 PRO E 37 CA - CB - CG ANGL. DEV. = -8.6 DEGREES REMARK 500 GLU E 38 N - CA - C ANGL. DEV. = 13.9 DEGREES REMARK 500 GLU E 38 CA - C - N ANGL. DEV. = 9.8 DEGREES REMARK 500 ASP E 39 C - N - CA ANGL. DEV. = -9.6 DEGREES REMARK 500 PRO F 37 CA - N - CD ANGL. DEV. =-13.5 DEGREES REMARK 500 GLU F 38 N - CA - C ANGL. DEV. = 15.5 DEGREES REMARK 500 GLU F 38 CA - C - N ANGL. DEV. = 9.0 DEGREES REMARK 500 PRO J 2 CA - N - CD ANGL. DEV. =-22.7 DEGREES REMARK 500 GLN K 65 OE1 - CD - NE2 ANGL. DEV. =-10.0 DEGREES REMARK 500 GLN K 65 CG - CD - NE2 ANGL. DEV. = 9.7 DEGREES REMARK 500 PRO K 69 CA - N - CD ANGL. DEV. =-13.7 DEGREES REMARK 500 PRO L 2 CA - N - CD ANGL. DEV. =-17.0 DEGREES REMARK 500 LYS L 3 C - N - CA ANGL. DEV. = -9.8 DEGREES REMARK 500 PRO L 37 CA - N - CD ANGL. DEV. =-15.8 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 GLU B 38 -37.69 37.36 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 1492 DISTANCE = 5.84 ANGSTROMS REMARK 525 HOH 1531 DISTANCE = 6.77 ANGSTROMS DBREF 1NGK A 1 128 UNP P0A595 GLBO_MYCTU 1 128 DBREF 1NGK B 1 128 UNP P0A595 GLBO_MYCTU 1 128 DBREF 1NGK C 1 128 UNP P0A595 GLBO_MYCTU 1 128 DBREF 1NGK D 1 128 UNP P0A595 GLBO_MYCTU 1 128 DBREF 1NGK E 1 128 UNP P0A595 GLBO_MYCTU 1 128 DBREF 1NGK F 1 128 UNP P0A595 GLBO_MYCTU 1 128 DBREF 1NGK G 1 128 UNP P0A595 GLBO_MYCTU 1 128 DBREF 1NGK H 1 128 UNP P0A595 GLBO_MYCTU 1 128 DBREF 1NGK I 1 128 UNP P0A595 GLBO_MYCTU 1 128 DBREF 1NGK J 1 128 UNP P0A595 GLBO_MYCTU 1 128 DBREF 1NGK K 1 128 UNP P0A595 GLBO_MYCTU 1 128 DBREF 1NGK L 1 128 UNP P0A595 GLBO_MYCTU 1 128 SEQRES 1 A 128 MET PRO LYS SER PHE TYR ASP ALA VAL GLY GLY ALA LYS SEQRES 2 A 128 THR PHE ASP ALA ILE VAL SER ARG PHE TYR ALA GLN VAL SEQRES 3 A 128 ALA GLU ASP GLU VAL LEU ARG ARG VAL TYR PRO GLU ASP SEQRES 4 A 128 ASP LEU ALA GLY ALA GLU GLU ARG LEU ARG MET PHE LEU SEQRES 5 A 128 GLU GLN TYR TRP GLY GLY PRO ARG THR TYR SER GLU GLN SEQRES 6 A 128 ARG GLY HIS PRO ARG LEU ARG MET ARG HIS ALA PRO PHE SEQRES 7 A 128 ARG ILE SER LEU ILE GLU ARG ASP ALA TRP LEU ARG CYS SEQRES 8 A 128 MET HIS THR ALA VAL ALA SER ILE ASP SER GLU THR LEU SEQRES 9 A 128 ASP ASP GLU HIS