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HEADER HYDROLASE 23-MAY-12 4FBL
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, C, D;
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: PETM11
KEYWDS THERMOSTABLE, STRUCTURAL GENOMICS, ENZYME FUNCTION INITIATIVE,
KEYWDS 2 STRUCTURAL PROTEOMICS IN EUROPE, SPINE, ALPHA/BETA HYDROLASE,
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.KOVACIC,W.R.STREIT,
AUTHOR 4 STRUCTURAL PROTEOMICS IN EUROPE (SPINE)
REVDAT 1 10-OCT-12 4FBL 0
JRNL AUTH J.CHOW,F.KOVACIC,Y.DALL ANTONIA,U.KRAUSS,F.FERSINI,
JRNL AUTH 2 C.SCHMEISSER,B.LAUINGER,P.BONGEN,J.PIETRUSZKA,M.SCHMIDT,
JRNL AUTH 3 I.MENYES,U.T.BORNSCHEUER,M.ECKSTEIN,O.THUM,A.LIESE,
JRNL AUTH 4 J.MUELLER-DIECKMANN,K.-E.JAEGER,W.R.STREIT
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. 1.99 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) : 1.99
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.30
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 85910
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) : 0.178
REMARK 3 R VALUE (WORKING SET) : 0.176
REMARK 3 FREE R VALUE : 0.217
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4534
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) : 1.99
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.04
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6324
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.95
REMARK 3 BIN R VALUE (WORKING SET) : 0.2920
REMARK 3 BIN FREE R VALUE SET COUNT : 334
REMARK 3 BIN FREE R VALUE : 0.3190
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7418
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 34
REMARK 3 SOLVENT ATOMS : 608
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 29.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.74
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.90000
REMARK 3 B22 (A**2) : 0.90000
REMARK 3 B33 (A**2) : -1.80000
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): 0.138
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.135
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.100
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.687
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.962
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.941
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7659 ; 0.029 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 10438 ; 2.193 ; 1.979
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 985 ; 6.533 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 294 ;32.334 ;23.537
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1205 ;16.412 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 47 ;20.096 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1189 ; 0.163 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5807 ; 0.013 ; 0.022
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 4921 ; 1.306 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7915 ; 2.160 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2738 ; 3.641 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2523 ; 5.658 ; 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 4FBL 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 RCSB072697.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-NOV-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-2
