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HEADER OXYGEN TRANSPORT 03-JUL-03 1OJ6 TITLE HUMAN BRAIN NEUROGLOBIN THREE-DIMENSIONAL STRUCTURE COMPND MOL_ID: 1; COMPND 2 MOLECULE: NEUROGLOBIN; COMPND 3 CHAIN: A, B, C, D; COMPND 4 SYNONYM: HEMOGLOBIN; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 SYNTHETIC: YES KEYWDS NEUROGLOBIN, HEME HEXACOORDINATION, OXYGEN TRANSPORT EXPDTA X-RAY DIFFRACTION AUTHOR A.PESCE,S.DEWILDE,M.NARDINI,L.MOENS,P.ASCENZI,T.HANKELN, AUTHOR 2 T.BURMESTER,M.BOLOGNESI REVDAT 1 11-SEP-03 1OJ6 0 JRNL AUTH A.PESCE,S.DEWILDE,M.NARDINI,L.MOENS,P.ASCENZI, JRNL AUTH 2 T.HANKELN,T.BURMESTER,M.BOLOGNESI JRNL TITL HUMAN BRAIN NEUROGLOBIN STRUCTURE REVEALS A JRNL TITL 2 DISTINCT MODE OF CONTROLLING OXYGEN AFFINITY. JRNL REF STRUCTURE V. 11 1087 2003 JRNL REFN ASTM STRUE6 UK ISSN 0969-2126 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 1.95 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 98.5 REMARK 3 NUMBER OF REFLECTIONS : 35871 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) : 0.178 REMARK 3 R VALUE (WORKING SET) : 0.178 REMARK 3 FREE R VALUE : 0.233 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000 REMARK 3 FREE R VALUE TEST SET COUNT : 3604 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 4584 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 207 REMARK 3 SOLVENT ATOMS : NULL REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.00 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): NULL REMARK 3 ESU BASED ON FREE R VALUE (A): 0.180 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 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA REMARK 3 BOND LENGTH (A) : NULL ; NULL REMARK 3 ANGLE DISTANCE (A) : NULL ; NULL REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL REMARK 3 REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL REMARK 3 REMARK 3 NON-BONDED CONTACT RESTRAINTS. REMARK 3 SINGLE TORSION (A) : NULL ; NULL REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL REMARK 3 REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS. REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL REMARK 3 PLANAR (DEGREES) : NULL ; NULL REMARK 3 STAGGERED (DEGREES) : NULL ; NULL REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: SOME ATOMS IN THIS ENTRY HAVE REMARK 3 OCCUPANCY OF 0.00 REMARK 4 REMARK 4 1OJ6 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 (2007-05-31) REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI . REMARK 100 THE EBI ID CODE IS EBI-12979 . REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 15-MAR-2002 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 6.50 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ESRF REMARK 200 BEAMLINE : ID29 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.738, 1.740, 0.933 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : NULL REMARK 200 DETECTOR MANUFACTURER : NULL REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35871 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950 REMARK 200 RESOLUTION RANGE LOW (A) : 40.