ARG ARG GLU LEU LEU ASP TYR LEU GLU SEQRES 10 A 128 MET ALA ALA HIS SER LEU VAL ASN SER PRO PHE SEQRES 1 B 128 MET PRO LYS SER PHE TYR ASP ALA VAL GLY GLY ALA LYS SEQRES 2 B 128 THR PHE ASP ALA ILE VAL SER ARG PHE TYR ALA GLN VAL SEQRES 3 B 128 ALA GLU ASP GLU VAL LEU ARG ARG VAL TYR PRO GLU ASP SEQRES 4 B 128 ASP LEU ALA GLY ALA GLU GLU ARG LEU ARG MET PHE LEU SEQRES 5 B 128 GLU GLN TYR TRP GLY GLY PRO ARG THR TYR SER GLU GLN SEQRES 6 B 128 ARG GLY HIS PRO ARG LEU ARG MET ARG HIS ALA PRO PHE SEQRES 7 B 128 ARG ILE SER LEU ILE GLU ARG ASP ALA TRP LEU ARG CYS SEQRES 8 B 128 MET HIS THR ALA VAL ALA SER ILE ASP SER GLU THR LEU SEQRES 9 B 128 ASP ASP GLU HIS ARG ARG GLU LEU LEU ASP TYR LEU GLU SEQRES 10 B 128 MET ALA ALA HIS SER LEU VAL ASN SER PRO PHE SEQRES 1 C 128 MET PRO LYS SER PHE TYR ASP ALA VAL GLY GLY ALA LYS SEQRES 2 C 128 THR PHE ASP ALA ILE VAL SER ARG PHE TYR ALA GLN VAL SEQRES 3 C 128 ALA GLU ASP GLU VAL LEU ARG ARG VAL TYR PRO GLU ASP SEQRES 4 C 128 ASP LEU ALA GLY ALA GLU GLU ARG LEU ARG MET PHE LEU SEQRES 5 C 128 GLU GLN TYR TRP GLY GLY PRO ARG THR TYR SER GLU GLN SEQRES 6 C 128 ARG GLY HIS PRO ARG LEU ARG MET ARG HIS ALA PRO PHE SEQRES 7 C 128 ARG ILE SER LEU ILE GLU ARG ASP ALA TRP LEU ARG CYS SEQRES 8 C 128 MET HIS THR ALA VAL ALA SER ILE ASP SER GLU THR LEU SEQRES 9 C 128 ASP ASP GLU HIS ARG ARG GLU LEU LEU ASP TYR LEU GLU SEQRES 10 C 128 MET ALA ALA HIS SER LEU VAL ASN SER PRO PHE SEQRES 1 D 128 MET PRO LYS SER PHE TYR ASP ALA VAL GLY GLY ALA LYS SEQRES 2 D 128 THR PHE ASP ALA ILE VAL SER ARG PHE TYR ALA GLN VAL SEQRES 3 D 128 ALA GLU ASP GLU VAL LEU ARG ARG VAL TYR PRO GLU ASP SEQRES 4 D 128 ASP LEU ALA GLY ALA GLU GLU ARG LEU ARG MET PHE LEU SEQRES 5 D 128 GLU GLN TYR TRP GLY GLY PRO ARG THR TYR SER GLU GLN SEQRES 6 D 128 ARG GLY HIS PRO ARG LEU ARG MET ARG HIS ALA PRO PHE SEQRES 7 D 128 ARG ILE SER LEU ILE GLU ARG ASP ALA TRP LEU ARG CYS SEQRES 8 D 128 MET HIS THR ALA VAL ALA SER ILE ASP SER GLU THR LEU SEQRES 9 D 128 ASP ASP GLU HIS ARG ARG GLU LEU LEU ASP TYR LEU GLU SEQRES 10 D 128 MET ALA ALA HIS SER LEU VAL ASN SER PRO PHE SEQRES 1 E 128 MET PRO LYS SER PHE TYR ASP