HEADER FLAVOENZYME 29-MAR-99 1CHU
TITLE STRUCTURE OF L-ASPARTATE OXIDASE: IMPLICATIONS FOR THE SUCCINATE
TITLE 2 DEHYDROGENASE/ FUMARATE REDUCATSE FAMILY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (L-ASPARTATE OXIDASE);
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: NADB;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21
KEYWDS FLAVOENZYME, NAD BIOSYNTHESIS, FAD, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.MATTEVI
REVDAT 3 27-DEC-23 1CHU 1 REMARK
REVDAT 2 24-FEB-09 1CHU 1 VERSN
REVDAT 1 23-JUN-99 1CHU 0
JRNL AUTH A.MATTEVI,G.TEDESCHI,L.BACCHELLA,A.CODA,A.NEGRI,S.RONCHI
JRNL TITL STRUCTURE OF L-ASPARTATE OXIDASE: IMPLICATIONS FOR THE
JRNL TITL 2 SUCCINATE DEHYDROGENASE/FUMARATE REDUCTASE OXIDOREDUCTASE
JRNL TITL 3 FAMILY.
JRNL REF STRUCTURE FOLD.DES. V. 7 745 1999
JRNL REFN ISSN 0969-2126
JRNL PMID 10425677
JRNL DOI 10.1016/S0969-2126(99)80099-9
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 3 NUMBER OF REFLECTIONS : 33258
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) : 0.225
REMARK 3 R VALUE (WORKING SET) : 0.224
REMARK 3 FREE R VALUE : 0.281
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1705
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3761
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 196
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 41.70
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 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.018 ; 0.020
REMARK 3 ANGLE DISTANCE (A) : 0.045 ; 0.040
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) : 2.000 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 3.100 ; 5.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.500 ; 4.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.500 ; 6.000
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1CHU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-APR-99.
REMARK 100 THE DEPOSITION ID IS D_1000000755.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-MAR-98
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.3
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33258
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : 0.04900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.30
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.4
REMARK 200 DATA REDUNDANCY IN SHELL : 3.10
REMARK 200 R MERGE FOR SHELL (I) : 0.14000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.74
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 8.3
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 106.48667
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 53.24333
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 53.24333
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 106.48667
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 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: DIMERIC
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 0.00000
REMARK 350 BIOMT2 2 0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 400
REMARK 400 COMPOUND
REMARK 400 THE CRYSTALLINE PROTEIN IS IN THE APO (FAD-FREE) FORM
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 GLY A 44
REMARK 465 SER A 45
REMARK 465 THR A 46
REMARK 465 PHE A 47