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.5 REMARK 200 DATA REDUNDANCY : 2.600 REMARK 200 R MERGE (I) : 0.05500 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 17.0000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.98 REMARK 200 COMPLETENESS FOR SHELL (%) : 97.9 REMARK 200 DATA REDUNDANCY IN SHELL : 2.50 REMARK 200 R MERGE FOR SHELL (I) : 0.22000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 5.000 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: 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 (%): 36.00 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.90 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.5 REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -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 47.46350 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2, 3, 4 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, W, X, Y, Z 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 350 BIOMOLECULE: 2 REMARK 350 APPLY THE FOLLOWING TO CHAINS: B 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 350 BIOMOLECULE: 3 REMARK 350 APPLY THE FOLLOWING TO CHAINS: C 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 350 BIOMOLECULE: 4 REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 MET A 1 REMARK 465 GLU A 2 REMARK 465 GLY A 150 REMARK 465 GLU A 151 REMARK 465 MET C 1 REMARK 465 GLU C 2 REMARK 465 ARG C 3 REMARK 465 GLU D 151 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 GLU A 22 CB CG CD OE1 OE2 REMARK 470 TYR A 44 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ARG A 47 CG CD NE CZ NH1 NH2 REMARK 470 GLN A 48 CG CD OE1 NE2 REMARK 470 SER A 50 OG REMARK 470 SER A 51 OG REMARK 470 GLU A 53 CG CD OE1 OE2 REMARK 470 ARG B 47 CG CD NE CZ NH1 NH2 REMARK 470 GLU B 53 CG CD OE1 OE2 REMARK 470 GLU B 151 CG CD OE1 OE2 REMARK 470 ASN C 45 CG OD1 ND2 REMARK 470 GLN C 48 CG CD OE1 NE2 REMARK 470 SER C 51 OG REMARK 470 GLU C 53 CG CD OE1 OE2 REMARK 470 ASP C 54 CG OD1 OD2 REMARK 470 ASP C 149 CG OD1 OD2 REMARK 470 GLU C 151 CG CD OE1 OE2 REMARK 470 MET D 1 CG SD CE REMARK 470 GLU D 2 CG CD OE1 OE2 REMARK 470 TYR D 44 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ASN D 45 CG OD1 ND2 REMARK 470 ARG D 47 CG CD NE CZ NH1 NH2 REMARK 470 SER D 