HEADER OXIDOREDUCTASE 16-DEC-02 1NG3
TITLE COMPLEX OF THIO (GLYCINE OXIDASE) WITH ACETYL-GLYCINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLYCINE OXIDASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 1.5.3.-;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;
SOURCE 3 ORGANISM_TAXID: 1423;
SOURCE 4 GENE: GOXB;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: B834(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET16-B
KEYWDS FLAVOPROTEIN, OXIDASE, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.C.SETTEMBRE,P.C.DORRESTEIN,J.PARK,A.AUGUSTINE,T.P.BEGLEY,S.E.EALICK
REVDAT 7 03-APR-24 1NG3 1 REMARK
REVDAT 6 14-FEB-24 1NG3 1 REMARK SEQADV
REVDAT 5 11-OCT-17 1NG3 1 REMARK
REVDAT 4 13-JUL-11 1NG3 1 VERSN
REVDAT 3 24-FEB-09 1NG3 1 VERSN
REVDAT 2 03-FEB-04 1NG3 1 REMARK
REVDAT 1 08-APR-03 1NG3 0
JRNL AUTH E.C.SETTEMBRE,P.C.DORRESTEIN,J.PARK,A.AUGUSTINE,T.P.BEGLEY,
JRNL AUTH 2 S.E.EALICK
JRNL TITL STRUCTURAL AND MECHANISTIC STUDIES ON THIO, A GLYCINE
JRNL TITL 2 OXIDASE ESSENTIAL FOR THIAMIN BIOSYNTHESIS IN BACILLUS
JRNL TITL 3 SUBTILIS
JRNL REF BIOCHEMISTRY V. 42 2971 2003
JRNL REFN ISSN 0006-2960
JRNL PMID 12627963
JRNL DOI 10.1021/BI026916V
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.17
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.3
REMARK 3 NUMBER OF REFLECTIONS : 35656
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 SET) : 0.208
REMARK 3 FREE R VALUE : 0.235
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.300
REMARK 3 FREE R VALUE TEST SET COUNT : 1905
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.76
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 5779
REMARK 3 BIN R VALUE (WORKING SET) : 0.2710
REMARK 3 BIN FREE R VALUE : 0.3210
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 2.20
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 128
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.028
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5692
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 127
REMARK 3 SOLVENT ATOMS : 107
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 42.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 41.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -4.54000
REMARK 3 B22 (A**2) : -4.54000
REMARK 3 B33 (A**2) : 9.07000
REMARK 3 B12 (A**2) : 6.19000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.30
REMARK 3 ESD FROM SIGMAA (A) : 0.32
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.36
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.38
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.20
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.410
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.320 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.230 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.980 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.980 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.36
REMARK 3 BSOL : 40.28
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : AAC.PARAM
REMARK 3 PARAMETER FILE 4 : FAD.PARAM
REMARK 3 PARAMETER FILE 5 : PO4_FIX.PARAM
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER_REP.TOP
REMARK 3 TOPOLOGY FILE 3 : FAD.TOP
REMARK 3 TOPOLOGY FILE 4 : AAC.TOP
REMARK 3 TOPOLOGY FILE 5 : PO4_FIX.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1NG3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-DEC-02.
REMARK 100 THE DEPOSITION ID IS D_1000017843.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JAN-02
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.15
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 8-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9791
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35656
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.4
REMARK 200 DATA REDUNDANCY : 4.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06800
REMARK 200 <I/SIGMA(I)> 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 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: MAD PHASED STRUCTURE OF THIO
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.75
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.52
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG MME 2000, HEPES, PH 7.15, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 295.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
REMARK 290 7555 Y,X,-Z+1/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+2/3
REMARK 290 10555 -Y,-X,-Z+5/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/6
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 69.38500
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 138.77000
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 104.07750
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 173.46250
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 34.69250
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 69.38500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 138.77000
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 173.46250
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 104.07750
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 34.69250
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A TETRAMER GENERATED FROM THE
REMARK 300 DIMER IN THE ASYMMETRIC UNIT BY THE TWO-FOLD AXIS: -Y,-X,-Z+5/6.