ALA VAL GLY GLY ALA LYS SEQRES 2 E 128 THR PHE ASP ALA ILE VAL SER ARG PHE TYR ALA GLN VAL SEQRES 3 E 128 ALA GLU ASP GLU VAL LEU ARG ARG VAL TYR PRO GLU ASP SEQRES 4 E 128 ASP LEU ALA GLY ALA GLU GLU ARG LEU ARG MET PHE LEU SEQRES 5 E 128 GLU GLN TYR TRP GLY GLY PRO ARG THR TYR SER GLU GLN SEQRES 6 E 128 ARG GLY HIS PRO ARG LEU ARG MET ARG HIS ALA PRO PHE SEQRES 7 E 128 ARG ILE SER LEU ILE GLU ARG ASP ALA TRP LEU ARG CYS SEQRES 8 E 128 MET HIS THR ALA VAL ALA SER ILE ASP SER GLU THR LEU SEQRES 9 E 128 ASP ASP GLU HIS ARG ARG GLU LEU LEU ASP TYR LEU GLU SEQRES 10 E 128 MET ALA ALA HIS SER LEU VAL ASN SER PRO PHE SEQRES 1 F 128 MET PRO LYS SER PHE TYR ASP ALA VAL GLY GLY ALA LYS SEQRES 2 F 128 THR PHE ASP ALA ILE VAL SER ARG PHE TYR ALA GLN VAL SEQRES 3 F 128 ALA GLU ASP GLU VAL LEU ARG ARG VAL TYR PRO GLU ASP SEQRES 4 F 128 ASP LEU ALA GLY ALA GLU GLU ARG LEU ARG MET PHE LEU SEQRES 5 F 128 GLU GLN TYR TRP GLY GLY PRO ARG THR TYR SER GLU GLN SEQRES 6 F 128 ARG GLY HIS PRO ARG LEU ARG MET ARG HIS ALA PRO PHE SEQRES 7 F 128 ARG ILE SER LEU ILE GLU ARG ASP ALA TRP LEU ARG CYS SEQRES 8 F 128 MET HIS THR ALA VAL ALA SER ILE ASP SER GLU THR LEU SEQRES 9 F 128 ASP ASP GLU HIS ARG ARG GLU LEU LEU ASP TYR LEU GLU SEQRES 10 F 128 MET ALA ALA HIS SER LEU VAL ASN SER PRO PHE SEQRES 1 G 128 MET PRO LYS SER PHE TYR ASP ALA VAL GLY GLY ALA LYS SEQRES 2 G 128 THR PHE ASP ALA ILE VAL SER ARG PHE TYR ALA GLN VAL SEQRES 3 G 128 ALA GLU ASP GLU VAL LEU ARG ARG VAL TYR PRO GLU ASP SEQRES 4 G 128 ASP LEU ALA GLY ALA GLU GLU ARG LEU ARG MET PHE LEU SEQRES 5 G 128 GLU GLN TYR TRP GLY GLY PRO ARG THR TYR SER GLU GLN SEQRES 6 G 128 ARG GLY HIS PRO ARG LEU ARG MET ARG HIS ALA PRO PHE SEQRES 7 G 128 ARG ILE SER LEU ILE GLU ARG ASP ALA TRP LEU ARG CYS SEQRES 8 G 128 MET HIS THR ALA VAL ALA SER ILE ASP SER GLU THR LEU SEQRES 9 G 128 ASP ASP GLU HIS ARG ARG GLU LEU LEU ASP TYR LEU GLU SEQRES 10 G 128 MET ALA ALA HIS SER LEU VAL ASN SER PRO PHE SEQRES 1 H 128 MET PRO LYS SER PHE TYR ASP ALA VAL GLY GLY ALA LYS SEQRES 2 H 128 THR PHE ASP ALA ILE VAL SER ARG PHE TYR ALA GLN VAL SEQRES 3 H 128 ALA GLU ASP GLU VAL LEU ARG ARG