51 OG REMARK 470 PRO D 52 CG CD REMARK 470 GLU D 53 CG CD OE1 OE2 REMARK 470 ASP D 54 CG OD1 OD2 REMARK 470 GLU D 60 CG CD OE1 OE2 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 OE2 GLU B 87 NH1 ARG C 47 1.99 REMARK 500 NE ARG B 94 O GLU B 151 2.02 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 OD1 ASP A 37 OH TYR B 115 2747 2.12 REMARK 500 NH1 ARG D 3 O2 SO4 B 1153 2647 2.14 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 A 6 CD PRO A 6 N 0.066 REMARK 500 PRO A 123 CD PRO A 123 N 0.066 REMARK 500 PRO A 127 CD PRO A 127 N 0.064 REMARK 500 PRO B 36 CD PRO B 36 N 0.066 REMARK 500 PRO B 59 CD PRO B 59 N 0.072 REMARK 500 PRO B 127 CD PRO B 127 N 0.076 REMARK 500 PRO C 4 CD PRO C 4 N 0.071 REMARK 500 PRO C 6 CD PRO C 6 N 0.066 REMARK 500 PRO C 20 CD PRO C 20 N 0.068 REMARK 500 PRO C 36 CD PRO C 36 N 0.064 REMARK 500 PRO C 40 CD PRO C 40 N 0.067 REMARK 500 PRO C 52 CD PRO C 52 N 0.075 REMARK 500 PRO C 59 CD PRO C 59 N 0.064 REMARK 500 PRO C 127 CD PRO C 127 N 0.067 REMARK 500 PRO D 6 CD PRO D 6 N 0.065 REMARK 500 PRO D 127 CD PRO D 127 N 0.065 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 GLN A 11 OE1 - CD - NE2 ANGL. DEV. = -9.8 DEGREES REMARK 500 GLN A 11 CG - CD - NE2 ANGL. DEV. = 10.6 DEGREES REMARK 500 GLN A 43 OE1 - CD - NE2 ANGL. DEV. = -9.9 DEGREES REMARK 500 GLN A 43 CG - CD - NE2 ANGL. DEV. = 10.7 DEGREES REMARK 500 PRO A 52 CA - N - CD ANGL. DEV. =-15.0 DEGREES REMARK 500 GLN A 135 OE1 - CD - NE2 ANGL. DEV. =-10.1 DEGREES REMARK 500 GLN A 135 CG - CD - NE2 ANGL. DEV. = 10.0 DEGREES REMARK 500 GLN A 142 OE1 - CD - NE2 ANGL. DEV. = -9.9 DEGREES REMARK 500 GLN A 142 CG - CD - NE2 ANGL. DEV. = 10.5 DEGREES REMARK 500 GLN B 11 OE1 - CD - NE2 ANGL. DEV. =-10.3 DEGREES REMARK 500 GLN B 11 CG - CD - NE2 ANGL. DEV. = 10.8 DEGREES REMARK 500 PRO B 20 CA - N - CD ANGL. DEV. =-16.2 DEGREES REMARK 500 GLN B 43 OE1 - CD - NE2 ANGL. DEV. =-10.1 DEGREES REMARK 500 GLN B 43 CG - CD - NE2 ANGL. DEV. = 10.5 DEGREES REMARK 500 GLN B 48 OE1 - CD - NE2 ANGL. DEV. =-10.1 DEGREES REMARK 500 GLN B 48 CG - CD - NE2 ANGL. DEV. = 9.3 DEGREES REMARK 500 GLN B 135 OE1 - CD - NE2 ANGL. DEV. = -9.5 DEGREES REMARK 500 GLN B 135 CG - CD - NE2 ANGL. DEV. = 10.1 DEGREES REMARK 500 GLN B 142 OE1 - CD - NE2 ANGL. DEV. =-10.4 DEGREES REMARK 500 GLN B 142 CG - CD - NE2 ANGL. DEV. = 10.5 DEGREES REMARK 500 PRO C 4 CB - CA - C ANGL. DEV. = 9.1 DEGREES REMARK 500 GLN C 11 OE1 - CD - NE2 ANGL. DEV. = -9.9 DEGREES REMARK 500 GLN C 11 CG - CD - NE2 ANGL. DEV. = 10.2 DEGREES REMARK 500 GLN C 43 OE1 - CD - NE2 ANGL. DEV. =-10.5 DEGREES REMARK 500 GLN C 43 CG - CD - NE2 ANGL. DEV. = 10.3 DEGREES REMARK 500 GLN C 135 CG - CD - NE2 ANGL. DEV. = 9.2 DEGREES REMARK 500 GLN C 142 OE1 - CD - NE2 ANGL. DEV. = -9.6 DEGREES REMARK 500 GLN C 142 CG - CD - NE2 ANGL. DEV. = 9.9 DEGREES REMARK 500 GLN D 11 OE1 - CD - NE2 ANGL. DEV. = -9.6 DEGREES REMARK 500 GLN D 11 CG - CD - NE2 ANGL. DEV. = 10.3 DEGREES REMARK 500 GLN D 43 OE1 - CD - NE2 ANGL. DEV. = -9.8 DEGREES REMARK 500 GLN D 43 CG - CD - NE2 ANGL. DEV. = 11.2 DEGREES REMARK 500 GLN D 48 OE1 - CD - NE2 ANGL. DEV. = -9.5 DEGREES REMARK 500 GLN D 48 CG - CD - NE2 ANGL. DEV. = 9.8 DEGREES REMARK 500 GLN D 48 N - CA - C ANGL. DEV. = 14.4 DEGREES REMARK 500 PHE D 49 CB - CA - C ANGL. DEV. = -9.7 DEGREES REMARK 500 GLN D 135 OE1 - CD - NE2 ANGL. DEV. =-10.2 DEGREES REMARK 500 GLN D 135 CG - CD - NE2 ANGL. DEV. = 10.4 DEGREES REMARK 500 GLN D 142 OE1 - CD - NE2 ANGL. DEV. = -9.3 DEGREES REMARK 500 GLN D 142 CG - CD - NE2 ANGL. DEV. = 9.4 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 ARG A 47 167.55 81.79 REMARK 500 TYR D 44 -49.76 58.45 REMARK 500 PHE D 49 167.95 36.65 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 SITE_DESCRIPTION: HEM BINDING SITE FOR CHAIN D DBREF 1OJ6 A 1 151 UNP Q9NPG2 NGB_HUMAN 1 151 DBREF 1OJ6 B 1 151 UNP Q9NPG2 NGB_HUMAN 1 151 DBREF 1OJ6 C 1 151 UNP Q9NPG2 NGB_HUMAN 1 151 DBREF 1OJ6 D 1 151 UNP Q9NPG2 NGB_HUMAN 1 151 SEQADV 1OJ6 GLY A 46 UNP Q9NPG2 CYS 46 ENGINEERED MUTATION SEQADV 1OJ6 SER A 55 UNP Q9NPG2 CYS 55 ENGINEERED MUTATION SEQADV 1OJ6 SER A 120 UNP Q9NPG2 CYS 120 ENGINEERED MUTATION SEQADV 1OJ6 GLY B 46 UNP Q9NPG2 CYS 46 ENGINEERED MUTATION SEQADV 1OJ6 SER B 55 UNP Q9NPG2 CYS 55 ENGINEERED MUTATION SEQADV 1OJ6 SER B 120 UNP Q9NPG2 CYS 120 ENGINEERED MUTATION SEQADV 1OJ6 GLY C 46 UNP Q9NPG2 CYS 46 ENGINEERED MUTATION SEQADV 1OJ6 SER C 55 UNP Q9NPG2 CYS 55 ENGINEERED MUTATION SEQADV 1OJ6 SER C 120 UNP Q9NPG2 CYS 120 ENGINEERED MUTATION SEQADV 1OJ6 GLY D 46 UNP Q9NPG2 CYS 46 ENGINEERED MUTATION SEQADV 1OJ6 SER D 55 UNP Q9NPG2 CYS 55 ENGINEERED MUTATION SEQADV 1OJ6 SER D 120 UNP Q9NPG2 CYS 120 ENGINEERED MUTATION SEQRES 1 A 151 MET GLU ARG PRO GLU PRO GLU LEU ILE ARG GLN SER TRP SEQRES 2 A 151 ARG ALA VAL SER ARG SER PRO LEU GLU HIS GLY THR VAL SEQRES 3 A 151 LEU PHE ALA ARG LEU PHE ALA LEU GLU PRO ASP LEU LEU SEQRES 4 A 151 PRO LEU PHE GLN TYR ASN GLY ARG GLN PHE SER SER PRO SEQRES 5 A 151 GLU ASP SER LEU SER SER PRO GLU PHE LEU ASP HIS ILE SEQRES 6 A 151 ARG LYS VAL MET LEU VAL ILE ASP ALA ALA VAL THR ASN SEQRES 7 A 151 VAL GLU ASP LEU SER SER LEU GLU GLU TYR LEU ALA SER SEQRES 8 A 151 LEU GLY ARG LYS HIS ARG ALA VAL GLY VAL LYS LEU SER SEQRES 9 A 151 SER PHE SER THR VAL GLY GLU SER LEU LEU TYR MET LEU SEQRES 10 A 151 GLU LYS SER LEU