REMARK 465 TYR A 48
REMARK 465 ALA A 49
REMARK 465 GLN A 50
REMARK 465 GLY A 51
REMARK 465 GLY A 52
REMARK 465 ILE A 53
REMARK 465 ALA A 54
REMARK 465 ALA A 55
REMARK 465 VAL A 56
REMARK 465 PHE A 104
REMARK 465 ASP A 105
REMARK 465 THR A 106
REMARK 465 HIS A 107
REMARK 465 ILE A 108
REMARK 465 GLN A 109
REMARK 465 PRO A 110
REMARK 465 ASN A 111
REMARK 465 GLY A 112
REMARK 465 GLU A 113
REMARK 465 GLU A 114
REMARK 465 SER A 115
REMARK 465 TYR A 116
REMARK 465 HIS A 117
REMARK 465 LEU A 118
REMARK 465 THR A 119
REMARK 465 ARG A 120
REMARK 465 GLU A 121
REMARK 465 GLY A 122
REMARK 465 GLY A 123
REMARK 465 HIS A 124
REMARK 465 SER A 125
REMARK 465 HIS A 126
REMARK 465 ARG A 127
REMARK 465 ARG A 128
REMARK 465 ILE A 129
REMARK 465 LEU A 130
REMARK 465 HIS A 131
REMARK 465 ALA A 132
REMARK 465 ALA A 133
REMARK 465 ASP A 134
REMARK 465 ALA A 135
REMARK 465 THR A 136
REMARK 465 GLY A 137
REMARK 465 ARG A 138
REMARK 465 GLU A 139
REMARK 465 VAL A 140
REMARK 465 GLU A 141
REMARK 465 PRO A 411
REMARK 465 TYR A 412
REMARK 465 ALA A 413
REMARK 465 GLY A 534
REMARK 465 ASN A 535
REMARK 465 HIS A 536
REMARK 465 TYR A 537
REMARK 465 ILE A 538
REMARK 465 ASN A 539
REMARK 465 ARG A 540
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 ASN A 2 CG OD1 ND2
REMARK 480 THR A 3 OG1 CG2
REMARK 480 LEU A 4 CG CD1 CD2
REMARK 480 ASP A 61 CG OD1 OD2
REMARK 480 LYS A 198 CG CD CE NZ
REMARK 480 ARG A 254 CG CD NE CZ NH1 NH2
REMARK 480 GLU A 265 CG CD OE1 OE2
REMARK 480 LYS A 316 C O CD CE NZ
REMARK 480 PRO A 317 N
REMARK 480 ASP A 319 CB CG OD1 OD2
REMARK 480 PHE A 320 CG CD1 CD2 CE1 CE2 CZ
REMARK 480 ILE A 321 CG2 CD1
REMARK 480 ARG A 322 CG CD NE CZ NH1 NH2
REMARK 480 GLN A 323 CG CD OE1 NE2
REMARK 480 HIS A 324 CG ND1 CD2 CE1 NE2
REMARK 480 GLN A 341 CG CD OE1 NE2
REMARK 480 HIS A 414 CG ND1 CD2 CE1 NE2
REMARK 480 ASP A 415 CG OD1 OD2
REMARK 480 ILE A 416 CG1 CG2 CD1
REMARK 480 SER A 425 OG
REMARK 480 ARG A 426 CG CD NE CZ NH1 NH2
REMARK 480 GLU A 428 CD OE1 OE2
REMARK 480 ARG A 482 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 NH1 ARG A 187 O HOH A 633 1.60
REMARK 500 SG CYS A 395 O HOH A 734 1.74
REMARK 500 CZ ARG A 462 O HOH A 735 1.91
REMARK 500 O PRO A 317 CB PHE A 320 1.91
REMARK 500 NE ARG A 462 O HOH A 735 1.93
REMARK 500 NH1 ARG A 364 NH2 ARG A 409 1.97
REMARK 500 O HOH A 587 O HOH A 615 1.98
REMARK 500 OG SER A 425 CB HIS A 480 2.07
REMARK 500 O HOH A 615 O HOH A 644 2.09
REMARK 500 O HOH A 644 O HOH A 670 2.11
REMARK 500 OE1 GLU A 158 O HOH A 674 2.14
REMARK 500 ND2 ASN A 161 OD1 ASN A 485 2.17
REMARK 500 O ILE A 154 O HOH A 628 2.17
REMARK 500 O PHE A 320 CD2 HIS A 324 2.17
REMARK 500 OE1 GLU A 6 N THR A 194 2.19
REMARK 500
REMARK 500 REMARK: NULL
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 O HOH A 650 O HOH A 650 4555 1.20
REMARK 500 ND2 ASN A 2 NE2 HIS A 480 5675 1.60
REMARK 500 CG1 VAL A 435 NH1 ARG A 462 4555 1.98
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 ASN A 2 CB ASN A 2 CG 0.148
REMARK 500 ASP A 61 CB ASP A 61 CG -0.152
REMARK 500 PHE A 320 CB PHE A 320 CG -0.135
REMARK 500 HIS A 414 CB HIS A 414 CG 0.149
REMARK 500 GLU A 428 CG GLU A 428 CD -0.149
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 ASN A 2 CA - CB - CG ANGL. DEV. = 17.8 DEGREES