VAL TYR PRO GLU ASP SEQRES 4 H 128 ASP LEU ALA GLY ALA GLU GLU ARG LEU ARG MET PHE LEU SEQRES 5 H 128 GLU GLN TYR TRP GLY GLY PRO ARG THR TYR SER GLU GLN SEQRES 6 H 128 ARG GLY HIS PRO ARG LEU ARG MET ARG HIS ALA PRO PHE SEQRES 7 H 128 ARG ILE SER LEU ILE GLU ARG ASP ALA TRP LEU ARG CYS SEQRES 8 H 128 MET HIS THR ALA VAL ALA SER ILE ASP SER GLU THR LEU SEQRES 9 H 128 ASP ASP GLU HIS ARG ARG GLU LEU LEU ASP TYR LEU GLU SEQRES 10 H 128 MET ALA ALA HIS SER LEU VAL ASN SER PRO PHE SEQRES 1 I 128 MET PRO LYS SER PHE TYR ASP ALA VAL GLY GLY ALA LYS SEQRES 2 I 128 THR PHE ASP ALA ILE VAL SER ARG PHE TYR ALA GLN VAL SEQRES 3 I 128 ALA GLU ASP GLU VAL LEU ARG ARG VAL TYR PRO GLU ASP SEQRES 4 I 128 ASP LEU ALA GLY ALA GLU GLU ARG LEU ARG MET PHE LEU SEQRES 5 I 128 GLU GLN TYR TRP GLY GLY PRO ARG THR TYR SER GLU GLN SEQRES 6 I 128 ARG GLY HIS PRO ARG LEU ARG MET ARG HIS ALA PRO PHE SEQRES 7 I 128 ARG ILE SER LEU ILE GLU ARG ASP ALA TRP LEU ARG CYS SEQRES 8 I 128 MET HIS THR ALA VAL ALA SER ILE ASP SER GLU THR LEU SEQRES 9 I 128 ASP ASP GLU HIS ARG ARG GLU LEU LEU ASP TYR LEU GLU SEQRES 10 I 128 MET ALA ALA HIS SER LEU VAL ASN SER PRO PHE SEQRES 1 J 128 MET PRO LYS SER PHE TYR ASP ALA VAL GLY GLY ALA LYS SEQRES 2 J 128 THR PHE ASP ALA ILE VAL SER ARG PHE TYR ALA GLN VAL SEQRES 3 J 128 ALA GLU ASP GLU VAL LEU ARG ARG VAL TYR PRO GLU ASP SEQRES 4 J 128 ASP LEU ALA GLY ALA GLU GLU ARG LEU ARG MET PHE LEU SEQRES 5 J 128 GLU GLN TYR TRP GLY GLY PRO ARG THR TYR SER GLU GLN SEQRES 6 J 128 ARG GLY HIS PRO ARG LEU ARG MET ARG HIS ALA PRO PHE SEQRES 7 J 128 ARG ILE SER LEU ILE GLU ARG ASP ALA TRP LEU ARG CYS SEQRES 8 J 128 MET HIS THR ALA VAL ALA SER ILE ASP SER GLU THR LEU SEQRES 9 J 128 ASP ASP GLU HIS ARG ARG GLU LEU LEU ASP TYR LEU GLU SEQRES 10 J 128 MET ALA ALA HIS SER LEU VAL ASN SER PRO PHE SEQRES 1 K 128 MET PRO LYS SER PHE TYR ASP ALA VAL GLY GLY ALA LYS SEQRES 2 K 128 THR PHE ASP ALA ILE VAL SER ARG PHE TYR ALA GLN VAL SEQRES 3 K 128 ALA GLU ASP GLU VAL LEU ARG ARG VAL TYR PRO GLU ASP SEQRES 4 K 128 ASP LEU ALA GLY ALA GLU GLU ARG LEU ARG MET PHE LEU SEQRES 5 K 128 GLU GLN TYR TRP GLY GLY PRO ARG