| content |
HEADER HYDROLASE 23-MAY-12 4FBM
TITLE LIPS AND LIPT, TWO METAGENOME-DERIVED LIPOLYTIC ENZYMES INCREASE THE
TITLE 2 DIVERSITY OF KNOWN LIPASE AND ESTERASE FAMILIES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPS LIPOLYTIC ENZYME;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: UNIDENTIFIED;
SOURCE 3 ORGANISM_TAXID: 32644;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET21A
KEYWDS THERMOSTABLE, STRUCTURAL GENOMICS, ENZYME FUNCTION INITIATIVE,
KEYWDS 2 STRUCTURAL PROTEOMICS IN EUROPE, SPINE, ALPHA/BETA HYDROLASES,
KEYWDS 3 LIPASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.CHOW,U.KRAUSS,Y.DALL ANTONIA,F.FERSINI,C.SCHMEISSER,M.SCHMIDT,
AUTHOR 2 I.MENYES,U.BORNSCHEUER,B.LAUINGER,P.BONGEN,J.PIETRUSZKA,M.ECKSTEIN,
AUTHOR 3 O.THUM,A.LIESE,J.MUELLER-DIECKMANN,K.-E.JAEGER,F.KOVAVIC,W.R.STREIT,
AUTHOR 4 STRUCTURAL PROTEOMICS IN EUROPE (SPINE)
REVDAT 1 10-OCT-12 4FBM 0
JRNL AUTH J.CHOW,F.KOVACIC,Y.DALL ANTONIA,W.R.KRAUSS,U.STREIT,
JRNL AUTH 2 J.FERSINI,F.MUELLER-DIECKMANN,C.SCHMEISSER,B.LAUINGER,
JRNL AUTH 3 P.BONGEN,J.PIETRUSZKA,M.SCHMIDT,I.MENYES,U.T.BORNSCHEUER,
JRNL AUTH 4 M.ECKSTEIN,O.THUM,A.LIESE
JRNL TITL THE METAGENOME-DERIVED ENZYMES LIPS AND LIPT INCREASE THE
JRNL TITL 2 DIVERSITY OF KNOWN LIPASES
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
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) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.30
REMARK 3 DATA CUTOFF (SIGMA(F)) : 3.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.3
REMARK 3 NUMBER OF REFLECTIONS : 15483
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) : 0.223
REMARK 3 FREE R VALUE : 0.270
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 833
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) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.87
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1143
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.01
REMARK 3 BIN R VALUE (WORKING SET) : 0.3010
REMARK 3 BIN FREE R VALUE SET COUNT : 76
REMARK 3 BIN FREE R VALUE : 0.4210
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3779
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 2
REMARK 3 SOLVENT ATOMS : 37
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 36.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.89
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.53000
REMARK 3 B22 (A**2) : 0.53000
REMARK 3 B33 (A**2) : -1.05000
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): 2.915
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.393
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.317
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 16.578
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.900
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.836
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3874 ; 0.016 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5279 ; 1.649 ; 1.974
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 501 ; 6.231 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 146 ;34.562 ;23.425
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 614 ;21.173 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 24 ;20.646 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 606 ; 0.100 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2920 ; 0.007 ; 0.021
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): 2507 ; 0.703 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4022 ; 1.345 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1367 ; 1.803 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1257 ; 3.160 ; 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 : 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: NULL
REMARK 4
REMARK 4 4FBM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-JUN-12.
REMARK 100 THE RCSB ID CODE IS RCSB072698.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-FEB-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.87
REMARK 200 MONOCHROMATOR : SINGLE CRYSTAL
REMARK 200 OPTICS : SINGLE SILICON (111)
REMARK 200 MONOCHROMATOR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15483
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 46.300
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.7
REMARK 200 DATA REDUNDANCY : 4.600
REMARK 200 R MERGE (I) : 0.19000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 7.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.87
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.9
REMARK 200 DATA REDUNDANCY IN SHELL : 5.00
REMARK 200 R MERGE FOR SHELL (I) : 0.69000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 4FBL,1TQH
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.19
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.69
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS, O.5% V/V JEFFAMINE ED-
REMARK 280 2001, 3.5 M NABR, PH 8.5, VAPOR DIFFUSION, TEMPERATURE 292K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 42 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/2
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/2
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 85.32500
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 85.32500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 23.41500
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 85.32500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 85.32500
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 23.41500
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 85.32500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 85.32500
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 23.41500
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 85.32500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 85.32500
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 23.41500
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2750 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18630 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH B 412 LIES ON A SPECIAL POSITION.
