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HEADER OXYGEN STORAGE/TRANSPORT 28-SEP-04 1W92 TITLE THE STRUCTURE OF CARBOMONOXY MURINE NEUROGLOBIN REVEALS A TITLE 2 HEME-SLIDING MECHANISM FOR AFFINITY REGULATION COMPND MOL_ID: 1; COMPND 2 MOLECULE: NEUROGLOBIN; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MUTATION: YES; COMPND 6 OTHER_DETAILS: CARBOMONOXY (CO) DERIVATIVE OF HEME FERROUS COMPND 7 (FE2) NEUROGLOBIN SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: MOUSE; SOURCE 4 ORGAN: BRAIN; SOURCE 5 TISSUE: NERVE; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21; SOURCE 8 EXPRESSION_SYSTEM_VARIANT: DE3(PLYS); SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET3A KEYWDS CARBOMONOXY NEUROGLOBIN, GLOBIN, HEME-SLIDING, OXYGEN KEYWDS 2 STORAGE/TRANSPORT EXPDTA X-RAY DIFFRACTION AUTHOR B.VALLONE,K.NIENHAUS,A.MATTHES,M.BRUNORI,G.U.NIENHAUS REVDAT 3 17-MAR-05 1W92 1 ATOM REVDAT 2 22-DEC-04 1W92 1 JRNL REVDAT 1 02-NOV-04 1W92 0 JRNL AUTH B.VALLONE,K.NIENHAUS,A.MATTHES,M.BRUNORI, JRNL AUTH 2 G.U.NIENHAUS JRNL TITL THE STRUCTURE OF CARBONMONOXY NEUROGLOBIN REVEALS JRNL TITL 2 A HEME-SLIDING MECHANISM FOR CONTROL OF LIGAND JRNL TITL 3 AFFINITY. JRNL REF PROC.NATL.ACAD.SCI.USA V. 101 17351 2004 JRNL REFN ASTM PNASA6 US ISSN 0027-8424 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH B.VALLONE,K.NIENHAUS,M.BRUNORI,G.U.NIENHAUS REMARK 1 TITL THE STRUCTURE OF MURINE NEUROGLOBIN: NOVEL REMARK 1 TITL 2 PATHWAYS FOR LIGAND MIGRATION AND BINDING REMARK 1 REF PROTEINS V. 56 85 2004 REMARK 1 REFN ASTM PSFGEY US ISSN 0887-3585 REMARK 2 REMARK 2 RESOLUTION. 1.70 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5 REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 97.5 REMARK 3 NUMBER OF REFLECTIONS : 882 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHUOT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING + TEST SET) : 0.260 REMARK 3 R VALUE (WORKING SET) : 0.260 REMARK 3 FREE R VALUE : 0.220 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 0.100 REMARK 3 FREE R VALUE TEST SET COUNT : 903 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : NULL REMARK 3 BIN RESOLUTION RANGE HIGH : NULL REMARK 3 BIN RESOLUTION RANGE LOW : NULL REMARK 3 REFLECTION IN BIN (WORKING SET) : NULL REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 BIN R VALUE (WORKING SET) : NULL REMARK 3 BIN FREE R VALUE SET COUNT : NULL REMARK 3 BIN FREE R VALUE : NULL REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 ALL ATOMS : 1322 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 22.80 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.30 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): NULL 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 : NULL REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : NULL REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): NULL ; NULL ; NULL REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): NULL ; NULL ; NULL 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): NULL ; NULL ; NULL REMARK 3 GENERAL PLANES REFINED ATOMS (A): NULL ; NULL ; NULL 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): NULL ; NULL ; NULL 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): NULL ; NULL ; NULL 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 : NULL REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : NULL REMARK 3 ION PROBE RADIUS : NULL REMARK 3 SHRINKAGE RADIUS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE REMARK 3 RIDING POSITIONS. REMARK 4 REMARK 4 1W92 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 3.102 (2007-05-31) REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI . REMARK 100 THE EBI ID CODE IS EBI-21181 . REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 20-OCT-2003 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 7.50 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ELETTRA REMARK 200 BEAMLINE : 5.2R REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1 REMARK 200 MONOCHROMATOR : DOUBLE-CRYSTAL MONOCHROMATOR REMARK 200 (SI(111) AND SI(220) ) REMARK 200 OPTICS : TOROIDAL FOCUSSING MIRROR REMARK 200 WITH A HORIZONTAL ACCEPTANCE REMARK 200 OF 2.8 MRAD REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MAR REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 92704 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700 REMARK 200 RESOLUTION RANGE LOW (A) : 15.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 94.8 REMARK 200 DATA REDUNDANCY : 2.500 REMARK 200 R MERGE (I) : 0.07000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 20.8000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.73 REMARK 200 COMPLETENESS FOR SHELL (%) : 97.5 REMARK 200 DATA REDUNDANCY IN SHELL : 2.39 REMARK 200 R MERGE FOR SHELL (I) : 0.23000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 2.940 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER REMARK 200 SOFTWARE USED: NULL REMARK 200 STARTING MODEL: PDB ENTRY 1Q1F REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 47.16 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.5 REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z REMARK 290 3555 -X+Y,-X,Z REMARK 290 4555 Y,X,-Z REMARK 290 5555 X-Y,-Y,-Z REMARK 290 6555 -X,-X+Y,-Z REMARK 290 7555 2/3+X,1/3+Y,1/3+Z REMARK 290 8555 2/3-Y,1/3+X-Y,1/3+Z REMARK 290 9555 2/3-X+Y,1/3-X,1/3+Z REMARK 290 10555 2/3+Y,1/3+X,1/3-Z REMARK 290 11555 2/3+X-Y,1/3-Y,1/3-Z REMARK 290 12555 2/3-X,1/3-X+Y,1/3-Z REMARK 290 13555 1/3+X,2/3+Y,2/3+Z REMARK 290 14555 1/3-Y,2/3+X-Y,2/3+Z REMARK 290 15555 1/3-X+Y,2/3-X,2/3+Z REMARK 290 16555 1/3+Y,2/3+X,2/3-Z