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 16710 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 51110 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -60.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 BIOMT1 2 0.500000 -0.866025 0.000000 69.68900
REMARK 350 BIOMT2 2 -0.866025 -0.500000 0.000000 120.70489
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 173.46250
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 -20
REMARK 465 GLY A -19
REMARK 465 HIS A -18
REMARK 465 HIS A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 HIS A -9
REMARK 465 SER A -8
REMARK 465 SER A -7
REMARK 465 GLY A -6
REMARK 465 HIS A -5
REMARK 465 ILE A -4
REMARK 465 GLU A -3
REMARK 465 GLY A -2
REMARK 465 ARG A -1
REMARK 465 HIS A 0
REMARK 465 GLU A 365
REMARK 465 ALA A 366
REMARK 465 VAL A 367
REMARK 465 GLN A 368
REMARK 465 ILE A 369
REMARK 465 MET B -20
REMARK 465 GLY B -19
REMARK 465 HIS B -18
REMARK 465 HIS B -17
REMARK 465 HIS B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 HIS B -9
REMARK 465 SER B -8
REMARK 465 SER B -7
REMARK 465 GLY B -6
REMARK 465 HIS B -5
REMARK 465 ILE B -4
REMARK 465 GLU B -3
REMARK 465 GLY B -2
REMARK 465 ARG B -1
REMARK 465 HIS B 0
REMARK 465 GLU B 365
REMARK 465 ALA B 366
REMARK 465 VAL B 367
REMARK 465 GLN B 368
REMARK 465 ILE B 369
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 GLY A 258 N - CA - C ANGL. DEV. = 25.7 DEGREES
REMARK 500 GLY A 258 CA - C - N ANGL. DEV. = -14.2 DEGREES
REMARK 500 ALA B 259 N - CA - C ANGL. DEV. = 21.0 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 LYS A 2 -173.56 -65.62
REMARK 500 ASN A 29 93.69 -54.69
REMARK 500 ARG A 41 -127.23 -111.53
REMARK 500 LEU A 50 55.96 -92.59
REMARK 500 ASP A 60 -160.84 -103.01
REMARK 500 ASP A 180 -49.89 -162.52
REMARK 500 SER A 190 32.12 -99.14
REMARK 500 LEU A 236 111.40 -161.87
REMARK 500 ALA A 259 118.47 67.84
REMARK 500 ASP A 295 -77.26 -99.83
REMARK 500 ASP A 318 99.27 176.83
REMARK 500 ALA A 324 67.55 -156.69
REMARK 500 PHE A 328 -75.84 -43.12
REMARK 500 ARG A 360 147.75 -39.39
REMARK 500 LYS B 2 177.24 -55.20
REMARK 500 ASN B 27 19.46 59.43
REMARK 500 ASN B 29 105.20 -54.04
REMARK 500 ARG B 41 -123.68 -103.50
REMARK 500 GLU B 57 -63.65 -108.26
REMARK 500 ASP B 60 -165.12 -66.76
REMARK 500 MET B 163 15.10 -66.29
REMARK 500 ALA B 166 136.17 -36.32
REMARK 500 LEU B 213 35.22 -96.66
REMARK 500 ALA B 259 102.72 81.27
REMARK 500 ASP B 295 -79.05 -112.32
REMARK 500 ASP B 318 99.90 -169.38
REMARK 500 PHE B 328 -98.26 25.81
REMARK 500 MET B 347 5.74 -69.77
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AAC A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD B 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AAC B 501
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1NG4 RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 ACCORDING TO THE AUTHOR, ALA 288 MAY
REMARK 999 HAVE BEEN MUTATED ACCIDENTALLY TO PRO
REMARK 999 DUE TO PCR ERROR.
