HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 21-OCT-08 3EYP
TITLE CRYSTAL STRUCTURE OF PUTATIVE ALPHA-L-FUCOSIDASE FROM BACTEROIDES
TITLE 2 THETAIOTAOMICRON
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE ALPHA-L-FUCOSIDASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: PUTATIVE LIPOPROTEIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACTEROIDES THETAIOTAOMICRON;
SOURCE 3 ORGANISM_TAXID: 818;
SOURCE 4 GENE: BT_2192;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: MODIFIED PET26
KEYWDS STRUCTURAL GENOMICS, HYDROLASE, LIPOPROTEIN, PSI-2, PROTEIN STRUCTURE
KEYWDS 2 INITIATIVE, NEW YORK SGX RESEARCH CENTER FOR STRUCTURAL GENOMICS,
KEYWDS 3 NYSGXRC, UNKNOWN FUNCTION
EXPDTA X-RAY DIFFRACTION
AUTHOR J.B.BONANNO,J.FREEMAN,K.T.BAIN,S.HU,R.ROMERO,S.WASSERMAN,J.M.SAUDER,
AUTHOR 2 S.K.BURLEY,S.C.ALMO,NEW YORK SGX RESEARCH CENTER FOR STRUCTURAL
AUTHOR 3 GENOMICS (NYSGXRC)
REVDAT 7 27-DEC-23 3EYP 1 REMARK
REVDAT 6 10-FEB-21 3EYP 1 AUTHOR JRNL REMARK
REVDAT 5 14-NOV-18 3EYP 1 AUTHOR
REVDAT 4 25-OCT-17 3EYP 1 REMARK
REVDAT 3 13-JUL-11 3EYP 1 VERSN
REVDAT 2 24-FEB-09 3EYP 1 VERSN
REVDAT 1 04-NOV-08 3EYP 0
JRNL AUTH J.B.BONANNO,J.FREEMAN,K.T.BAIN,S.HU,R.ROMERO,S.WASSERMAN,
JRNL AUTH 2 J.M.SAUDER,S.K.BURLEY,S.C.ALMO
JRNL TITL CRYSTAL STRUCTURE OF PUTATIVE ALPHA-L-FUCOSIDASE FROM
JRNL TITL 2 BACTEROIDES THETAIOTAOMICRON
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.90 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 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 94091
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) : 0.211
REMARK 3 R VALUE (WORKING SET) : 0.208
REMARK 3 FREE R VALUE : 0.252
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4717
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) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6490
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.3830
REMARK 3 BIN FREE R VALUE SET COUNT : 341
REMARK 3 BIN FREE R VALUE : 0.4340
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7302
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 48
REMARK 3 SOLVENT ATOMS : 638
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 32.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 46.17
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.83000
REMARK 3 B22 (A**2) : -0.60000
REMARK 3 B33 (A**2) : 2.43000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.151
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.146
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.113
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.964
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.964
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.949
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7591 ; 0.019 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 5121 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 10321 ; 1.613 ; 1.938
REMARK 3 BOND ANGLES OTHERS (DEGREES): 12417 ; 1.826 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 927 ; 6.222 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 362 ;32.594 ;23.840
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1203 ;15.212 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 43 ;18.982 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1084 ; 0.105 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 8509 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1612 ; 0.002 ; 0.020
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): 4580 ; 0.901 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1866 ; 0.279 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7365 ; 1.491 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3011 ; 2.579 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2950 ; 3.878 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER 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 : 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 : 1.20
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 3EYP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-OCT-08.
