REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH C.S.MILES,K.H.D.LE,F.LEDERER REMARK 1 TITL PROBING INTRAMOLECULAR ELECTRON TRANSFER WITHIN REMARK 1 TITL 2 FLAVOCYTOCHROME B2 WITH A MONOCLONAL ANTIBODY REMARK 1 REF BIOCHEMISTRY V. 37 3440 1998 REMARK 1 REFN ISSN 0006-2960 REMARK 1 PMID 9521665 REMARK 1 DOI 10.1021/BI972639U REMARK 1 REFERENCE 2 REMARK 1 AUTH K.H.D.LE,M.MAYER,F.LEDERER REMARK 1 TITL EPITOPE MAPPING FOR THE MONOCLONAL ANTIBODY THAT INHIBITS REMARK 1 TITL 2 INTRAMOLECULAR ELECTRON TRANSFER IN FLAVOCYTOCHROME B2 REMARK 1 REF BIOCHEM.J. V. 373 115 2003 REMARK 1 REFN ISSN 0264-6021 REMARK 1 PMID 12646042 REMARK 1 DOI 10.1042/BJ20030024 REMARK 2 REMARK 2 RESOLUTION. 2.70 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.5.0102 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) : 2.70 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.75 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 96.6 REMARK 3 NUMBER OF REFLECTIONS : 27762 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) : 0.218 REMARK 3 R VALUE (WORKING SET) : 0.214 REMARK 3 FREE R VALUE : 0.289 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100 REMARK 3 FREE R VALUE TEST SET COUNT : 1487 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.70 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.77 REMARK 3 REFLECTION IN BIN (WORKING SET) : 1987 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.74 REMARK 3 BIN R VALUE (WORKING SET) : 0.2760 REMARK 3 BIN FREE R VALUE SET COUNT : 108 REMARK 3 BIN FREE R VALUE : 0.3930 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 7803 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 86 REMARK 3 SOLVENT ATOMS : 132 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.71 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.42000 REMARK 3 B22 (A**2) : -0.15000 REMARK 3 B33 (A**2) : 0.62000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.22000 REMARK 3 B23 (A**2) : 0.00000 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): 0.432 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.309 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 14.848 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.908 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.835 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8125 ; 0.015 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11163 ; 1.821 ; 1.990 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1025 ; 6.449 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 293 ;39.093 ;24.744 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1196 ;19.179 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 17 ;28.341 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1267 ; 0.103 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6155 ; 0.009 ; 0.022 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): 5160 ; 0.688 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8397 ; 1.290 ; 2.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2965 ; 1.732 ; 3.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2766 ; 2.869 ; 4.500 REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL 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: HYDROGENS HAVE BEEN ADDED IN THE RIDING REMARK 3 POSITIONS REMARK 4 REMARK 4 3KS0 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-DEC-09. REMARK 100 THE RCSB ID CODE IS RCSB056374. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 10-NOV-03 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 6.