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 : HORIZONTALLY DIFFRACTING
REMARK 200 MONOCHROMATOR
REMARK 200 OPTICS : MONOCHROMATOR (HORIZONTALLY SIDE
REMARK 200 DIFFRACTING SILICON 111 CRYSTAL)
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 85910
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.990
REMARK 200 RESOLUTION RANGE LOW (A) : 40.300
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 5.100
REMARK 200 R MERGE (I) : 0.11000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.99
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.10
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.00
REMARK 200 R MERGE FOR SHELL (I) : 0.80000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.000
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: 1TQH
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.38
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M NAACETATE, 3 M NACL,0.01 M
REMARK 280 SPERMIDINE, PH 4.5, VAPOR DIFFUSION, TEMPERATURE 292K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 4
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,X,Z
REMARK 290 4555 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 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3630 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17830 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3210 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17730 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -40.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D
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 D 500 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 GLY A -1
REMARK 465 ALA A 0
REMARK 465 MET A 1
REMARK 465 CYS 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 GLY B -1
REMARK 465 ALA B 0
REMARK 465 MET B 1
REMARK 465 CYS 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 GLY C -1
REMARK 465 ALA C 0
REMARK 465 MET C 1
REMARK 465 CYS C 2
REMARK 465 ARG C 3
REMARK 465 LYS C 4
REMARK 465 SER C 5
REMARK 465 ARG C 6
REMARK 465 ASN C 7
REMARK 465 CYS C 8
REMARK 465 ARG C 9
REMARK 465 ASN C 10
REMARK 465 PRO C 11
REMARK 465 PRO C 12
REMARK 465 ARG C 13
REMARK 465 SER C 14
REMARK 465 GLY C 15
REMARK 465 ASP C 16
REMARK 465 ALA C 17
REMARK 465 GLN C 18
REMARK 465 GLN C 19
REMARK 465 ARG C 20
REMARK 465 PRO C 21
REMARK 465 ARG C 22
REMARK 465 GLU C 23
REMARK 465 ARG C 24
REMARK 465 SER C 25
REMARK 465 GLY C 26
REMARK 465 SER C 27
REMARK 465 GLY C 28
REMARK 465 MET C 29
REMARK 465 SER C 30
REMARK 465 THR C 31
REMARK 465 THR C 32
REMARK 465 PRO C 33
REMARK 465 GLY D -1
REMARK 465 ALA D 0
REMARK 465 MET D 1
REMARK 465 CYS D 2
REMARK 465 ARG D 3
REMARK 465 LYS D 4
REMARK 465 SER D 5
REMARK 465 ARG D 6
REMARK 465 ASN D 7
REMARK 465 CYS D 8
REMARK 465 ARG D 9
REMARK 465 ASN D 10
REMARK 465 PRO D 11
REMARK 465 PRO D 12
REMARK 465 ARG D 13
REMARK 465 SER D 14
REMARK 465 GLY D 15
REMARK 465 ASP D 16
REMARK 465 ALA D 17
REMARK 465 GLN D 18
REMARK 465 GLN D 19
REMARK 465 ARG D 20
REMARK 465 PRO D 21
REMARK 465 ARG D 22
REMARK 465 GLU D 23
REMARK 465 ARG D 24
REMARK 465 SER D 25
REMARK 465 GLY D 26
REMARK 465 SER D 27
REMARK 465 GLY D 28
REMARK 465 MET D 29
REMARK 465 SER D 30
REMARK 465 THR D 31
REMARK 465 THR D 32
REMARK 465 PRO D 33
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 ARG B 49 CG CD NE CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 NE2 HIS A 257 N10 SPD A 301 2.08