THR TYR SER GLU GLN SEQRES 6 K 128 ARG GLY HIS PRO ARG LEU ARG MET ARG HIS ALA PRO PHE SEQRES 7 K 128 ARG ILE SER LEU ILE GLU ARG ASP ALA TRP LEU ARG CYS SEQRES 8 K 128 MET HIS THR ALA VAL ALA SER ILE ASP SER GLU THR LEU SEQRES 9 K 128 ASP ASP GLU HIS ARG ARG GLU LEU LEU ASP TYR LEU GLU SEQRES 10 K 128 MET ALA ALA HIS SER LEU VAL ASN SER PRO PHE SEQRES 1 L 128 MET PRO LYS SER PHE TYR ASP ALA VAL GLY GLY ALA LYS SEQRES 2 L 128 THR PHE ASP ALA ILE VAL SER ARG PHE TYR ALA GLN VAL SEQRES 3 L 128 ALA GLU ASP GLU VAL LEU ARG ARG VAL TYR PRO GLU ASP SEQRES 4 L 128 ASP LEU ALA GLY ALA GLU GLU ARG LEU ARG MET PHE LEU SEQRES 5 L 128 GLU GLN TYR TRP GLY GLY PRO ARG THR TYR SER GLU GLN SEQRES 6 L 128 ARG GLY HIS PRO ARG LEU ARG MET ARG HIS ALA PRO PHE SEQRES 7 L 128 ARG ILE SER LEU ILE GLU ARG ASP ALA TRP LEU ARG CYS SEQRES 8 L 128 MET HIS THR ALA VAL ALA SER ILE ASP SER GLU THR LEU SEQRES 9 L 128 ASP ASP GLU HIS ARG ARG GLU LEU LEU ASP TYR LEU GLU SEQRES 10 L 128 MET ALA ALA HIS SER LEU VAL ASN SER PRO PHE HET SO4 2001 5 HET SO4 2002 5 HET SO4 2003 5 HET SO4 2004 5 HET SO4 2005 5 HET SO4 2006 5 HET SO4 2007 5 HET SO4 2008 5 HET SO4 2009 5 HET SO4 2010 5 HET SO4 2011 5 HET SO4 2012 5 HET SO4 2013 5 HET SO4 2014 5 HET SO4 2015 5 HET SO4 2016 5 HET SO4 2017 5 HET SO4 2018 5 HET CYN A 800 2 HET CYN B 800 2 HET CYN C 800 2 HET CYN D 800 2 HET CYN E 800 2 HET CYN F 800 2 HET CYN G 800 2 HET CYN H 800 2 HET CYN I 800 2 HET CYN J 800 2 HET CYN K 800 2 HET CYN L 800 2 HET HEM A 700 43 HET HEM B 700 43 HET HEM C 700 43 HET HEM D 700 43 HET HEM E 700 43 HET HEM F 700 43 HET HEM G 700 43 HET HEM H 700 43 HET HEM I 700 43 HET HEM J 700 43 HET HEM K 700 43 HET HEM L 700 43 HETNAM SO4 SULFATE ION HETNAM CYN CYANIDE ION HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE HETSYN HEM HEME FORMUL 13 SO4 18(O4 S 2-) FORMUL 31 CYN 12(C N 1-) FORMUL 43 HEM 12(C34 H32 FE N4 O4) FORMUL 55 HOH *1618(H2 O) HELIX 1 1 SER A 4 VAL A 9 1 6 HELIX 2 2 GLY A 11 ASP A 29 1 19 HELIX 3 3 ASP A 29 TYR A 36 1 8 HELIX 4 4 LEU A 41 TRP A 56 1 16 HELIX 5 5 ARG A 60 GLY A 67 1 8 HELIX 6 6 ARG A 70 ALA A 76 1 7 HELIX 7 7 SER A 81 SER A 98 1 