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 SER A 2
REMARK 465 ARG A 3
REMARK 465 LYS A 4
REMARK 465 SER A 5
REMARK 465 ARG A 6
REMARK 465 ASN A 7
REMARK 465 CYS A 8
REMARK 465 ARG A 9
REMARK 465 ASN A 10
REMARK 465 PRO A 11
REMARK 465 PRO A 12
REMARK 465 ARG A 13
REMARK 465 SER A 14
REMARK 465 GLY A 15
REMARK 465 ASP A 16
REMARK 465 ALA A 17
REMARK 465 GLN A 18
REMARK 465 GLN A 19
REMARK 465 ARG A 20
REMARK 465 PRO A 21
REMARK 465 ARG A 22
REMARK 465 GLU A 23
REMARK 465 ARG A 24
REMARK 465 SER A 25
REMARK 465 GLY A 26
REMARK 465 SER A 27
REMARK 465 GLY A 28
REMARK 465 MET A 29
REMARK 465 SER A 30
REMARK 465 THR A 31
REMARK 465 THR A 32
REMARK 465 PRO A 33
REMARK 465 LEU A 34
REMARK 465 GLU A 287
REMARK 465 HIS A 288
REMARK 465 HIS A 289
REMARK 465 HIS A 290
REMARK 465 HIS A 291
REMARK 465 HIS A 292
REMARK 465 HIS A 293
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 ARG B 3
REMARK 465 LYS B 4
REMARK 465 SER B 5
REMARK 465 ARG B 6
REMARK 465 ASN B 7
REMARK 465 CYS B 8
REMARK 465 ARG B 9
REMARK 465 ASN B 10
REMARK 465 PRO B 11
REMARK 465 PRO B 12
REMARK 465 ARG B 13
REMARK 465 SER B 14
REMARK 465 GLY B 15
REMARK 465 ASP B 16
REMARK 465 ALA B 17
REMARK 465 GLN B 18
REMARK 465 GLN B 19
REMARK 465 ARG B 20
REMARK 465 PRO B 21
REMARK 465 ARG B 22
REMARK 465 GLU B 23
REMARK 465 ARG B 24
REMARK 465 SER B 25
REMARK 465 GLY B 26
REMARK 465 SER B 27
REMARK 465 GLY B 28
REMARK 465 MET B 29
REMARK 465 SER B 30
REMARK 465 THR B 31
REMARK 465 THR B 32
REMARK 465 PRO B 33
REMARK 465 LEU B 34
REMARK 465 ALA B 285
REMARK 465 LEU B 286
REMARK 465 GLU B 287
REMARK 465 HIS B 288
REMARK 465 HIS B 289
REMARK 465 HIS B 290
REMARK 465 HIS B 291
REMARK 465 HIS B 292
REMARK 465 HIS B 293
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 A 53 CA - CB - CG ANGL. DEV. = 14.9 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 SER A 48 -167.60 -63.68
REMARK 500 THR A 85 127.08 -39.62
REMARK 500 THR A 89 -90.03 -121.79
REMARK 500 SER A 126 -112.55 70.47
REMARK 500 TYR A 256 -147.95 -95.15
REMARK 500 ASP A 262 -155.66 -65.90
REMARK 500 SER B 48 -162.00 -70.20
REMARK 500 THR B 59 -0.97 69.39
REMARK 500 THR B 89 -95.01 -112.26
REMARK 500 SER B 126 -122.25 66.30
REMARK 500 PHE B 139 75.78 -119.52
REMARK 500 LEU B 188 98.44 -69.18
REMARK 500 PRO B 232 1.04 -66.65
REMARK 500 TYR B 256 -133.89 -98.26
REMARK 500 ASP B 262 -159.12 -81.08
REMARK 500 ALA B 283 -102.27 34.40
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B 412 DISTANCE = 5.19 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR B 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4FBL RELATED DB: PDB