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ESRF REMARK 200 BEAMLINE : ID14-1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.934 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM REMARK 200 DATA SCALING SOFTWARE : SCALA REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29267 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700 REMARK 200 RESOLUTION RANGE LOW (A) : 25.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 97.0 REMARK 200 DATA REDUNDANCY : 3.500 REMARK 200 R MERGE (I) : 0.16500 REMARK 200 R SYM (I) : 0.16500 REMARK 200 FOR THE DATA SET : 9.1000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.85 REMARK 200 COMPLETENESS FOR SHELL (%) : 94.6 REMARK 200 DATA REDUNDANCY IN SHELL : 3.30 REMARK 200 R MERGE FOR SHELL (I) : 0.66600 REMARK 200 R SYM FOR SHELL (I) : 0.66600 REMARK 200 FOR SHELL : 1.200 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 48.82 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 20 % PEG 4000, 0.1 M MES PH 6.5, 0.2 M REMARK 280 MGCL2, VAPOR DIFFUSION, TEMPERATURE 291K 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,Y+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 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 41.84000 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 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 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 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, J, K 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 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, H, 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 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 ASP L 213 REMARK 465 CYS L 214 REMARK 465 SER H 132 REMARK 465 ALA H 133 REMARK 465 ALA H 134 REMARK 465 GLN H 135 REMARK 465 THR H 136 REMARK 465 ASN H 137 REMARK 465 ASP H 218 REMARK 465 CYS H 219 REMARK 465 GLY H 220 REMARK 465 CYS H 221 REMARK 465 LYS H 222 REMARK 465 PRO H 223 REMARK 465 CYS H 224 REMARK 465 ILE H 225 REMARK 465 ALA A 98 REMARK 465 PRO A 99 REMARK 465 GLY A 100 REMARK 465 ASP J 213 REMARK 465 CYS J 214 REMARK 465 SER K 132 REMARK 465 ALA K 133 REMARK 465 ALA K 134 REMARK 465 GLN K 135 REMARK 465 THR K 136 REMARK 465 ASN K 137 REMARK 465 CYS K 221 REMARK 465 LYS K 222 REMARK 465 PRO K 223 REMARK 465 CYS K 224 REMARK 465 ILE K 225 REMARK 465 ALA B 98 REMARK 465 PRO B 99 REMARK 465 GLY B 100 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 ASN L 131 CG OD1 ND2 REMARK 470 MET L 162 CG SD CE REMARK 470 ARG L 186 CG CD NE CZ NH1 NH2 REMARK 470 SER H 10 OG REMARK 470 SER H 15 OG REMARK 470 LYS H 44 CG CD CE NZ REMARK 470 SER H 162 OG REMARK 470 SER H 189 OG REMARK 470 GLU H 195 CB CG CD OE1 REMARK 470 LYS A 21 CG CD CE NZ REMARK 470 ARG A 38 CG CD NE CZ NH1 NH2 REMARK 470 PRO J 42 CD REMARK 470 GLN J 160 CG CD OE1 NE2 REMARK 470 ARG J 186 CG CD NE CZ NH1 NH2 REMARK 470 ARG J 190 CG CD NE CZ NH1 NH2 REMARK 470 GLU K 1 CG CD OE1 REMARK 470 SER K 10 OG REMARK 470 SER K 15 OG REMARK 470 ASN K 43 CG OD1 ND2 REMARK 470 LYS K 44 CG CD CE NZ REMARK 470 LEU K 45 CG CD1 CD2 REMARK 470 SER K 162 OG REMARK 470 SER K 189 OG REMARK 470 GLU K 195 CB CG CD OE1 REMARK 470 ASP K 218 CG OD1 OD2 REMARK 470 CYS K 219 SG REMARK 470 LYS B 21 CG CD CE NZ REMARK 470 ARG B 38 CG CD NE CZ NH1 NH2 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 DISTANCE REMARK 500 O GLY L 155 O HOH L 238 2.13 REMARK 500 OD2 ASP B 57 OG1 THR B 59 2.17 REMARK 500 REMARK 500 REMARK: NULL 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),1X,F6.3) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 CYS H 199 CB CYS H 199 SG -0.099 REMARK 500 REMARK 500 REMARK: NULL 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 PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 LEU K 181 CA - CB - CG ANGL. DEV. = 15.5 DEGREES REMARK 500 TYR B 97 CA - C - O ANGL. DEV. = -38.5 DEGREES REMARK 500 REMARK 500 REMARK: NULL 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 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 THR L 53 -57.51 71.59 REMARK 500 ASN L 54 51.25 -143.20 REMARK 500 GLU L 85 101.69 -59.09 REMARK 500 ALA L 86 -173.25 -177.84 REMARK 500 GLN L 111 160.37 176.75 REMARK 500 PRO L 122 -179.12 -69.99 REMARK 500 GLU L 201 62.48 31.70 REMARK 500 PRO L 211 61.75 2.79 REMARK 500 VAL H 2 114.52 49.39 REMARK 500 SER H 15 -22.44 95.78 REMARK 500 LYS H 44 177.95 70.36 REMARK 500 THR H 87 -35.00 -34.61 REMARK 500 PHE H 99 79.87 -61.30 REMARK 500 SER H 101 -33.31 73.15 REMARK 500 TYR H 102 -147.01 -96.98 REMARK 500 TYR H 106 115.80 86.60 REMARK 500 ASP H 177 5.65 55.63 REMARK 500 SER H 194 -68.52 -23.81 REMARK 500 LYS H 209 107.99 -170.51 REMARK 500 ASN A 20 55.51 -149.70 REMARK 500 ASP A 24 80.04 -157.48 REMARK 500 ASN A 30 -124.56 68.38 REMARK 500 LEU A 40 -61.79 -27.27 REMARK 500 TYR J 34 56.68 35.63 REMARK 500 ASP J 43 43.33 75.32 REMARK 500 THR J 53 -66.23 71.10 REMARK 500 ASN J 96 19.29 50.99 REMARK 500 LEU J 109 107.02 -52.73 REMARK 500 GLN J 111 161.02 174.34 REMARK 500 GLU J 129 12.63 -65.32 REMARK 500 GLU J 201 64.26 37.27 REMARK 500 VAL K 2 107.85 59.65 REMARK 500 SER K 15 -24.26 104.58 REMARK 500 THR K 30 31.74 -81.65 REMARK 500 ASN K 43 6.43 80.94 REMARK 500 ASN K 60 124.77 -31.66 REMARK 500 THR K 87 -37.14 -26.57 REMARK 500 ALA K 91 -176.62 -178.73 REMARK 500 PHE K 99 83.89 -65.15 REMARK 500 SER K 101 -31.73 78.39 REMARK 500 TYR K 102 -142.46 -96.98 REMARK 500 TYR K 106 112.59 81.30 REMARK 500 ALA K 118 138.30 -39.48 REMARK 500 ASP K 177 8.68 49.67 REMARK 500 SER K 194 -70.99 2.25 REMARK 500 ARG K 217 -179.12 -57.59 REMARK 500 ASP K 218 -169.20 -119.75 REMARK 500 CYS K 219 155.71 174.45 REMARK 500 ASN B 20 44.66 -141.72 REMARK 500 ASN B 30 -131.63 65.34 REMARK 500 REMARK 500 THIS ENTRY HAS 52 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CHIRAL CENTERS REMARK 500 REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16) REMARK 500 REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS REMARK 500 ASN H 35 24.7 L L OUTSIDE RANGE REMARK 500 ASN J 173 24.1 L L OUTSIDE RANGE REMARK 500 GLU K 6 24.8 L L OUTSIDE RANGE REMARK 500 ASN K 35 24.1 L L OUTSIDE RANGE REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 HEM B 101 FE REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS B 43 NE2 REMARK 620 2 HEM B 101 NA 94.5 REMARK 620 3 HEM B 101 NB 93.4 87.0 REMARK 620 4 HEM B 101 NC 83.8 176.7 90.3 REMARK 620 5 HEM B 101 ND 85.6 92.3 178.7 90.3 REMARK 620 6 HIS B 66 NE2 171.6 89.8 94.0 92.3 87.1 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 HEM A 101 FE REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS A 43 NE2 REMARK 620 2 HEM A 101 NA 94.5 REMARK 620 3 HEM A 101 NB 93.2 85.6 REMARK 620 4 HEM A 101 NC 84.1 176.7 91.5 REMARK 620 5 HEM A 101 ND 83.6 94.3 176.8 88.5 REMARK 620 6 HIS A 66 NE2 170.9 88.2 95.7 93.6 87.5 REMARK 620 N 1 2 3 4 5 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 101 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 101 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1FCB RELATED DB: PDB REMARK 900 MOLECULAR STRUCTURE OF FLAVOCYTOCHROME B2 AT 2.4 ANGSTROMS REMARK 900 RESOLUTION REMARK 900 RELATED ID: 1KBI RELATED DB: PDB REMARK 900 CRYSTALLOGRAPHIC STUDY OF THE RECOMBINANT FLAVIN-BINDING REMARK 900 DOMAIN OF BAKER'S YEAST FLAVOCYTOCHROME B2: COMPARISON WITH REMARK 900 THE INTACT WILD-TYPE ENZYME