REMARK 290 17555 1/3+X-Y,2/3-Y,2/3-Z REMARK 290 18555 1/3-X,2/3-X+Y,2/3-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 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 4 0.866025 0.500000 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 0.00000 REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 44.18650 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 25.51109 REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 36.99433 REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 44.18650 REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 25.51109 REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 36.99433 REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 44.18650 REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 25.51109 REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 36.99433 REMARK 290 SMTRY1 10 -0.500000 0.866025 0.000000 44.18650 REMARK 290 SMTRY2 10 0.866025 0.500000 0.000000 25.51109 REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 36.99433 REMARK 290 SMTRY1 11 1.000000 0.000000 0.000000 44.18650 REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 25.51109 REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 36.99433 REMARK 290 SMTRY1 12 -0.500000 -0.866025 0.000000 44.18650 REMARK 290 SMTRY2 12 -0.866025 0.500000 0.000000 25.51109 REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 36.99433 REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 51.02218 REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 73.98867 REMARK 290 SMTRY1 14 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 14 0.866025 -0.500000 0.000000 51.02218 REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 73.98867 REMARK 290 SMTRY1 15 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 15 -0.866025 -0.500000 0.000000 51.02218 REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 73.98867 REMARK 290 SMTRY1 16 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 16 0.866025 0.500000 0.000000 51.02218 REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 73.98867 REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 51.02218 REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 73.98867 REMARK 290 SMTRY1 18 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 18 -0.866025 0.500000 0.000000 51.02218 REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 73.98867 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 1 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 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 BIOMT1 2 -0.500000 -0.866025 0.000000 44.18650 REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 76.53326 REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 -44.18650 REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 76.53326 REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 4 -0.500000 0.866025 0.000000 -44.18650 REMARK 350 BIOMT2 4 0.866025 0.500000 0.000000 25.51109 REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 36.99433 REMARK 350 BIOMT1 5 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 5 0.000000 -1.000000 0.000000 102.04435 REMARK 350 BIOMT3 5 0.000000 0.000000 -1.000000 36.99433 REMARK 350 BIOMT1 6 -0.500000 -0.866025 0.000000 44.18650 REMARK 350 BIOMT2 6 -0.866025 0.500000 0.000000 25.51109 REMARK 350 BIOMT3 6 0.000000 0.000000 -1.000000 36.99433 REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 ASP A 149 REMARK 465 GLY A 150 REMARK 465 GLU A 151 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 NE2 HIS A 96 FE HEM A 1149 2.11 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 ARG A 18 CD - NE - CZ ANGL. DEV. = 24.0 DEGREES REMARK 500 ARG A 135 CD - NE - CZ ANGL. DEV. = 43.7 DEGREES 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 Z 34 DISTANCE = 6.11 ANGSTROMS REMARK 525 HOH Z 37 DISTANCE = 5.48 ANGSTROMS REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 SITE_DESCRIPTION: CMO BINDING SITE FOR CHAIN A DBREF 1W92 A 1 151 UNP Q9ER97 NGB_MOUSE 1 151 SEQADV 1W92 SER A 55 UNP Q9ER97 CYS 55 ENGINEERED MUTATION SEQADV 1W92 SER A 120 UNP Q9ER97 CYS 120 ENGINEERED MUTATION SEQRES 1 A 151 MET GLU ARG PRO GLU SER GLU LEU ILE ARG GLN SER TRP SEQRES 2 A 151 ARG VAL 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 SER 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 THR SER SEQRES 8 A 151 LEU GLY ARG LYS HIS ARG ALA VAL GLY VAL ARG 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 ASP PHE THR PRO ALA THR ARG SEQRES 11 A 151 THR ALA TRP SER ARG LEU TYR GLY ALA VAL VAL GLN ALA SEQRES 12 A 151 MET SER ARG GLY TRP ASP GLY GLU HET HEM A1149 43 HET CMO A1150 2 HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE HETNAM CMO CARBON MONOXIDE HETSYN HEM HEME FORMUL 2 HEM C34 H32 FE N4 O4 FORMUL 3 CMO C O FORMUL 4 HOH *107(H2 O) HELIX 1 1 PRO A 4 ARG A 18 1 15 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 SER A 57 1 7 HELIX 5 5 SER A 58 ASN A 78 1 21 HELIX 6 6 LEU A 82 SER A 84 5 3 HELIX 7 7 LEU A 85 VAL A 99 1 15 HELIX 8 8 ARG A 102 SER A 104 5 3 HELIX 9 9 SER A 105 GLY A 122 1 18 HELIX 10 10 PRO A 123 PHE A 125 5 3 HELIX 11 11 THR A 126 ARG A 146 1 21 LINK FE HEM A1149 C CMO A1150 SITE 1 AC1 13 PHE A 42 TYR A 44 HIS A 64 LYS A 67 SITE 2 AC1 13 LEU A 92 LYS A 95 HIS A 96 SER A 105 SITE 3 AC1 13 PHE A 106 TYR A 137 MET A 144 HOH Z 73 SITE 4 AC1 13 HOH Z 106 SITE 1 AC2 2 PHE A 28 HIS A 64 CRYST1 88.373 88.373 110.983 90.00 90.00 120.00 H 3 2 18 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 0.011320 0.006530 0.000000 0.00000 SCALE2 0.000000 0.013070 0.000000 0.00000 SCALE3 0.000000 0.000000 0.009010 0.00000