REMARK 500 GLU A 43 OE1 - CD - OE2 ANGL. DEV. = -14.2 DEGREES
REMARK 500 ASP A 61 CB - CG - OD1 ANGL. DEV. = -18.9 DEGREES
REMARK 500 ASP A 61 CB - CG - OD2 ANGL. DEV. = 17.9 DEGREES
REMARK 500 ASP A 64 CB - CG - OD2 ANGL. DEV. = 6.1 DEGREES
REMARK 500 ARG A 91 NE - CZ - NH1 ANGL. DEV. = 8.3 DEGREES
REMARK 500 ARG A 91 NE - CZ - NH2 ANGL. DEV. = -7.0 DEGREES
REMARK 500 ALA A 162 N - CA - CB ANGL. DEV. = 8.7 DEGREES
REMARK 500 ASP A 164 CB - CG - OD1 ANGL. DEV. = 8.3 DEGREES
REMARK 500 ARG A 177 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG A 178 NH1 - CZ - NH2 ANGL. DEV. = 8.6 DEGREES
REMARK 500 ARG A 178 NE - CZ - NH2 ANGL. DEV. = -7.4 DEGREES
REMARK 500 ARG A 187 CD - NE - CZ ANGL. DEV. = 36.3 DEGREES
REMARK 500 ARG A 187 NE - CZ - NH1 ANGL. DEV. = -7.4 DEGREES
REMARK 500 ARG A 187 NE - CZ - NH2 ANGL. DEV. = 7.1 DEGREES
REMARK 500 ASP A 218 CB - CG - OD1 ANGL. DEV. = 8.1 DEGREES
REMARK 500 ASP A 223 CB - CG - OD1 ANGL. DEV. = 8.5 DEGREES
REMARK 500 ARG A 263 NE - CZ - NH1 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ASP A 273 CB - CA - C ANGL. DEV. = -20.2 DEGREES
REMARK 500 ASP A 273 CB - CG - OD1 ANGL. DEV. = -10.7 DEGREES
REMARK 500 ASP A 273 CB - CG - OD2 ANGL. DEV. = 7.2 DEGREES
REMARK 500 ARG A 276 CD - NE - CZ ANGL. DEV. = 9.9 DEGREES
REMARK 500 ARG A 276 NE - CZ - NH1 ANGL. DEV. = 4.8 DEGREES
REMARK 500 ASP A 280 CB - CG - OD1 ANGL. DEV. = 11.2 DEGREES
REMARK 500 ASP A 280 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 ARG A 290 CD - NE - CZ ANGL. DEV. = -9.1 DEGREES
REMARK 500 ARG A 290 NE - CZ - NH1 ANGL. DEV. = 4.8 DEGREES
REMARK 500 ASP A 291 CB - CG - OD1 ANGL. DEV. = 10.4 DEGREES
REMARK 500 ASP A 291 CB - CG - OD2 ANGL. DEV. = -7.0 DEGREES
REMARK 500 ARG A 295 NE - CZ - NH1 ANGL. DEV. = -4.6 DEGREES
REMARK 500 ARG A 303 NE - CZ - NH2 ANGL. DEV. = 3.6 DEGREES
REMARK 500 PRO A 317 CA - C - N ANGL. DEV. = -20.8 DEGREES
REMARK 500 PRO A 317 O - C - N ANGL. DEV. = 16.1 DEGREES
REMARK 500 ASP A 319 N - CA - CB ANGL. DEV. = -25.2 DEGREES
REMARK 500 PHE A 320 CB - CG - CD2 ANGL. DEV. = -15.3 DEGREES
REMARK 500 PHE A 320 CB - CG - CD1 ANGL. DEV. = 13.1 DEGREES
REMARK 500 ILE A 321 CA - CB - CG2 ANGL. DEV. = 13.0 DEGREES
REMARK 500 ARG A 322 NE - CZ - NH2 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ASP A 338 CB - CG - OD1 ANGL. DEV. = 6.2 DEGREES
REMARK 500 GLN A 341 CA - CB - CG ANGL. DEV. = 22.4 DEGREES
REMARK 500 GLN A 341 CB - CG - CD ANGL. DEV. = 16.8 DEGREES
REMARK 500 TYR A 352 CB - CG - CD2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 ASP A 360 CB - CG - OD1 ANGL. DEV. = 12.5 DEGREES
REMARK 500 ASP A 360 CB - CG - OD2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 ASP A 361 CB - CG - OD1 ANGL. DEV. = -5.9 DEGREES
REMARK 500 ASP A 361 CB - CG - OD2 ANGL. DEV. = 7.4 DEGREES
REMARK 500 ARG A 364 NE - CZ - NH2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 TYR A 371 CB - CG - CD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 TYR A 371 CB - CG - CD1 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ARG A 386 CD - NE - CZ ANGL. DEV. = 18.9 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 77 ANGLE DEVIATIONS.