GLY PRO ALA PHE THR PRO ALA THR ARG SEQRES 11 A 151 ALA ALA TRP SER GLN LEU TYR GLY ALA VAL VAL GLN ALA SEQRES 12 A 151 MET SER ARG GLY TRP ASP GLY GLU SEQRES 1 B 151 MET GLU ARG PRO GLU PRO GLU LEU ILE ARG GLN SER TRP SEQRES 2 B 151 ARG ALA VAL SER ARG SER PRO LEU GLU HIS GLY THR VAL SEQRES 3 B 151 LEU PHE ALA ARG LEU PHE ALA LEU GLU PRO ASP LEU LEU SEQRES 4 B 151 PRO LEU PHE GLN TYR ASN GLY ARG GLN PHE SER SER PRO SEQRES 5 B 151 GLU ASP SER LEU SER SER PRO GLU PHE LEU ASP HIS ILE SEQRES 6 B 151 ARG LYS VAL MET LEU VAL ILE ASP ALA ALA VAL THR ASN SEQRES 7 B 151 VAL GLU ASP LEU SER SER LEU GLU GLU TYR LEU ALA SER SEQRES 8 B 151 LEU GLY ARG LYS HIS ARG ALA VAL GLY VAL LYS LEU SER SEQRES 9 B 151 SER PHE SER THR VAL GLY GLU SER LEU LEU TYR MET LEU SEQRES 10 B 151 GLU LYS SER LEU GLY PRO ALA PHE THR PRO ALA THR ARG SEQRES 11 B 151 ALA ALA TRP SER GLN LEU TYR GLY ALA VAL VAL GLN ALA SEQRES 12 B 151 MET SER ARG GLY TRP ASP GLY GLU SEQRES 1 C 151 MET GLU ARG PRO GLU PRO GLU LEU ILE ARG GLN SER TRP SEQRES 2 C 151 ARG ALA VAL SER ARG SER PRO LEU GLU HIS GLY THR VAL SEQRES 3 C 151 LEU PHE ALA ARG LEU PHE ALA LEU GLU PRO ASP LEU LEU SEQRES 4 C 151 PRO LEU PHE GLN TYR ASN GLY ARG GLN PHE SER SER PRO SEQRES 5 C 151 GLU ASP SER LEU SER SER PRO GLU PHE LEU ASP HIS ILE SEQRES 6 C 151 ARG LYS VAL MET LEU VAL ILE ASP ALA ALA VAL THR ASN SEQRES 7 C 151 VAL GLU ASP LEU SER SER LEU GLU GLU TYR LEU ALA SER SEQRES 8 C 151 LEU GLY ARG LYS HIS ARG ALA VAL GLY VAL LYS LEU SER SEQRES 9 C 151 SER PHE SER THR VAL GLY GLU SER LEU LEU TYR MET LEU SEQRES 10 C 151 GLU LYS SER LEU GLY PRO ALA PHE THR PRO ALA THR ARG SEQRES 11 C 151 ALA ALA TRP SER GLN LEU TYR GLY ALA VAL VAL GLN ALA SEQRES 12 C 151 MET SER ARG GLY TRP ASP GLY GLU SEQRES 1 D 151 MET GLU ARG PRO GLU PRO GLU LEU ILE ARG GLN SER TRP SEQRES 2 D 151 ARG ALA VAL SER ARG SER PRO LEU GLU HIS GLY THR VAL SEQRES 3 D 151 LEU PHE ALA ARG LEU PHE ALA LEU GLU PRO ASP LEU LEU SEQRES 4 D 151 PRO LEU PHE GLN TYR ASN GLY ARG GLN PHE SER SER PRO SEQRES 5 D 151 GLU ASP SER LEU SER SER PRO GLU PHE LEU ASP HIS ILE SEQRES 6 D 151 ARG LYS VAL MET LEU VAL ILE ASP ALA ALA VAL THR ASN SEQRES 7 D 151 VAL GLU ASP LEU SER SER LEU GLU GLU TYR LEU ALA SER SEQRES 8 D 151 LEU GLY ARG LYS HIS ARG ALA VAL GLY VAL LYS LEU SER SEQRES 9 D 151 SER PHE SER THR VAL GLY GLU SER LEU LEU TYR MET LEU SEQRES 10 D 151 GLU LYS SER LEU GLY PRO ALA PHE THR PRO ALA THR ARG SEQRES 11 D 151 ALA ALA TRP SER GLN LEU TYR GLY ALA VAL VAL GLN ALA SEQRES 12 D 151 MET SER ARG GLY TRP ASP GLY GLU HET SO4 B1153 5 HET SO4 B1154 5 HET SO4 B1155 5 HET SO4 B1156 5 HET SO4 C1153 5 HET SO4 C1154 5 HET SO4 C1155 5 HET HEM A1150 43 HET HEM