REMARK 100 THE DEPOSITION ID IS D_1000049933.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-OCT-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 31-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97958
REMARK 200 MONOCHROMATOR : DIAMOND
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.2.25
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 94178
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 98.173
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 10.20
REMARK 200 R MERGE (I) : 0.11000
REMARK 200 R SYM (I) : 0.11000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 10.10
REMARK 200 R MERGE FOR SHELL (I) : 0.63900
REMARK 200 R SYM FOR SHELL (I) : 0.63900
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELXCD
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.03
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.80
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.8M AMMONIUM TRI-CITRATE PH 7.0,
REMARK 280 VAPOR DIFFUSION, TEMPERATURE 294K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X,-Y+1/2,Z
REMARK 290 7555 -X+1/2,Y,-Z
REMARK 290 8555 X,-Y,-Z+1/2
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 60.35450
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 79.10350
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 62.59650
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 79.10350
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 60.35450
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 62.59650
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 60.35450
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 62.59650
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 79.10350
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 62.59650
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 60.35450
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
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 79.10350
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: MONOMERIC
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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 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 23
REMARK 465 LYS A 483
REMARK 465 GLU A 484
REMARK 465 GLY A 485
REMARK 465 HIS A 486
REMARK 465 HIS A 487
REMARK 465 HIS A 488
REMARK 465 HIS A 489
REMARK 465 HIS A 490
REMARK 465 HIS A 491
REMARK 465 MET B 23
REMARK 465 LYS B 483
REMARK 465 GLU B 484
REMARK 465 GLY B 485
REMARK 465 HIS B 486
REMARK 465 HIS B 487
REMARK 465 HIS B 488
REMARK 465 HIS B 489