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 SER A 16 43.85 -146.83
REMARK 500 VAL A 102 54.61 -97.15
REMARK 500 ALA A 203 35.93 -141.33
REMARK 500 PHE A 240 79.91 -104.82
REMARK 500 HIS A 315 -22.75 -30.14
REMARK 500 PRO A 317 125.68 -33.64
REMARK 500 ALA A 318 -78.62 -47.94
REMARK 500 LEU A 339 -9.27 -59.92
REMARK 500 GLU A 368 137.37 -39.87
REMARK 500 SER A 389 -10.67 82.01
REMARK 500 ASP A 415 158.66 -48.61
REMARK 500 ILE A 416 -178.14 172.76
REMARK 500 SER A 417 179.23 73.85
REMARK 500 VAL A 451 38.59 -146.91
REMARK 500 HIS A 480 18.17 46.30
REMARK 500 PHE A 481 154.82 -44.97
REMARK 500 LYS A 508 50.93 -101.26
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 GLU A 375 0.07 SIDE CHAIN
REMARK 500 ASP A 415 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 SER A 22 -12.25
REMARK 500 ASP A 29 -12.02
REMARK 500 ALA A 82 -10.79
REMARK 500 ARG A 155 -12.46
REMARK 500 CYS A 195 10.63
REMARK 500 GLY A 205 -11.49
REMARK 500 ARG A 234 -10.38
REMARK 500 PRO A 251 -14.73
REMARK 500 ASP A 273 14.60
REMARK 500 ARG A 303 -10.87
REMARK 500 CYS A 395 11.01
REMARK 500 LEU A 396 -11.12
REMARK 500 ARG A 408 -13.06
REMARK 500
REMARK 500 REMARK: NULL
REMARK 615
REMARK 615 ZERO OCCUPANCY ATOM
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 615 M RES C SSEQI
REMARK 615 HOH A 570
REMARK 615 HOH A 688
DBREF 1CHU A 1 540 UNP P10902 NADB_ECOLI 1 540
SEQRES 1 A 540 MET ASN THR LEU PRO GLU HIS SER CYS ASP VAL LEU ILE
SEQRES 2 A 540 ILE GLY SER GLY ALA ALA GLY LEU SER LEU ALA LEU ARG
SEQRES 3 A 540 LEU ALA ASP GLN HIS GLN VAL ILE VAL LEU SER LYS GLY
SEQRES 4 A 540 PRO VAL THR GLU GLY SER THR PHE TYR ALA GLN GLY GLY
SEQRES 5 A 540 ILE ALA ALA VAL PHE ASP GLU THR ASP SER ILE ASP SER
SEQRES 6 A 540 HIS VAL GLU ASP THR LEU ILE ALA GLY ALA GLY ILE CYS
SEQRES 7 A 540 ASP ARG HIS ALA VAL GLU PHE VAL ALA SER ASN ALA ARG
SEQRES 8 A 540 SER CYS VAL GLN TRP LEU ILE ASP GLN GLY VAL LEU PHE
SEQRES 9 A 540 ASP THR HIS ILE GLN PRO ASN GLY GLU GLU SER TYR HIS
SEQRES 10 A 540 LEU THR ARG GLU GLY GLY HIS SER HIS ARG ARG ILE LEU
SEQRES 11 A 540 HIS ALA ALA ASP ALA THR GLY ARG GLU VAL GLU THR THR
SEQRES 12 A 540 LEU VAL SER LYS ALA LEU ASN HIS PRO ASN ILE ARG VAL
SEQRES 13 A 540 LEU GLU ARG THR ASN ALA VAL ASP LEU ILE VAL SER ASP
SEQRES 14 A 540 LYS ILE GLY LEU PRO GLY THR ARG ARG VAL VAL GLY ALA
SEQRES 15 A 540 TRP VAL TRP ASN ARG ASN LYS GLU THR VAL GLU THR CYS
SEQRES 16 A 540 HIS ALA LYS ALA VAL VAL LEU ALA THR GLY GLY ALA SER
SEQRES 17 A 540 LYS VAL TYR GLN TYR THR THR ASN PRO ASP ILE SER SER
SEQRES 18 A 540 GLY ASP GLY ILE ALA MET ALA TRP ARG ALA GLY CYS ARG
SEQRES 19 A 540 VAL ALA ASN LEU GLU PHE ASN GLN PHE HIS PRO THR ALA
SEQRES 20 A 540 LEU TYR HIS PRO GLN ALA ARG ASN PHE LEU LEU THR GLU
SEQRES 21 A 540 ALA LEU ARG GLY GLU GLY ALA TYR LEU LYS ARG PRO ASP
SEQRES 22 A 540 GLY THR ARG PHE MET PRO ASP PHE ASP GLU ARG GLY GLU
SEQRES 23 A 540 LEU ALA PRO ARG ASP ILE VAL ALA ARG ALA ILE ASP HIS