REMARK 500 OG SER D 126 NE2 HIS D 257 2.11
REMARK 500 OG SER C 126 NE2 HIS C 257 2.13
REMARK 500 OG SER B 126 NE2 HIS B 257 2.15
REMARK 500 OG SER B 126 N10 SPD B 301 2.18
REMARK 500 NE2 HIS B 257 N10 SPD B 301 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 CYS C 117 CB CYS C 117 SG -0.131
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 LYS A 265 CD - CE - NZ ANGL. DEV. = -22.0 DEGREES
REMARK 500 ARG B 271 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 ARG B 271 NE - CZ - NH2 ANGL. DEV. = -4.7 DEGREES
REMARK 500 MET C 65 CG - SD - CE ANGL. DEV. = 10.7 DEGREES
REMARK 500 ARG C 74 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG C 83 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 LEU C 173 CA - CB - CG ANGL. DEV. = 16.8 DEGREES
REMARK 500 ARG C 214 NE - CZ - NH1 ANGL. DEV. = 4.9 DEGREES
REMARK 500 ARG C 214 NE - CZ - NH2 ANGL. DEV. = -5.7 DEGREES
REMARK 500 ARG C 277 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG C 277 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 THR A 59 -5.33 74.12
REMARK 500 THR A 89 -96.70 -136.04
REMARK 500 SER A 126 -116.35 68.86
REMARK 500 TYR A 256 -140.43 -99.75
REMARK 500 THR B 59 -6.19 71.40
REMARK 500 THR B 89 -92.10 -135.37
REMARK 500 SER B 126 -114.39 67.71
REMARK 500 ASP B 168 71.29 -117.30
REMARK 500 PRO B 174 134.11 -30.88
REMARK 500 SER B 178 41.49 72.07
REMARK 500 VAL B 229 -51.92 -124.02
REMARK 500 TYR B 256 -137.40 -103.39
REMARK 500 THR C 89 -90.97 -123.83
REMARK 500 SER C 126 -115.09 61.04
REMARK 500 PRO C 174 142.16 -38.45
REMARK 500 TYR C 256 -138.74 -96.99
REMARK 500 THR D 59 -8.98 73.74
REMARK 500 ALA D 75 5.02 -68.17
REMARK 500 THR D 81 74.85 -119.76
REMARK 500 THR D 89 -94.32 -131.58
REMARK 500 SER D 126 -118.12 64.20
REMARK 500 ALA D 152 72.73 -101.46
REMARK 500 TYR D 256 -142.92 -96.35
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 GLU A 41 24.7 L L OUTSIDE RANGE
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 553 DISTANCE = 5.20 ANGSTROMS
REMARK 525 HOH C 511 DISTANCE = 6.90 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SPD A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SPD B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SPD C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4FBM RELATED DB: PDB
DBREF 4FBL A -1 279 PDB 4FBL 4FBL -1 279
DBREF 4FBL B -1 279 PDB 4FBL 4FBL -1 279
DBREF 4FBL C -1 279 PDB 4FBL 4FBL -1 279
DBREF 4FBL D -1 279 PDB 4FBL 4FBL -1 279
SEQRES 1 A 281 GLY ALA MET CYS ARG LYS SER ARG ASN CYS ARG ASN PRO
SEQRES 2 A 281 PRO ARG SER GLY ASP ALA GLN GLN ARG PRO ARG GLU ARG
SEQRES 3 A 281 SER GLY SER GLY MET SER THR THR PRO LEU GLN VAL LEU
SEQRES 4 A 281 PRO GLY ALA GLU PRO LEU TYR SER VAL GLY SER ARG ILE
SEQRES 5 A 281 GLY VAL LEU VAL SER HIS GLY PHE THR GLY SER PRO GLN
SEQRES 6 A 281 SER MET ARG PHE LEU ALA GLU GLY PHE ALA ARG ALA GLY
SEQRES 7 A 281 TYR THR VAL ALA THR PRO ARG LEU THR GLY HIS GLY THR
SEQRES 8 A 281 THR PRO ALA GLU MET ALA ALA SER THR ALA SER ASP TRP
SEQRES 9 A 281 THR ALA ASP ILE VAL ALA ALA MET ARG TRP LEU GLU GLU
SEQRES 10 A 281 ARG CYS ASP VAL LEU PHE MET THR GLY LEU SER MET GLY
SEQRES 11 A 281 GLY ALA LEU THR VAL TRP ALA ALA GLY GLN PHE PRO GLU
SEQRES 12 A 281 ARG PHE ALA GLY ILE MET PRO ILE ASN ALA ALA LEU ARG
SEQRES 13 A 281 MET GLU SER PRO ASP LEU ALA ALA LEU ALA PHE ASN PRO