DBREF 1NG3 A 1 369 UNP O31616 GLOX_BACSU 1 369
DBREF 1NG3 B 1 369 UNP O31616 GLOX_BACSU 1 369
SEQADV 1NG3 PRO A 288 UNP O31616 ALA 288 SEE REMARK 999
SEQADV 1NG3 MET A -20 UNP O31616 EXPRESSION TAG
SEQADV 1NG3 GLY A -19 UNP O31616 EXPRESSION TAG
SEQADV 1NG3 HIS A -18 UNP O31616 EXPRESSION TAG
SEQADV 1NG3 HIS A -17 UNP O31616 EXPRESSION TAG
SEQADV 1NG3 HIS A -16 UNP O31616 EXPRESSION TAG
SEQADV 1NG3 HIS A -15 UNP O31616 EXPRESSION TAG
SEQADV 1NG3 HIS A -14 UNP O31616 EXPRESSION TAG
SEQADV 1NG3 HIS A -13 UNP O31616 EXPRESSION TAG
SEQADV 1NG3 HIS A -12 UNP O31616 EXPRESSION TAG
SEQADV 1NG3 HIS A -11 UNP O31616 EXPRESSION TAG
SEQADV 1NG3 HIS A -10 UNP O31616 EXPRESSION TAG
SEQADV 1NG3 HIS A -9 UNP O31616 EXPRESSION TAG
SEQADV 1NG3 SER A -8 UNP O31616 EXPRESSION TAG
SEQADV 1NG3 SER A -7 UNP O31616 EXPRESSION TAG
SEQADV 1NG3 GLY A -6 UNP O31616 EXPRESSION TAG
SEQADV 1NG3 HIS A -5 UNP O31616 EXPRESSION TAG
SEQADV 1NG3 ILE A -4 UNP O31616 EXPRESSION TAG
SEQADV 1NG3 GLU A -3 UNP O31616 EXPRESSION TAG
SEQADV 1NG3 GLY A -2 UNP O31616 EXPRESSION TAG
SEQADV 1NG3 ARG A -1 UNP O31616 EXPRESSION TAG
SEQADV 1NG3 HIS A 0 UNP O31616 EXPRESSION TAG
SEQADV 1NG3 PRO B 288 UNP O31616 ALA 288 SEE REMARK 999
SEQADV 1NG3 MET B -20 UNP O31616 EXPRESSION TAG
SEQADV 1NG3 GLY B -19 UNP O31616 EXPRESSION TAG
SEQADV 1NG3 HIS B -18 UNP O31616 EXPRESSION TAG
SEQADV 1NG3 HIS B -17 UNP O31616 EXPRESSION TAG
SEQADV 1NG3 HIS B -16 UNP O31616 EXPRESSION TAG
SEQADV 1NG3 HIS B -15 UNP O31616 EXPRESSION TAG
SEQADV 1NG3 HIS B -14 UNP O31616 EXPRESSION TAG
SEQADV 1NG3 HIS B -13 UNP O31616 EXPRESSION TAG
SEQADV 1NG3 HIS B -12 UNP O31616 EXPRESSION TAG
SEQADV 1NG3 HIS B -11 UNP O31616 EXPRESSION TAG
SEQADV 1NG3 HIS B -10 UNP O31616 EXPRESSION TAG
SEQADV 1NG3 HIS B -9 UNP O31616 EXPRESSION TAG
SEQADV 1NG3 SER B -8 UNP O31616 EXPRESSION TAG
SEQADV 1NG3 SER B -7 UNP O31616 EXPRESSION TAG
SEQADV 1NG3 GLY B -6 UNP O31616 EXPRESSION TAG
SEQADV 1NG3 HIS B -5 UNP O31616 EXPRESSION TAG
SEQADV 1NG3 ILE B -4 UNP O31616 EXPRESSION TAG
SEQADV 1NG3 GLU B -3 UNP O31616 EXPRESSION TAG
SEQADV 1NG3 GLY B -2 UNP O31616 EXPRESSION TAG
SEQADV 1NG3 ARG B -1 UNP O31616 EXPRESSION TAG
SEQADV 1NG3 HIS B 0 UNP O31616 EXPRESSION TAG
SEQRES 1 A 390 MET GLY HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS SER