SEQRES 24 A 540 GLU MET LYS ARG LEU GLY ALA ASP CYS MET PHE LEU ASP
SEQRES 25 A 540 ILE SER HIS LYS PRO ALA ASP PHE ILE ARG GLN HIS PHE
SEQRES 26 A 540 PRO MET ILE TYR GLU LYS LEU LEU GLY LEU GLY ILE ASP
SEQRES 27 A 540 LEU THR GLN GLU PRO VAL PRO ILE VAL PRO ALA ALA HIS
SEQRES 28 A 540 TYR THR CYS GLY GLY VAL MET VAL ASP ASP HIS GLY ARG
SEQRES 29 A 540 THR ASP VAL GLU GLY LEU TYR ALA ILE GLY GLU VAL SER
SEQRES 30 A 540 TYR THR GLY LEU HIS GLY ALA ASN ARG MET ALA SER ASN
SEQRES 31 A 540 SER LEU LEU GLU CYS LEU VAL TYR GLY TRP SER ALA ALA
SEQRES 32 A 540 GLU ASP ILE THR ARG ARG MET PRO TYR ALA HIS ASP ILE
SEQRES 33 A 540 SER THR LEU PRO PRO TRP ASP GLU SER ARG VAL GLU ASN
SEQRES 34 A 540 PRO ASP GLU ARG VAL VAL ILE GLN HIS ASN TRP HIS GLU
SEQRES 35 A 540 LEU ARG LEU PHE MET TRP ASP TYR VAL GLY ILE VAL ARG
SEQRES 36 A 540 THR THR LYS ARG LEU GLU ARG ALA LEU ARG ARG ILE THR
SEQRES 37 A 540 MET LEU GLN GLN GLU ILE ASP GLU TYR TYR ALA HIS PHE
SEQRES 38 A 540 ARG VAL SER ASN ASN LEU LEU GLU LEU ARG ASN LEU VAL
SEQRES 39 A 540 GLN VAL ALA GLU LEU ILE VAL ARG CYS ALA MET MET ARG
SEQRES 40 A 540 LYS GLU SER ARG GLY LEU HIS PHE THR LEU ASP TYR PRO
SEQRES 41 A 540 GLU LEU LEU THR HIS SER GLY PRO SER ILE LEU SER PRO
SEQRES 42 A 540 GLY ASN HIS TYR ILE ASN ARG
FORMUL 2 HOH *196(H2 O)
HELIX 1 1 ALA A 18 LEU A 27 1 10
HELIX 2 2 THR A 60 ALA A 73 1 14
HELIX 3 3 ARG A 80 GLN A 100 1 21
HELIX 4 4 VAL A 145 ASN A 150 1 6
HELIX 5 5 SER A 168 LYS A 170 5 3
HELIX 6 6 SER A 208 VAL A 210 5 3
HELIX 7 7 PRO A 217 ILE A 219 5 3
HELIX 8 8 ASP A 223 ALA A 231 1 9
HELIX 9 9 GLU A 260 GLY A 264 1 5
HELIX 10 10 MET A 278 ASP A 280 5 3
HELIX 11 11 GLY A 285 LEU A 287 5 3
HELIX 12 12 ARG A 290 ARG A 303 1 14
HELIX 13 13 ALA A 318 HIS A 324 1 7
HELIX 14 14 PRO A 326 LEU A 335 1 10
HELIX 15 15 GLY A 374 VAL A 376 5 3
HELIX 16 16 ASN A 390 ARG A 409 1 20
HELIX 17 17 PRO A 430 TYR A 450 1 21
HELIX 18 18 THR A 457 TYR A 478 1 22
HELIX 19 19 ASN A 485 MET A 506 1 22
SHEET 1 A 5 LEU A 370 ALA A 372 0
SHEET 2 A 5 ALA A 199 LEU A 202 1 N VAL A 200 O TYR A 371
SHEET 3 A 5 VAL A 11 ILE A 14 1 N LEU A 12 O ALA A 199
SHEET 4 A 5 VAL A 33 LEU A 36 1 N ILE A 34 O VAL A 11
SHEET 5 A 5 ILE A 154 LEU A 157 1 N ARG A 155 O VAL A 33
SHEET 1 B 3 THR A 191 HIS A 196 0
SHEET 2 B 3 GLY A 181 ASN A 186 -1 N ASN A 186 O THR A 191
SHEET 3 B 3 THR A 160 ILE A 166 -1 N ILE A 166 O GLY A 181
SHEET 1 C 3 TYR A 268 LYS A 270 0
SHEET 2 C 3 MET A 309 ASP A 312 -1 N ASP A 312 O TYR A 268
SHEET 3 C 3 VAL A 344 ILE A 346 -1 N ILE A 346 O MET A 309
SHEET 1 D 2 ASN A 241 HIS A 244 0
SHEET 2 D 2 ALA A 349 THR A 353 -1 N TYR A 352 O GLN A 242
CRYST1 84.750 84.750 159.730 90.00 90.00 120.00 P 32 2 1 6
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 0.011799 0.006812 0.000000 0.00000
SCALE2 0.000000 0.013625 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006260 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