B1152 43 HET HEM C1152 43 HET HEM D1151 43 HETNAM SO4 SULFATE ION HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE HETSYN HEM HEME FORMUL 5 SO4 7(O4 S 2-) FORMUL 12 HEM 4(C34 H32 FE N4 O4) FORMUL 16 HOH *160(H2 O) HELIX 1 1 GLU A 5 ARG A 18 1 14 HELIX 2 2 SER A 19 GLU A 35 1 17 HELIX 3 3 PRO A 36 PHE A 42 5 7 HELIX 4 4 SER A 51 LEU A 56 1 6 HELIX 5 5 SER A 58 ASN A 78 1 21 HELIX 6 6 ASP A 81 SER A 84 5 4 HELIX 7 7 LEU A 85 VAL A 99 1 15 HELIX 8 8 SER A 104 GLY A 122 1 19 HELIX 9 9 PRO A 123 PHE A 125 5 3 HELIX 10 10 THR A 126 SER A 145 1 20 HELIX 11 11 ARG A 146 TRP A 148 5 3 HELIX 12 12 GLU B 5 SER B 17 1 13 HELIX 13 13 SER B 19 GLU B 35 1 17 HELIX 14 14 PRO B 36 PHE B 42 5 7 HELIX 15 15 SER B 51 LEU B 56 1 6 HELIX 16 16 SER B 58 ASN B 78 1 21 HELIX 17 17 ASP B 81 SER B 84 5 4 HELIX 18 18 LEU B 85 ALA B 98 1 14 HELIX 19 19 SER B 104 GLY B 122 1 19 HELIX 20 20 PRO B 123 PHE B 125 5 3 HELIX 21 21 THR B 126 TRP B 148 1 23 HELIX 22 22 GLU C 5 ARG C 18 1 14 HELIX 23 23 SER C 19 GLU C 35 1 17 HELIX 24 24 PRO C 36 PHE C 42 5 7 HELIX 25 25 SER C 51 LEU C 56 1 6 HELIX 26 26 SER C 58 ASN C 78 1 21 HELIX 27 27 ASP C 81 SER C 84 5 4 HELIX 28 28 LEU C 85 VAL C 99 1 15 HELIX 29 29 SER C 104 GLY C 122 1 19 HELIX 30 30 PRO C 123 PHE C 125 5 3 HELIX 31 31 THR C 126 SER C 145 1 20 HELIX 32 32 ARG C 146 TRP C 148 5 3 HELIX 33 33 GLU D 5 SER D 17 1 13 HELIX 34 34 SER D 19 GLU D 35 1 17 HELIX 35 35 PRO D 36 GLN D 43 5 8 HELIX 36 36 SER D 58 ASN D 78 1 21 HELIX 37 37 VAL D 79 SER D 84 5 6 HELIX 38 38 LEU D 85 GLY D 100 1 16 HELIX 39 39 SER D 104 GLY D 122 1 19 HELIX 40 40 PRO D 123 PHE D 125 5 3 HELIX 41 41 THR D 126 SER D 145 1 20 HELIX 42 42 ARG D 146 ASP D 149 5 4 LINK FE HEM A1150 NE2 HIS A 64 LINK FE HEM A1150 NE2 HIS A 96 LINK FE HEM B1152 NE2 HIS B 96 LINK FE HEM B1152 NE2 HIS B 64 LINK FE HEM C1152 NE2 HIS C 64 LINK FE HEM C1152 NE2 HIS C 96 LINK FE HEM D1151 NE2 HIS D 96 LINK FE HEM D1151 NE2 HIS D 64 SITE 1 AC1 7 HIS A 64 LYS A 67 LEU A 92 HIS A 96 SITE 2 AC1 7 PHE A 106 ASP B 73 HOH Z 38 SITE 1 AC2 13 THR A 77 ASN A 78 LEU B 41 PHE B 42 SITE 2 AC2 13 TYR B 44 HIS B 64 LYS B 67 TYR B 88 SITE 3 AC2 13 LEU B 92 LYS B 95 HIS B 96 HOH Y 39 SITE 4 AC2 13 HOH Y 40 SITE 1 AC3 11 LEU C 38 LEU C 41 PHE C 42 TYR C 44 SITE 2 AC3 11 HIS C 64 LYS C 67 LEU C 92 LYS C 95 SITE 3 AC3 11 HIS C 96 PHE C 106 HOH X 32 SITE 1 AC4 7 PHE D 42 HIS D 64 LYS D 67 TYR D 88 SITE 2 AC4 7 LEU D 92 HIS D 96 HOH W 31 CRYST1 39.598 94.927 67.563 90.00 94.38 90.00 P 1 21 1 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 0.025254 0.000000 0.001934 0.00000 SCALE2 0.000000 0.010534 0.000000 0.00000 SCALE3 0.000000 0.000000 0.014844 0.00000