SEQRES 2 A 390 SER GLY HIS ILE GLU GLY ARG HIS MET LYS ARG HIS TYR
SEQRES 3 A 390 GLU ALA VAL VAL ILE GLY GLY GLY ILE ILE GLY SER ALA
SEQRES 4 A 390 ILE ALA TYR TYR LEU ALA LYS GLU ASN LYS ASN THR ALA
SEQRES 5 A 390 LEU PHE GLU SER GLY THR MET GLY GLY ARG THR THR SER
SEQRES 6 A 390 ALA ALA ALA GLY MET LEU GLY ALA HIS ALA GLU CYS GLU
SEQRES 7 A 390 GLU ARG ASP ALA PHE PHE ASP PHE ALA MET HIS SER GLN
SEQRES 8 A 390 ARG LEU TYR LYS GLY LEU GLY GLU GLU LEU TYR ALA LEU
SEQRES 9 A 390 SER GLY VAL ASP ILE ARG GLN HIS ASN GLY GLY MET PHE
SEQRES 10 A 390 LYS LEU ALA PHE SER GLU GLU ASP VAL LEU GLN LEU ARG
SEQRES 11 A 390 GLN MET ASP ASP LEU ASP SER VAL SER TRP TYR SER LYS
SEQRES 12 A 390 GLU GLU VAL LEU GLU LYS GLU PRO TYR ALA SER GLY ASP
SEQRES 13 A 390 ILE PHE GLY ALA SER PHE ILE GLN ASP ASP VAL HIS VAL
SEQRES 14 A 390 GLU PRO TYR PHE VAL CYS LYS ALA TYR VAL LYS ALA ALA
SEQRES 15 A 390 LYS MET LEU GLY ALA GLU ILE PHE GLU HIS THR PRO VAL
SEQRES 16 A 390 LEU HIS VAL GLU ARG ASP GLY GLU ALA LEU PHE ILE LYS
SEQRES 17 A 390 THR PRO SER GLY ASP VAL TRP ALA ASN HIS VAL VAL VAL
SEQRES 18 A 390 ALA SER GLY VAL TRP SER GLY MET PHE PHE LYS GLN LEU
SEQRES 19 A 390 GLY LEU ASN ASN ALA PHE LEU PRO VAL LYS GLY GLU CYS
SEQRES 20 A 390 LEU SER VAL TRP ASN ASP ASP ILE PRO LEU THR LYS THR
SEQRES 21 A 390 LEU TYR HIS ASP HIS CYS TYR ILE VAL PRO ARG LYS SER
SEQRES 22 A 390 GLY ARG LEU VAL VAL GLY ALA THR MET LYS PRO GLY ASP
SEQRES 23 A 390 TRP SER GLU THR PRO ASP LEU GLY GLY LEU GLU SER VAL
SEQRES 24 A 390 MET LYS LYS ALA LYS THR MET LEU PRO PRO ILE GLN ASN
SEQRES 25 A 390 MET LYS VAL ASP ARG PHE TRP ALA GLY LEU ARG PRO GLY
SEQRES 26 A 390 THR LYS ASP GLY LYS PRO TYR ILE GLY ARG HIS PRO GLU
SEQRES 27 A 390 ASP SER ARG ILE LEU PHE ALA ALA GLY HIS PHE ARG ASN
SEQRES 28 A 390 GLY ILE LEU LEU ALA PRO ALA THR GLY ALA LEU ILE SER
SEQRES 29 A 390 ASP LEU ILE MET ASN LYS GLU VAL ASN GLN ASP TRP LEU
SEQRES 30 A 390 HIS ALA PHE ARG ILE ASP ARG LYS GLU ALA VAL GLN ILE
SEQRES 1 B 390 MET GLY HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS SER
SEQRES 2 B 390 SER GLY HIS ILE GLU GLY ARG HIS MET LYS ARG HIS TYR
SEQRES 3 B 390 GLU ALA VAL VAL ILE GLY GLY GLY ILE ILE GLY SER ALA
SEQRES 4 B 390 ILE ALA TYR TYR LEU ALA LYS GLU ASN LYS ASN THR ALA