DBREF 4FBM A 1 293 PDB 4FBM 4FBM 1 293
DBREF 4FBM B 1 293 PDB 4FBM 4FBM 1 293
SEQRES 1 A 293 MET SER ARG LYS SER ARG ASN CYS ARG ASN PRO PRO ARG
SEQRES 2 A 293 SER GLY ASP ALA GLN GLN ARG PRO ARG GLU ARG SER GLY
SEQRES 3 A 293 SER GLY MET SER THR THR PRO LEU GLN VAL LEU PRO GLY
SEQRES 4 A 293 ALA GLU PRO LEU TYR SER VAL GLY SER ARG ILE GLY VAL
SEQRES 5 A 293 LEU VAL SER HIS GLY PHE THR GLY SER PRO GLN SER MET
SEQRES 6 A 293 ARG PHE LEU ALA GLU GLY PHE ALA ARG ALA GLY TYR THR
SEQRES 7 A 293 VAL ALA THR PRO ARG LEU THR GLY HIS GLY THR THR PRO
SEQRES 8 A 293 ALA GLU MET ALA ALA SER THR ALA SER ASP TRP THR ALA
SEQRES 9 A 293 ASP ILE VAL ALA ALA MET ARG TRP LEU GLU GLU ARG CYS
SEQRES 10 A 293 ASP VAL LEU PHE MET THR GLY LEU SER MET GLY GLY ALA
SEQRES 11 A 293 LEU THR VAL TRP ALA ALA GLY GLN PHE PRO GLU ARG PHE
SEQRES 12 A 293 ALA GLY ILE MET PRO ILE ASN ALA ALA LEU ARG MET GLU
SEQRES 13 A 293 SER PRO ASP LEU ALA ALA LEU ALA PHE ASN PRO ASP ALA
SEQRES 14 A 293 PRO ALA GLU LEU PRO GLY ILE GLY SER ASP ILE LYS ALA
SEQRES 15 A 293 GLU GLY VAL LYS GLU LEU ALA TYR PRO VAL THR PRO VAL
SEQRES 16 A 293 PRO ALA ILE LYS HIS LEU ILE THR ILE GLY ALA VAL ALA
SEQRES 17 A 293 GLU MET LEU LEU PRO ARG VAL LYS CYS PRO ALA LEU ILE
SEQRES 18 A 293 ILE GLN SER ARG GLU ASP HIS VAL VAL PRO PRO HIS ASN
SEQRES 19 A 293 GLY GLU LEU ILE TYR ASN GLY ILE GLY SER THR GLU LYS
SEQRES 20 A 293 GLU LEU LEU TRP LEU GLU ASN SER TYR HIS VAL ALA THR
SEQRES 21 A 293 LEU ASP ASN ASP LYS GLU LEU ILE LEU GLU ARG SER LEU
SEQRES 22 A 293 ALA PHE ILE ARG LYS HIS SER LYS LEU ALA ALA ALA LEU
SEQRES 23 A 293 GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 293 MET SER ARG LYS SER ARG ASN CYS ARG ASN PRO PRO ARG
SEQRES 2 B 293 SER GLY ASP ALA GLN GLN ARG PRO ARG GLU ARG SER GLY
SEQRES 3 B 293 SER GLY MET SER THR THR PRO LEU GLN VAL LEU PRO GLY
SEQRES 4 B 293 ALA GLU PRO LEU TYR SER VAL GLY SER ARG ILE GLY VAL
SEQRES 5 B 293 LEU VAL SER HIS GLY PHE THR GLY SER PRO GLN SER MET
SEQRES 6 B 293 ARG PHE LEU ALA GLU GLY PHE ALA ARG ALA GLY TYR THR
SEQRES 7 B 293 VAL ALA THR PRO ARG LEU THR GLY HIS GLY THR THR PRO
SEQRES 8 B 293 ALA GLU MET ALA ALA SER THR ALA SER ASP TRP THR ALA
SEQRES 9 B 293 ASP ILE VAL ALA ALA MET ARG TRP LEU GLU GLU ARG CYS
SEQRES 10 B 293 ASP VAL LEU PHE MET THR GLY LEU SER MET GLY GLY ALA
SEQRES 11 B 293 LEU THR VAL TRP ALA ALA GLY GLN PHE PRO GLU ARG PHE
SEQRES 12 B 293 ALA GLY ILE MET PRO ILE ASN ALA ALA LEU ARG MET GLU
SEQRES 13 B 293 SER PRO ASP LEU ALA ALA LEU ALA PHE ASN PRO ASP ALA
SEQRES 14 B 293 PRO ALA GLU LEU PRO GLY ILE GLY SER ASP ILE LYS ALA