18 HELIX 8 8 ASP A 105 LEU A 123 1 19 HELIX 9 9 SER B 4 VAL B 9 1 6 HELIX 10 10 GLY B 10 ASP B 29 1 20 HELIX 11 11 VAL B 31 VAL B 35 5 5 HELIX 12 12 LEU B 41 TRP B 56 1 16 HELIX 13 13 ARG B 60 GLY B 67 1 8 HELIX 14 14 ARG B 70 ALA B 76 1 7 HELIX 15 15 SER B 81 SER B 98 1 18 HELIX 16 16 ASP B 105 LEU B 123 1 19 HELIX 17 17 SER C 4 VAL C 9 1 6 HELIX 18 18 GLY C 10 ALA C 27 1 18 HELIX 19 19 ASP C 29 TYR C 36 1 8 HELIX 20 20 LEU C 41 TRP C 56 1 16 HELIX 21 21 ARG C 60 GLY C 67 1 8 HELIX 22 22 ARG C 70 ALA C 76 1 7 HELIX 23 23 SER C 81 ALA C 97 1 17 HELIX 24 24 ASP C 105 VAL C 124 1 20 HELIX 25 25 SER D 4 VAL D 9 1 6 HELIX 26 26 GLY D 10 ASP D 29 1 20 HELIX 27 27 ASP D 29 ARG D 34 1 6 HELIX 28 28 LEU D 41 TRP D 56 1 16 HELIX 29 29 ARG D 60 GLY D 67 1 8 HELIX 30 30 ARG D 70 ALA D 76 1 7 HELIX 31 31 SER D 81 SER D 98 1 18 HELIX 32 32 ASP D 105 LEU D 123 1 19 HELIX 33 33 SER E 4 VAL E 9 1 6 HELIX 34 34 GLY E 10 ASP E 29 1 20 HELIX 35 35 VAL E 31 VAL E 35 5 5 HELIX 36 36 LEU E 41 TRP E 56 1 16 HELIX 37 37 ARG E 60 GLY E 67 1 8 HELIX 38 38 ARG E 70 ALA E 76 1 7 HELIX 39 39 SER E 81 SER E 98 1 18 HELIX 40 40 ASP E 105 LEU E 123 1 19 HELIX 41 41 SER F 4 VAL F 9 1 6 HELIX 42 42 GLY F 10 ASP F 29 1 20 HELIX 43 43 ASP F 29 TYR F 36 1 8 HELIX 44 44 LEU F 41 TRP F 56 1 16 HELIX 45 45 ARG F 60 GLY F 67 1 8 HELIX 46 46 ARG F 70 ALA F 76 1 7 HELIX 47 47 SER F 81 SER F 98 1 18 HELIX 48 48 ASP F 105 LEU F 123 1 19 HELIX 49 49 SER G 4 VAL G 9 1 6 HELIX 50 50 GLY G 10 GLU G 28 1 19 HELIX 51 51 VAL G 31 VAL G 35 5 5 HELIX 52 52 ASP G 40 TRP G 56 1 17 HELIX 53 53 ARG G 60 GLY G 67 1 8 HELIX 54 54 ARG G 70 ALA G 76 1 7 HELIX 55 55 SER G 81 SER G 98 1 18 HELIX 56 56 ASP G 105 LEU G 123 1 19 HELIX 57 57 SER H 4 VAL H 9 1 6 HELIX 58 58 GLY H 10 GLU H 28 1 19 HELIX 59 59 VAL H 31 VAL H 35 5 5 HELIX 60 60 ASP H 40 TRP H 56 1 17 HELIX 61 61 ARG H 60 GLY H 67 1 8 HELIX 62 62 ARG H 70 ALA H 76 1 7 HELIX 63 63 SER H 81 SER H 98 1 18 HELIX 64 64 ASP H 105 LEU H 123 1 19 HELIX 65 65 SER I 4 VAL I 9 1 6 HELIX 66 66 GLY I 10 GLU I 28 1 19 HELIX 67 67 VAL I 31 VAL I 35 5 5 HELIX 68 68 ASP I 40 TRP I 56 1 17 HELIX 69 69 ARG I 60 