SEQRES 5 B 390 LEU PHE GLU SER GLY THR MET GLY GLY ARG THR THR SER
SEQRES 6 B 390 ALA ALA ALA GLY MET LEU GLY ALA HIS ALA GLU CYS GLU
SEQRES 7 B 390 GLU ARG ASP ALA PHE PHE ASP PHE ALA MET HIS SER GLN
SEQRES 8 B 390 ARG LEU TYR LYS GLY LEU GLY GLU GLU LEU TYR ALA LEU
SEQRES 9 B 390 SER GLY VAL ASP ILE ARG GLN HIS ASN GLY GLY MET PHE
SEQRES 10 B 390 LYS LEU ALA PHE SER GLU GLU ASP VAL LEU GLN LEU ARG
SEQRES 11 B 390 GLN MET ASP ASP LEU ASP SER VAL SER TRP TYR SER LYS
SEQRES 12 B 390 GLU GLU VAL LEU GLU LYS GLU PRO TYR ALA SER GLY ASP
SEQRES 13 B 390 ILE PHE GLY ALA SER PHE ILE GLN ASP ASP VAL HIS VAL
SEQRES 14 B 390 GLU PRO TYR PHE VAL CYS LYS ALA TYR VAL LYS ALA ALA
SEQRES 15 B 390 LYS MET LEU GLY ALA GLU ILE PHE GLU HIS THR PRO VAL
SEQRES 16 B 390 LEU HIS VAL GLU ARG ASP GLY GLU ALA LEU PHE ILE LYS
SEQRES 17 B 390 THR PRO SER GLY ASP VAL TRP ALA ASN HIS VAL VAL VAL
SEQRES 18 B 390 ALA SER GLY VAL TRP SER GLY MET PHE PHE LYS GLN LEU
SEQRES 19 B 390 GLY LEU ASN ASN ALA PHE LEU PRO VAL LYS GLY GLU CYS
SEQRES 20 B 390 LEU SER VAL TRP ASN ASP ASP ILE PRO LEU THR LYS THR
SEQRES 21 B 390 LEU TYR HIS ASP HIS CYS TYR ILE VAL PRO ARG LYS SER
SEQRES 22 B 390 GLY ARG LEU VAL VAL GLY ALA THR MET LYS PRO GLY ASP
SEQRES 23 B 390 TRP SER GLU THR PRO ASP LEU GLY GLY LEU GLU SER VAL
SEQRES 24 B 390 MET LYS LYS ALA LYS THR MET LEU PRO PRO ILE GLN ASN
SEQRES 25 B 390 MET LYS VAL ASP ARG PHE TRP ALA GLY LEU ARG PRO GLY
SEQRES 26 B 390 THR LYS ASP GLY LYS PRO TYR ILE GLY ARG HIS PRO GLU
SEQRES 27 B 390 ASP SER ARG ILE LEU PHE ALA ALA GLY HIS PHE ARG ASN
SEQRES 28 B 390 GLY ILE LEU LEU ALA PRO ALA THR GLY ALA LEU ILE SER
SEQRES 29 B 390 ASP LEU ILE MET ASN LYS GLU VAL ASN GLN ASP TRP LEU
SEQRES 30 B 390 HIS ALA PHE ARG ILE ASP ARG LYS GLU ALA VAL GLN ILE
HET PO4 A 402 5
HET FAD A 400 53
HET AAC A 401 8
HET FAD B 500 53
HET AAC B 501 8
HETNAM PO4 PHOSPHATE ION
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
HETNAM AAC ACETYLAMINO-ACETIC ACID
FORMUL 3 PO4 O4 P 3-
FORMUL 4 FAD 2(C27 H33 N9 O15 P2)
FORMUL 5 AAC 2(C4 H7 N O3)
FORMUL 8 HOH *107(H2 O)
HELIX 1 1 GLY A 13 GLU A 26 1 14
HELIX 2 2 ARG A 41 ALA A 46 1 6
HELIX 3 3 GLY A 51 GLU A 55 5 5
HELIX 4 4 ASP A 60 TYR A 73 1 14
HELIX 5 5 GLY A 75 GLY A 85 1 11
HELIX 6 6 SER A 101 GLN A 110 1 10
HELIX 7 7 SER A 121 GLU A 129 1 9