SEQRES 15 B 293 GLU GLY VAL LYS GLU LEU ALA TYR PRO VAL THR PRO VAL
SEQRES 16 B 293 PRO ALA ILE LYS HIS LEU ILE THR ILE GLY ALA VAL ALA
SEQRES 17 B 293 GLU MET LEU LEU PRO ARG VAL LYS CYS PRO ALA LEU ILE
SEQRES 18 B 293 ILE GLN SER ARG GLU ASP HIS VAL VAL PRO PRO HIS ASN
SEQRES 19 B 293 GLY GLU LEU ILE TYR ASN GLY ILE GLY SER THR GLU LYS
SEQRES 20 B 293 GLU LEU LEU TRP LEU GLU ASN SER TYR HIS VAL ALA THR
SEQRES 21 B 293 LEU ASP ASN ASP LYS GLU LEU ILE LEU GLU ARG SER LEU
SEQRES 22 B 293 ALA PHE ILE ARG LYS HIS SER LYS LEU ALA ALA ALA LEU
SEQRES 23 B 293 GLU HIS HIS HIS HIS HIS HIS
HET BR A 301 1
HET BR B 301 1
HETNAM BR BROMIDE ION
FORMUL 3 BR 2(BR 1-)
FORMUL 5 HOH *37(H2 O)
HELIX 1 1 SER A 61 SER A 64 5 4
HELIX 2 2 MET A 65 ALA A 75 1 11
HELIX 3 3 THR A 90 SER A 97 1 8
HELIX 4 4 THR A 98 GLU A 115 1 18
HELIX 5 5 SER A 126 PHE A 139 1 14
HELIX 6 6 SER A 157 ALA A 162 1 6
HELIX 7 7 ALA A 197 LEU A 212 1 16
HELIX 8 8 PRO A 213 VAL A 215 5 3
HELIX 9 9 HIS A 233 ASN A 240 1 8
HELIX 10 10 ASP A 264 LYS A 281 1 18
HELIX 11 11 SER B 61 SER B 64 5 4
HELIX 12 12 MET B 65 ALA B 73 1 9
HELIX 13 13 THR B 90 ALA B 96 1 7
HELIX 14 14 THR B 98 CYS B 117 1 20
HELIX 15 15 SER B 126 PHE B 139 1 14
HELIX 16 16 SER B 157 PHE B 165 1 9
HELIX 17 17 ALA B 197 LEU B 211 1 15
HELIX 18 18 LEU B 212 VAL B 215 5 4
HELIX 19 19 PRO B 232 ILE B 242 1 11
HELIX 20 20 VAL B 258 ASP B 262 5 5
HELIX 21 21 ASP B 264 LYS B 281 1 18
SHEET 1 A 4 THR A 78 ALA A 80 0
SHEET 2 A 4 ILE A 50 SER A 55 1 N VAL A 52 O ALA A 80
SHEET 3 A 4 VAL A 119 LEU A 125 1 O VAL A 119 N GLY A 51
SHEET 4 A 4 GLY A 145 ILE A 149 1 O MET A 147 N MET A 122
SHEET 1 B 2 GLU A 172 PRO A 174 0
SHEET 2 B 2 VAL A 192 PRO A 194 -1 O THR A 193 N LEU A 173
SHEET 1 C 2 ALA A 219 SER A 224 0
SHEET 2 C 2 LYS A 247 LEU A 252 1 O LEU A 250 N ILE A 221
SHEET 1 D 5 LEU B 43 SER B 45 0
SHEET 2 D 5 THR B 78 THR B 81 -1 O VAL B 79 N SER B 45
SHEET 3 D 5 ILE B 50 SER B 55 1 N VAL B 54 O ALA B 80
SHEET 4 D 5 VAL B 119 LEU B 125 1 O PHE B 121 N LEU B 53
SHEET 5 D 5 GLY B 145 ILE B 149 1 O MET B 147 N MET B 122
SHEET 1 E 2 GLU B 172 PRO B 174 0
SHEET 2 E 2 VAL B 192 PRO B 194 -1 O THR B 193 N LEU B 173
SHEET 1 F 2 ALA B 219 SER B 224 0
SHEET 2 F 2 LYS B 247 LEU B 252 1 O LEU B 250 N ILE B 221
SITE 1 AC1 2 PHE A 139 GLU A 141
SITE 1 AC2 2 PHE B 139 GLU B 141
CRYST1 170.650 170.650 46.830 90.00 90.00 90.00 P 42 21 2 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 0.005860 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005860 0.000000 0.00000
SCALE3 0.000000 0.000000 0.021354 0.00000
TER 1897 LEU A 286
TER 3781 ALA B 284
MASTER 425 0 2 21 17 0 2 6 3818 2 0 46
END |