REMARK 465 HIS B 490
REMARK 465 HIS B 491
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 LYS A 354 CG CD CE NZ
REMARK 470 LYS A 356 CG CD CE NZ
REMARK 470 LYS A 396 CG CD CE NZ
REMARK 470 LYS A 427 CG CD CE NZ
REMARK 470 ASN A 428 CG OD1 ND2
REMARK 470 LYS A 453 CG CD CE NZ
REMARK 470 LYS B 205 CG CD CE NZ
REMARK 470 ARG B 298 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 354 CG CD CE NZ
REMARK 470 LYS B 356 CG CD CE NZ
REMARK 470 LYS B 396 CG CD CE NZ
REMARK 470 LYS B 427 CG CD CE NZ
REMARK 470 ASN B 428 CG OD1 ND2
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 ARG A 208 NE - CZ - NH2 ANGL. DEV. = -3.2 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 GLU A 43 -50.96 70.51
REMARK 500 ASN A 72 66.08 -161.12
REMARK 500 ALA A 75 42.40 -152.97
REMARK 500 LYS A 98 116.03 -161.73
REMARK 500 LYS A 220 -122.56 51.55
REMARK 500 ASP A 253 42.74 -97.65
REMARK 500 GLU A 254 -67.53 -21.88
REMARK 500 SER A 307 -79.07 -134.56
REMARK 500 ASN A 373 19.33 55.31
REMARK 500 ASP A 401 20.01 -143.20
REMARK 500 GLN A 439 -74.60 -107.84
REMARK 500 GLU B 43 -51.81 69.42
REMARK 500 ASN B 72 64.10 -158.92
REMARK 500 ALA B 75 53.40 -155.00
REMARK 500 LYS B 220 -127.83 49.81
REMARK 500 ASP B 253 54.93 -113.03
REMARK 500 SER B 307 -72.51 -130.76
REMARK 500 SER B 312 -165.59 -129.85
REMARK 500 ASP B 401 22.27 -149.02
REMARK 500 GLN B 439 -73.41 -110.14
REMARK 500 ILE B 441 -76.19 -113.81
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 GOL A 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 4
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 6
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 5
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 7
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 8
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: NYSGXRC-11092K RELATED DB: TARGETDB
DBREF 3EYP A 26 483 UNP Q8A5P6 Q8A5P6_BACTN 26 483
DBREF 3EYP B 26 483 UNP Q8A5P6 Q8A5P6_BACTN 26 483
SEQADV 3EYP MET A 23 UNP Q8A5P6 EXPRESSION TAG
SEQADV 3EYP SER A 24 UNP Q8A5P6 EXPRESSION TAG
SEQADV 3EYP LEU A 25 UNP Q8A5P6 EXPRESSION TAG
SEQADV 3EYP GLU A 484 UNP Q8A5P6 EXPRESSION TAG
SEQADV 3EYP GLY A 485 UNP Q8A5P6 EXPRESSION TAG
SEQADV 3EYP HIS A 486 UNP Q8A5P6 EXPRESSION TAG
SEQADV 3EYP HIS A 487 UNP Q8A5P6 EXPRESSION TAG
SEQADV 3EYP HIS A 488 UNP Q8A5P6 EXPRESSION TAG
SEQADV 3EYP HIS A 489 UNP Q8A5P6 EXPRESSION TAG
SEQADV 3EYP HIS A 490 UNP Q8A5P6 EXPRESSION TAG
SEQADV 3EYP HIS A 491 UNP Q8A5P6 EXPRESSION TAG
SEQADV 3EYP MET B 23 UNP Q8A5P6 EXPRESSION TAG