GLY I 67 1 8 HELIX 70 70 ARG I 70 ALA I 76 1 7 HELIX 71 71 SER I 81 SER I 98 1 18 HELIX 72 72 ASP I 105 LEU I 123 1 19 HELIX 73 73 SER J 4 VAL J 9 1 6 HELIX 74 74 GLY J 10 ASP J 29 1 20 HELIX 75 75 VAL J 31 VAL J 35 5 5 HELIX 76 76 ASP J 40 TRP J 56 1 17 HELIX 77 77 ARG J 60 GLY J 67 1 8 HELIX 78 78 ARG J 70 ALA J 76 1 7 HELIX 79 79 SER J 81 SER J 98 1 18 HELIX 80 80 ASP J 105 LEU J 123 1 19 HELIX 81 81 SER K 4 VAL K 9 1 6 HELIX 82 82 GLY K 10 GLU K 28 1 19 HELIX 83 83 VAL K 31 VAL K 35 5 5 HELIX 84 84 ASP K 40 TRP K 56 1 17 HELIX 85 85 ARG K 60 GLY K 67 1 8 HELIX 86 86 ARG K 70 ALA K 76 1 7 HELIX 87 87 SER K 81 SER K 98 1 18 HELIX 88 88 ASP K 105 LEU K 123 1 19 HELIX 89 89 SER L 4 VAL L 9 1 6 HELIX 90 90 GLY L 11 GLU L 28 1 18 HELIX 91 91 VAL L 31 VAL L 35 5 5 HELIX 92 92 PRO L 37 ASP L 39 5 3 HELIX 93 93 ASP L 40 TRP L 56 1 17 HELIX 94 94 ARG L 60 GLY L 67 1 8 HELIX 95 95 ARG L 70 ALA L 76 1 7 HELIX 96 96 SER L 81 SER L 98 1 18 HELIX 97 97 ASP L 105 LEU L 123 1 19 LINK FE HEM A 700 NE2 HIS A 75 LINK FE HEM A 700 C CYN A 800 LINK FE HEM B 700 NE2 HIS B 75 LINK FE HEM B 700 C CYN B 800 LINK FE HEM C 700 NE2 HIS C 75 LINK FE HEM C 700 C CYN C 800 LINK FE HEM D 700 NE2 HIS D 75 LINK FE HEM D 700 C CYN D 800 LINK FE HEM E 700 NE2 HIS E 75 LINK FE HEM E 700 C CYN E 800 LINK FE HEM F 700 NE2 HIS F 75 LINK FE HEM F 700 C CYN F 800 LINK FE HEM G 700 NE2 HIS G 75 LINK FE HEM G 700 C CYN G 800 LINK FE HEM H 700 NE2 HIS H 75 LINK FE HEM H 700 C CYN H 800 LINK FE HEM I 700 NE2 HIS I 75 LINK FE HEM I 700 C CYN I 800 LINK FE HEM J 700 NE2 HIS J 75 LINK FE HEM J 700 C CYN J 800 LINK FE HEM K 700 NE2 HIS K 75 LINK FE HEM K 700 C CYN K 800 LINK FE HEM L 700 NE2 HIS L 75 LINK FE HEM L 700 C CYN L 800 LINK OH TYR A 23 CE2 TYR A 36 LINK OH TYR B 23 CE2 TYR B 36 LINK OH TYR C 23 CE2 TYR C 36 LINK OH TYR D 23 CE2 TYR D 36 LINK OH TYR E 23 CE2 TYR E 36 LINK OH TYR F 23 CE2 TYR F 36 CRYST1 187.034 187.034 274.861 90.00 90.00 90.00 I 41 2 2 192 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 0.005347 0.000000 0.000000 0.00000 SCALE2 0.000000 0.005347 0.000000 0.00000 SCALE3 0.000000 0.000000 0.003638 0.00000