SEQRES 14 A 281 ASP ALA PRO ALA GLU LEU PRO GLY ILE GLY SER ASP ILE
SEQRES 15 A 281 LYS ALA GLU GLY VAL LYS GLU LEU ALA TYR PRO VAL THR
SEQRES 16 A 281 PRO VAL PRO ALA ILE LYS HIS LEU ILE THR ILE GLY ALA
SEQRES 17 A 281 VAL ALA GLU MET LEU LEU PRO ARG VAL LYS CYS PRO ALA
SEQRES 18 A 281 LEU ILE ILE GLN SER ARG GLU ASP HIS VAL VAL PRO PRO
SEQRES 19 A 281 HIS ASN GLY GLU LEU ILE TYR ASN GLY ILE GLY SER THR
SEQRES 20 A 281 GLU LYS GLU LEU LEU TRP LEU GLU ASN SER TYR HIS VAL
SEQRES 21 A 281 ALA THR LEU ASP ASN ASP LYS GLU LEU ILE LEU GLU ARG
SEQRES 22 A 281 SER LEU ALA PHE ILE ARG LYS HIS
SEQRES 1 B 281 GLY ALA MET CYS ARG LYS SER ARG ASN CYS ARG ASN PRO
SEQRES 2 B 281 PRO ARG SER GLY ASP ALA GLN GLN ARG PRO ARG GLU ARG
SEQRES 3 B 281 SER GLY SER GLY MET SER THR THR PRO LEU GLN VAL LEU
SEQRES 4 B 281 PRO GLY ALA GLU PRO LEU TYR SER VAL GLY SER ARG ILE
SEQRES 5 B 281 GLY VAL LEU VAL SER HIS GLY PHE THR GLY SER PRO GLN
SEQRES 6 B 281 SER MET ARG PHE LEU ALA GLU GLY PHE ALA ARG ALA GLY
SEQRES 7 B 281 TYR THR VAL ALA THR PRO ARG LEU THR GLY HIS GLY THR
SEQRES 8 B 281 THR PRO ALA GLU MET ALA ALA SER THR ALA SER ASP TRP
SEQRES 9 B 281 THR ALA ASP ILE VAL ALA ALA MET ARG TRP LEU GLU GLU
SEQRES 10 B 281 ARG CYS ASP VAL LEU PHE MET THR GLY LEU SER MET GLY
SEQRES 11 B 281 GLY ALA LEU THR VAL TRP ALA ALA GLY GLN PHE PRO GLU
SEQRES 12 B 281 ARG PHE ALA GLY ILE MET PRO ILE ASN ALA ALA LEU ARG
SEQRES 13 B 281 MET GLU SER PRO ASP LEU ALA ALA LEU ALA PHE ASN PRO
SEQRES 14 B 281 ASP ALA PRO ALA GLU LEU PRO GLY ILE GLY SER ASP ILE
SEQRES 15 B 281 LYS ALA GLU GLY VAL LYS GLU LEU ALA TYR PRO VAL THR
SEQRES 16 B 281 PRO VAL PRO ALA ILE LYS HIS LEU ILE THR ILE GLY ALA
SEQRES 17 B 281 VAL ALA GLU MET LEU LEU PRO ARG VAL LYS CYS PRO ALA
SEQRES 18 B 281 LEU ILE ILE GLN SER ARG GLU ASP HIS VAL VAL PRO PRO
SEQRES 19 B 281 HIS ASN GLY GLU LEU ILE TYR ASN GLY ILE GLY SER THR
SEQRES 20 B 281 GLU LYS GLU LEU LEU TRP LEU GLU ASN SER TYR HIS VAL
SEQRES 21 B 281 ALA THR LEU ASP ASN ASP LYS GLU LEU ILE LEU GLU ARG
SEQRES 22 B 281 SER LEU ALA PHE ILE ARG LYS HIS
SEQRES 1 C 281 GLY ALA MET CYS ARG LYS SER ARG ASN CYS ARG ASN PRO
SEQRES 2 C 281 PRO ARG SER GLY ASP ALA GLN GLN ARG PRO ARG GLU ARG
SEQRES 3 C 281 SER GLY SER GLY MET SER THR THR PRO LEU GLN VAL LEU
SEQRES 4 C 281 PRO GLY ALA GLU PRO LEU TYR SER VAL GLY SER ARG ILE
SEQRES 5 C 281 GLY VAL LEU VAL SER HIS GLY PHE THR GLY SER PRO GLN
SEQRES 6 C 281 SER MET ARG PHE LEU ALA GLU GLY PHE ALA ARG ALA GLY
SEQRES 7 C 281 TYR THR VAL ALA THR PRO ARG LEU THR GLY HIS GLY THR
SEQRES 8 C 281 THR PRO ALA GLU MET ALA ALA SER THR ALA SER ASP TRP
SEQRES 9 C 281 THR ALA ASP ILE VAL ALA ALA MET ARG TRP LEU GLU GLU
SEQRES 10 C 281 ARG CYS ASP VAL LEU PHE MET THR GLY LEU SER MET GLY
SEQRES 11 C 281 GLY ALA LEU THR VAL TRP ALA ALA GLY GLN PHE PRO GLU
SEQRES 12 C 281 ARG PHE ALA GLY ILE MET PRO ILE ASN ALA ALA LEU ARG
SEQRES 13 C 281 MET GLU SER PRO ASP LEU ALA ALA LEU ALA PHE ASN PRO
SEQRES 14 C 281 ASP ALA PRO ALA GLU LEU PRO GLY ILE GLY SER ASP ILE
SEQRES 15 C 281 LYS ALA GLU GLY VAL LYS GLU LEU ALA TYR PRO VAL THR
SEQRES 16 C 281 PRO VAL PRO ALA ILE LYS HIS LEU ILE THR ILE GLY ALA
SEQRES 17 C 281 VAL ALA GLU MET LEU LEU PRO ARG VAL LYS CYS PRO ALA
SEQRES 18 C 281 LEU ILE ILE GLN SER ARG GLU ASP HIS VAL VAL PRO PRO
SEQRES 19 C 281 HIS ASN GLY GLU LEU ILE TYR ASN GLY ILE GLY SER THR