SEQADV 3EYP SER B 24 UNP Q8A5P6 EXPRESSION TAG
SEQADV 3EYP LEU B 25 UNP Q8A5P6 EXPRESSION TAG
SEQADV 3EYP GLU B 484 UNP Q8A5P6 EXPRESSION TAG
SEQADV 3EYP GLY B 485 UNP Q8A5P6 EXPRESSION TAG
SEQADV 3EYP HIS B 486 UNP Q8A5P6 EXPRESSION TAG
SEQADV 3EYP HIS B 487 UNP Q8A5P6 EXPRESSION TAG
SEQADV 3EYP HIS B 488 UNP Q8A5P6 EXPRESSION TAG
SEQADV 3EYP HIS B 489 UNP Q8A5P6 EXPRESSION TAG
SEQADV 3EYP HIS B 490 UNP Q8A5P6 EXPRESSION TAG
SEQADV 3EYP HIS B 491 UNP Q8A5P6 EXPRESSION TAG
SEQRES 1 A 469 MET SER LEU ALA PRO CYS GLY LEU VAL PRO SER ALA ARG
SEQRES 2 A 469 GLN LEU GLU TRP TYR ASN ARG GLU MET ILE ALA PHE PHE
SEQRES 3 A 469 HIS PHE GLY ILE ASN THR PHE GLU GLU TYR VAL ASN GLU
SEQRES 4 A 469 GLY ASP GLY LYS ALA SER THR ALA ILE PHE ASN PRO THR
SEQRES 5 A 469 ALA LEU ASP CYS ARG GLN TRP MET GLN THR LEU LYS ALA
SEQRES 6 A 469 ALA GLY ILE PRO ALA ALA ILE LEU THR ALA LYS HIS ALA
SEQRES 7 A 469 ASP GLY PHE CYS LEU TRP PRO SER LYS TYR THR ASP TYR
SEQRES 8 A 469 SER VAL LYS ASN ALA ALA TRP LYS ASN GLY LYS GLY ASP
SEQRES 9 A 469 VAL VAL ARG GLU PHE VAL ASP ALA CYS GLU GLU TYR GLY
SEQRES 10 A 469 LEU LYS ALA GLY ILE TYR LEU GLY PRO HIS ASP ARG HIS
SEQRES 11 A 469 GLU HIS LEU SER PRO LEU TYR THR THR GLU ARG TYR LYS
SEQRES 12 A 469 GLU TYR TYR ALA HIS GLN LEU GLY GLU LEU MET SER ASP
SEQRES 13 A 469 TYR GLY LYS ILE TRP GLU THR TRP TRP ASP GLY ALA GLY
SEQRES 14 A 469 ALA ASP GLU LEU THR THR PRO VAL TYR ARG HIS TRP TYR
SEQRES 15 A 469 LYS ILE VAL ARG GLU LYS GLN PRO ASP CYS VAL ILE PHE
SEQRES 16 A 469 GLY THR LYS ASN SER TYR PRO PHE ALA ASP VAL ARG TRP
SEQRES 17 A 469 MET GLY ASN GLU ALA GLY GLU ALA GLY ASP PRO CYS TRP
SEQRES 18 A 469 ALA THR THR ASP SER VAL ALA ILE ARG ASP GLU ALA GLN
SEQRES 19 A 469 TYR TYR LYS GLY LEU ASN GLU GLY MET LEU ASP GLY ASP
SEQRES 20 A 469 ALA TYR ILE PRO ALA GLU THR ASP VAL SER ILE ARG PRO
SEQRES 21 A 469 SER TRP PHE TYR HIS ALA GLU GLU ASP SER ARG VAL LYS
SEQRES 22 A 469 SER VAL ARG GLU LEU TRP ASP ILE TYR CYS THR SER VAL
SEQRES 23 A 469 GLY ARG ASN SER VAL LEU LEU LEU ASN PHE PRO PRO ASP
SEQRES 24 A 469 ARG ARG GLY LEU ILE HIS SER THR ASP SER LEU HIS ALA
SEQRES 25 A 469 ALA LEU LEU LYS GLN GLY ILE ASP GLU THR PHE SER THR
SEQRES 26 A 469 ASN LEU LEU ARG GLY ALA LYS VAL LYS ALA THR ASN VAL
SEQRES 27 A 469 ARG GLY ALA LYS TYR SER PRO GLU LYS MET LEU ASP ASN
SEQRES 28 A 469 GLU LYS ASN THR TYR PHE ALA GLY LYS ASP GLY GLU VAL
SEQRES 29 A 469 LYS ALA ASP ILE ILE PHE THR LEU PRO LYS THR ILE GLU
SEQRES 30 A 469 PHE ASP CYS LEU MET ILE GLU GLU VAL ILE GLU LEU GLY