HELIX 8 8 GLU A 149 LEU A 164 1 16
HELIX 9 9 SER A 202 TRP A 205 5 4
HELIX 10 10 SER A 206 LEU A 213 1 8
HELIX 11 11 ASP A 271 LEU A 286 1 16
HELIX 12 12 PRO A 287 MET A 292 5 6
HELIX 13 13 LEU A 334 MET A 347 1 14
HELIX 14 14 ASN A 352 PHE A 359 1 8
HELIX 15 15 GLY B 13 GLU B 26 1 14
HELIX 16 16 ARG B 41 ALA B 46 5 6
HELIX 17 17 ASP B 60 TYR B 73 1 14
HELIX 18 18 GLY B 75 GLY B 85 1 11
HELIX 19 19 SER B 101 ARG B 109 1 9
HELIX 20 20 GLN B 110 ASP B 112 5 3
HELIX 21 21 SER B 121 GLU B 129 1 9
HELIX 22 22 GLU B 149 MET B 163 1 15
HELIX 23 23 SER B 202 TRP B 205 5 4
HELIX 24 24 SER B 206 LEU B 213 1 8
HELIX 25 25 ASP B 271 LEU B 286 1 16
HELIX 26 26 PRO B 287 MET B 292 5 6
HELIX 27 27 ASN B 330 MET B 347 1 18
HELIX 28 28 ASN B 352 PHE B 359 1 8
SHEET 1 A 6 TYR A 311 HIS A 315 0
SHEET 2 A 6 ASP A 318 ALA A 325 -1 O PHE A 323 N GLY A 313
SHEET 3 A 6 GLY A 191 VAL A 200 1 N VAL A 200 O LEU A 322
SHEET 4 A 6 HIS A 4 ILE A 10 1 N ILE A 10 O VAL A 199
SHEET 5 A 6 THR A 30 PHE A 33 1 O ALA A 31 N VAL A 9
SHEET 6 A 6 GLU A 167 PHE A 169 1 O PHE A 169 N LEU A 32
SHEET 1 B 5 TYR A 311 HIS A 315 0
SHEET 2 B 5 ASP A 318 ALA A 325 -1 O PHE A 323 N GLY A 313
SHEET 3 B 5 GLY A 191 VAL A 200 1 N VAL A 200 O LEU A 322
SHEET 4 B 5 LEU A 184 THR A 188 -1 N ILE A 186 O VAL A 193
SHEET 5 B 5 HIS A 176 ARG A 179 -1 N GLU A 178 O PHE A 185
SHEET 1 C 8 LYS A 293 GLY A 304 0
SHEET 2 C 8 LEU A 220 TRP A 230 -1 N CYS A 226 O TRP A 298
SHEET 3 C 8 ARG A 254 GLY A 258 -1 O VAL A 257 N LEU A 227
SHEET 4 C 8 CYS A 245 PRO A 249 -1 N VAL A 248 O VAL A 256
SHEET 5 C 8 THR A 239 HIS A 242 -1 N HIS A 242 O CYS A 245
SHEET 6 C 8 MET A 95 LEU A 98 1 N PHE A 96 O THR A 239
SHEET 7 C 8 ALA A 139 ILE A 142 -1 O ILE A 142 N MET A 95
SHEET 8 C 8 VAL A 117 TYR A 120 -1 N SER A 118 O PHE A 141
SHEET 1 D 3 LYS A 293 GLY A 304 0
SHEET 2 D 3 LEU A 220 TRP A 230 -1 N CYS A 226 O TRP A 298
SHEET 3 D 3 LYS A 262 PRO A 263 -1 O LYS A 262 N LYS A 223
SHEET 1 E 4 HIS B 4 TYR B 5 0
SHEET 2 E 4 GLY B 191 ALA B 195 1 O TRP B 194 N TYR B 5
SHEET 3 E 4 LEU B 184 THR B 188 -1 N THR B 188 O GLY B 191
SHEET 4 E 4 HIS B 176 GLU B 178 -1 N GLU B 178 O PHE B 185
SHEET 1 F 6 GLU B 167 GLU B 170 0
SHEET 2 F 6 THR B 30 GLU B 34 1 N LEU B 32 O PHE B 169
SHEET 3 F 6 ALA B 7 ILE B 10 1 N VAL B 9 O ALA B 31