SEQRES 31 A 469 HIS ARG THR THR LYS TRP SER VAL GLU TYR THR VAL ASP
SEQRES 32 A 469 GLY LYS ASN TRP ILE THR ILE PRO GLU ALA THR ASP LYS
SEQRES 33 A 469 GLN ALA ILE GLY HIS LYS TRP ILE VAL ARG LEU ALA PRO
SEQRES 34 A 469 VAL LYS ALA LYS GLN VAL ARG LEU ARG ILE GLN ASP GLY
SEQRES 35 A 469 LYS ALA CYS PRO ALA ILE HIS THR PHE GLY VAL TYR LYS
SEQRES 36 A 469 GLN SER PRO VAL PHE LYS GLU GLY HIS HIS HIS HIS HIS
SEQRES 37 A 469 HIS
SEQRES 1 B 469 MET SER LEU ALA PRO CYS GLY LEU VAL PRO SER ALA ARG
SEQRES 2 B 469 GLN LEU GLU TRP TYR ASN ARG GLU MET ILE ALA PHE PHE
SEQRES 3 B 469 HIS PHE GLY ILE ASN THR PHE GLU GLU TYR VAL ASN GLU
SEQRES 4 B 469 GLY ASP GLY LYS ALA SER THR ALA ILE PHE ASN PRO THR
SEQRES 5 B 469 ALA LEU ASP CYS ARG GLN TRP MET GLN THR LEU LYS ALA
SEQRES 6 B 469 ALA GLY ILE PRO ALA ALA ILE LEU THR ALA LYS HIS ALA
SEQRES 7 B 469 ASP GLY PHE CYS LEU TRP PRO SER LYS TYR THR ASP TYR
SEQRES 8 B 469 SER VAL LYS ASN ALA ALA TRP LYS ASN GLY LYS GLY ASP
SEQRES 9 B 469 VAL VAL ARG GLU PHE VAL ASP ALA CYS GLU GLU TYR GLY
SEQRES 10 B 469 LEU LYS ALA GLY ILE TYR LEU GLY PRO HIS ASP ARG HIS
SEQRES 11 B 469 GLU HIS LEU SER PRO LEU TYR THR THR GLU ARG TYR LYS
SEQRES 12 B 469 GLU TYR TYR ALA HIS GLN LEU GLY GLU LEU MET SER ASP
SEQRES 13 B 469 TYR GLY LYS ILE TRP GLU THR TRP TRP ASP GLY ALA GLY
SEQRES 14 B 469 ALA ASP GLU LEU THR THR PRO VAL TYR ARG HIS TRP TYR
SEQRES 15 B 469 LYS ILE VAL ARG GLU LYS GLN PRO ASP CYS VAL ILE PHE
SEQRES 16 B 469 GLY THR LYS ASN SER TYR PRO PHE ALA ASP VAL ARG TRP
SEQRES 17 B 469 MET GLY ASN GLU ALA GLY GLU ALA GLY ASP PRO CYS TRP
SEQRES 18 B 469 ALA THR THR ASP SER VAL ALA ILE ARG ASP GLU ALA GLN
SEQRES 19 B 469 TYR TYR LYS GLY LEU ASN GLU GLY MET LEU ASP GLY ASP
SEQRES 20 B 469 ALA TYR ILE PRO ALA GLU THR ASP VAL SER ILE ARG PRO
SEQRES 21 B 469 SER TRP PHE TYR HIS ALA GLU GLU ASP SER ARG VAL LYS
SEQRES 22 B 469 SER VAL ARG GLU LEU TRP ASP ILE TYR CYS THR SER VAL
SEQRES 23 B 469 GLY ARG ASN SER VAL LEU LEU LEU ASN PHE PRO PRO ASP
SEQRES 24 B 469 ARG ARG GLY LEU ILE HIS SER THR ASP SER LEU HIS ALA
SEQRES 25 B 469 ALA LEU LEU LYS GLN GLY ILE ASP GLU THR PHE SER THR
SEQRES 26 B 469 ASN LEU LEU ARG GLY ALA LYS VAL LYS ALA THR ASN VAL
SEQRES 27 B 469 ARG GLY ALA LYS TYR SER PRO GLU LYS MET LEU ASP ASN
SEQRES 28 B 469 GLU LYS ASN THR TYR PHE ALA GLY LYS ASP GLY GLU VAL
SEQRES 29 B 469 LYS ALA ASP ILE ILE PHE THR LEU PRO LYS THR ILE GLU
SEQRES 30 B 469 PHE ASP CYS LEU MET ILE GLU GLU VAL ILE GLU LEU GLY
SEQRES 31 B 469 HIS ARG THR THR LYS TRP SER VAL GLU TYR THR VAL ASP
SEQRES 32 B 469 GLY LYS ASN TRP ILE THR ILE PRO GLU ALA THR ASP LYS
SEQRES 33 B 469 GLN ALA ILE GLY HIS LYS TRP ILE VAL ARG LEU ALA PRO
SEQRES 34 B 469 VAL LYS ALA LYS GLN VAL ARG LEU ARG ILE GLN ASP GLY
SEQRES 35 B 469 LYS ALA CYS PRO ALA ILE HIS THR PHE GLY VAL TYR LYS
SEQRES 36 B 469 GLN SER PRO VAL PHE LYS GLU GLY HIS HIS HIS HIS HIS
SEQRES 37 B 469 HIS
HET GOL A 2 6
HET GOL A 3 6
HET GOL A 4 6
HET GOL A 6 6
HET GOL B 1 6
HET GOL B 5 6
HET GOL B 7 6
HET GOL B 8 6
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 GOL 8(C3 H8 O3)
FORMUL 11 HOH *638(H2 O)
HELIX 1 1 SER A 33 GLU A 43 1 11
HELIX 2 2 GLY A 51 GLU A 56 5 6
HELIX 3 3 SER A 67 PHE A 71 5 5
HELIX 4 4 ASP A 77 ALA A 88 1 12
HELIX 5 5 SER A 114 ALA A 118 5 5
HELIX 6 6 ALA A 119 LYS A 124 5 6
HELIX 7 7 ASP A 126 GLY A 139 1 14
HELIX 8 8 ASP A 150 LEU A 155 1 6
HELIX 9 9 THR A 160 ASP A 178 1 19
HELIX 10 10 THR A 196 GLN A 211 1 16
HELIX 11 11 THR A 219 ALA A 226 5 8
HELIX 12 12 ASP A 247 ASP A 253 1 7
HELIX 13 13 GLU A 254 GLN A 256 5 3
HELIX 14 14 TYR A 257 GLU A 263 1 7
HELIX 15 15 HIS A 287 VAL A 294 5 8
HELIX 16 16 SER A 296 THR A 306 1 11
HELIX 17 17 SER A 307 ASN A 311 5 5
HELIX 18 18 HIS A 327 SER A 346 1 20
HELIX 19 19 GLY A 362 ASP A 372 5 11
HELIX 20 20 ILE A 409 GLY A 412 5 4
HELIX 21 21 PRO A 433 THR A 436 5 4
HELIX 22 22 SER B 33 GLU B 43 1 11
HELIX 23 23 GLY B 51 GLU B 56 5 6
HELIX 24 24 SER B 67 PHE B 71 5 5
HELIX 25 25 ASP B 77 GLY B 89 1 13
HELIX 26 26 SER B 114 ALA B 118 5 5
HELIX 27 27 ALA B 119 LYS B 124 5 6
HELIX 28 28 ASP B 126 GLY B 139 1 14
HELIX 29 29 ASP B 150 LEU B 155 1 6
HELIX 30 30 THR B 160 ASP B 178 1 19
HELIX 31 31 THR B 196 GLN B 211 1 16
HELIX 32 32 THR B 219 ALA B 226 5 8
HELIX 33 33 ASP B 247 ASP B 253 1 7
HELIX 34 34 GLU B 254 GLN B 256 5 3
HELIX 35 35 TYR B 257 GLU B 263 1 7
HELIX 36 36 HIS B 287 ASP B 291 5 5
HELIX 37 37 SER B 296 THR B 306 1 11
HELIX 38 38 SER B 307 ASN B 311 5 5
HELIX 39 39 HIS B 327 PHE B 345 1 19
HELIX 40 40 GLY B 362 ASP B 372 5 11
HELIX 41 41 ILE B 409 GLY B 412 5 4
HELIX 42 42 PRO B 433 THR B 436 5 4
SHEET 1 A 7 VAL A 215 PHE A 217 0
SHEET 2 A 7 GLU A 184 TRP A 186 1 N THR A 185 O VAL A 215
SHEET 3 A 7 LYS A 141 LEU A 146 1 N ILE A 144 O GLU A 184
SHEET 4 A 7 ALA A 92 LYS A 98 1 N LEU A 95 O TYR A 145
SHEET 5 A 7 MET A 44 PHE A 48 1 N ALA A 46 O ALA A 92
SHEET 6 A 7 VAL A 313 ASN A 317 1 O LEU A 314 N ILE A 45
SHEET 7 A 7 GLU A 275 SER A 279 1 N THR A 276 O LEU A 315
SHEET 1 B 2 THR A 245 THR A 246 0
SHEET 2 B 2 ALA A 270 TYR A 271 -1 O ALA A 270 N THR A 246