SHEET 4 F 6 VAL B 198 VAL B 200 1 O VAL B 199 N ILE B 10
SHEET 5 F 6 ASP B 318 ALA B 325 1 O LEU B 322 N VAL B 198
SHEET 6 F 6 TYR B 311 HIS B 315 -1 N HIS B 315 O ILE B 321
SHEET 1 G 8 LYS B 293 GLY B 304 0
SHEET 2 G 8 LEU B 220 TRP B 230 -1 N LEU B 220 O GLY B 304
SHEET 3 G 8 ARG B 254 GLY B 258 -1 O VAL B 257 N LEU B 227
SHEET 4 G 8 CYS B 245 PRO B 249 -1 N VAL B 248 O VAL B 256
SHEET 5 G 8 THR B 239 HIS B 242 -1 N HIS B 242 O CYS B 245
SHEET 6 G 8 MET B 95 ALA B 99 1 N PHE B 96 O THR B 239
SHEET 7 G 8 GLY B 138 ILE B 142 -1 O SER B 140 N LYS B 97
SHEET 8 G 8 VAL B 117 TYR B 120 -1 N TYR B 120 O ALA B 139
SHEET 1 H 3 LYS B 293 GLY B 304 0
SHEET 2 H 3 LEU B 220 TRP B 230 -1 N LEU B 220 O GLY B 304
SHEET 3 H 3 LYS B 262 PRO B 263 -1 O LYS B 262 N LYS B 223
SITE 1 AC1 4 ARG A 89 ARG A 254 ARG B 89 ARG B 254
SITE 1 AC2 36 GLY A 11 GLY A 13 ILE A 14 ILE A 15
SITE 2 AC2 36 PHE A 33 GLU A 34 SER A 35 ARG A 41
SITE 3 AC2 36 THR A 42 THR A 43 ALA A 46 ALA A 47
SITE 4 AC2 36 GLY A 48 MET A 49 VAL A 174 SER A 202
SITE 5 AC2 36 GLY A 203 TRP A 205 PHE A 209 CYS A 226
SITE 6 AC2 36 TYR A 246 GLY A 300 ARG A 302 HIS A 327
SITE 7 AC2 36 PHE A 328 ARG A 329 ASN A 330 GLY A 331
SITE 8 AC2 36 ILE A 332 LEU A 333 AAC A 401 HOH A 403
SITE 9 AC2 36 HOH A 405 HOH A 409 HOH A 410 HOH A 438
SITE 1 AC3 7 MET A 49 TYR A 241 TYR A 246 ALA A 259
SITE 2 AC3 7 ARG A 302 ARG A 329 FAD A 400
SITE 1 AC4 35 GLY B 11 GLY B 13 ILE B 14 ILE B 15
SITE 2 AC4 35 PHE B 33 GLU B 34 SER B 35 ARG B 41
SITE 3 AC4 35 THR B 42 THR B 43 ALA B 46 ALA B 47
SITE 4 AC4 35 GLY B 48 MET B 49 VAL B 174 SER B 202
SITE 5 AC4 35 GLY B 203 TRP B 205 PHE B 209 CYS B 226
SITE 6 AC4 35 TYR B 246 GLY B 300 ARG B 302 HIS B 327
SITE 7 AC4 35 PHE B 328 ARG B 329 ASN B 330 GLY B 331
SITE 8 AC4 35 ILE B 332 LEU B 333 AAC B 501 HOH B 502
SITE 9 AC4 35 HOH B 504 HOH B 505 HOH B 543
SITE 1 AC5 9 MET B 49 GLU B 55 TYR B 241 TYR B 246
SITE 2 AC5 9 ALA B 259 ARG B 302 ARG B 329 FAD B 500
SITE 3 AC5 9 HOH B 514
CRYST1 139.378 139.378 208.155 90.00 90.00 120.00 P 61 2 2 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 0.007175 0.004142 0.000000 0.00000
SCALE2 0.000000 0.008285 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004804 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