SHEET 1 C 4 LYS A 354 ALA A 357 0
SHEET 2 C 4 ALA A 388 GLU A 407 -1 O THR A 393 N LYS A 354
SHEET 3 C 4 ALA A 469 TYR A 476 -1 O TYR A 476 N CYS A 402
SHEET 4 C 4 PHE A 379 ALA A 380 -1 N PHE A 379 O ILE A 470
SHEET 1 D 5 LYS A 354 ALA A 357 0
SHEET 2 D 5 ALA A 388 GLU A 407 -1 O THR A 393 N LYS A 354
SHEET 3 D 5 TRP A 445 GLY A 464 -1 O ILE A 461 N ALA A 388
SHEET 4 D 5 THR A 415 THR A 423 -1 N THR A 423 O LYS A 455
SHEET 5 D 5 ILE A 430 THR A 431 -1 O ILE A 430 N TYR A 422
SHEET 1 E 7 VAL B 215 PHE B 217 0
SHEET 2 E 7 GLU B 184 TRP B 186 1 N THR B 185 O VAL B 215
SHEET 3 E 7 LYS B 141 LEU B 146 1 N ILE B 144 O GLU B 184
SHEET 4 E 7 ALA B 92 LYS B 98 1 N LEU B 95 O TYR B 145
SHEET 5 E 7 MET B 44 PHE B 48 1 N ALA B 46 O ALA B 92
SHEET 6 E 7 VAL B 313 ASN B 317 1 O LEU B 316 N ILE B 45
SHEET 7 E 7 GLU B 275 SER B 279 1 N THR B 276 O LEU B 315
SHEET 1 F 2 THR B 245 THR B 246 0
SHEET 2 F 2 ALA B 270 TYR B 271 -1 O ALA B 270 N THR B 246
SHEET 1 G 4 LYS B 354 ALA B 357 0
SHEET 2 G 4 ALA B 388 GLU B 407 -1 O ILE B 391 N LYS B 356
SHEET 3 G 4 ALA B 469 TYR B 476 -1 O TYR B 476 N CYS B 402
SHEET 4 G 4 PHE B 379 ALA B 380 -1 N PHE B 379 O ILE B 470
SHEET 1 H 5 LYS B 354 ALA B 357 0
SHEET 2 H 5 ALA B 388 GLU B 407 -1 O ILE B 391 N LYS B 356
SHEET 3 H 5 TRP B 445 GLY B 464 -1 O ILE B 461 N ALA B 388
SHEET 4 H 5 THR B 415 THR B 423 -1 N GLU B 421 O ARG B 458
SHEET 5 H 5 ILE B 430 THR B 431 -1 O ILE B 430 N TYR B 422
CISPEP 1 ASP A 240 PRO A 241 0 2.10
CISPEP 2 ASP B 240 PRO B 241 0 6.36
SITE 1 AC1 9 GOL A 3 ASP A 188 GLY A 189 THR A 219
SITE 2 AC1 9 TRP A 230 GLU A 234 GLU A 254 ASP A 277
SITE 3 AC1 9 HOH A 645
SITE 1 AC2 8 GOL A 2 HIS A 49 GLU A 61 HIS A 99
SITE 2 AC2 8 TYR A 145 ASP A 188 TRP A 284 HOH A 612
SITE 1 AC3 4 LYS A 364 TYR A 365 THR A 377 TYR A 378
SITE 1 AC4 5 GLU A 43 TYR A 304 PHE A 345 MET A 404
SITE 2 AC4 5 LYS A 444
SITE 1 AC5 7 GOL B 8 ASP B 188 GLY B 189 THR B 219
SITE 2 AC5 7 TRP B 230 GLU B 234 ASP B 277
SITE 1 AC6 4 LYS B 364 TYR B 365 THR B 377 TYR B 378
SITE 1 AC7 5 GLU B 43 TYR B 304 PHE B 345 MET B 404
SITE 2 AC7 5 LYS B 444
SITE 1 AC8 10 GOL B 1 HIS B 49 GLU B 61 HIS B 99
SITE 2 AC8 10 TYR B 145 ASP B 188 GLU B 234 TRP B 284
SITE 3 AC8 10 HOH B 652 HOH B 791
CRYST1 120.709 125.193 158.207 90.00 90.00 90.00 I 21 21 21 16
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 0.008284 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007988 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006321 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