SEQRES 20 C 281 GLU LYS GLU LEU LEU TRP LEU GLU ASN SER TYR HIS VAL
SEQRES 21 C 281 ALA THR LEU ASP ASN ASP LYS GLU LEU ILE LEU GLU ARG
SEQRES 22 C 281 SER LEU ALA PHE ILE ARG LYS HIS
SEQRES 1 D 281 GLY ALA MET CYS ARG LYS SER ARG ASN CYS ARG ASN PRO
SEQRES 2 D 281 PRO ARG SER GLY ASP ALA GLN GLN ARG PRO ARG GLU ARG
SEQRES 3 D 281 SER GLY SER GLY MET SER THR THR PRO LEU GLN VAL LEU
SEQRES 4 D 281 PRO GLY ALA GLU PRO LEU TYR SER VAL GLY SER ARG ILE
SEQRES 5 D 281 GLY VAL LEU VAL SER HIS GLY PHE THR GLY SER PRO GLN
SEQRES 6 D 281 SER MET ARG PHE LEU ALA GLU GLY PHE ALA ARG ALA GLY
SEQRES 7 D 281 TYR THR VAL ALA THR PRO ARG LEU THR GLY HIS GLY THR
SEQRES 8 D 281 THR PRO ALA GLU MET ALA ALA SER THR ALA SER ASP TRP
SEQRES 9 D 281 THR ALA ASP ILE VAL ALA ALA MET ARG TRP LEU GLU GLU
SEQRES 10 D 281 ARG CYS ASP VAL LEU PHE MET THR GLY LEU SER MET GLY
SEQRES 11 D 281 GLY ALA LEU THR VAL TRP ALA ALA GLY GLN PHE PRO GLU
SEQRES 12 D 281 ARG PHE ALA GLY ILE MET PRO ILE ASN ALA ALA LEU ARG
SEQRES 13 D 281 MET GLU SER PRO ASP LEU ALA ALA LEU ALA PHE ASN PRO
SEQRES 14 D 281 ASP ALA PRO ALA GLU LEU PRO GLY ILE GLY SER ASP ILE
SEQRES 15 D 281 LYS ALA GLU GLY VAL LYS GLU LEU ALA TYR PRO VAL THR
SEQRES 16 D 281 PRO VAL PRO ALA ILE LYS HIS LEU ILE THR ILE GLY ALA
SEQRES 17 D 281 VAL ALA GLU MET LEU LEU PRO ARG VAL LYS CYS PRO ALA
SEQRES 18 D 281 LEU ILE ILE GLN SER ARG GLU ASP HIS VAL VAL PRO PRO
SEQRES 19 D 281 HIS ASN GLY GLU LEU ILE TYR ASN GLY ILE GLY SER THR
SEQRES 20 D 281 GLU LYS GLU LEU LEU TRP LEU GLU ASN SER TYR HIS VAL
SEQRES 21 D 281 ALA THR LEU ASP ASN ASP LYS GLU LEU ILE LEU GLU ARG
SEQRES 22 D 281 SER LEU ALA PHE ILE ARG LYS HIS
HET SPD A 301 10
HET CL A 302 1
HET SPD B 301 10
HET CL B 302 1
HET SPD C 301 10
HET CL C 302 1
HET CL D 301 1
HETNAM SPD SPERMIDINE
HETNAM CL CHLORIDE ION
HETSYN SPD N-(2-AMINO-PROPYL)-1,4-DIAMINOBUTANE; PA(34)
FORMUL 5 SPD 3(C7 H19 N3)
FORMUL 6 CL 4(CL 1-)
FORMUL 12 HOH *608(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 ALA A 96 1 7
HELIX 4 4 THR A 98 CYS A 117 1 20
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 PRO A 232 ILE A 242 1 11
HELIX 10 10 VAL A 258 ASP A 262 5 5
HELIX 11 11 ASP A 264 LYS A 278 1 15
HELIX 12 12 SER B 61 SER B 64 5 4
HELIX 13 13 MET B 65 ALA B 75 1 11
HELIX 14 14 THR B 90 ALA B 96 1 7
HELIX 15 15 THR B 98 CYS B 117 1 20
HELIX 16 16 SER B 126 PHE B 139 1 14
HELIX 17 17 SER B 157 ALA B 162 1 6
HELIX 18 18 ALA B 197 LEU B 212 1 16
HELIX 19 19 PRO B 213 VAL B 215 5 3
HELIX 20 20 PRO B 232 ILE B 242 1 11
HELIX 21 21 VAL B 258 ASP B 262 5 5
HELIX 22 22 ASP B 264 HIS B 279 1 16
HELIX 23 23 SER C 61 SER C 64 5 4
HELIX 24 24 MET C 65 ALA C 75 1 11
HELIX 25 25 THR C 90 ALA C 96 1 7
HELIX 26 26 THR C 98 CYS C 117 1 20
HELIX 27 27 SER C 126 PHE C 139 1 14
HELIX 28 28 SER C 157 ALA C 162 1 6
HELIX 29 29 ALA C 197 LEU C 212 1 16
HELIX 30 30 PRO C 213 VAL C 215 5 3
HELIX 31 31 PRO C 232 ILE C 242 1 11
HELIX 32 32 VAL C 258 ASP C 262 5 5
HELIX 33 33 ASP C 264 LYS C 278 1 15
HELIX 34 34 SER D 61 SER D 64 5 4
HELIX 35 35 MET D 65 ALA D 75 1 11
HELIX 36 36 THR D 90 ALA D 96 1 7
HELIX 37 37 THR D 98 GLU D 115 1 18
HELIX 38 38 SER D 126 PHE D 139 1 14
HELIX 39 39 SER D 157 ALA D 162 1 6
HELIX 40 40 ALA D 197 LEU D 212 1 16
HELIX 41 41 PRO D 213 VAL D 215 5 3
HELIX 42 42 PRO D 232 ILE D 242 1 11
HELIX 43 43 VAL D 258 ASP D 262 5 5
HELIX 44 44 ASP D 264 LYS D 278 1 15
SHEET 1 A 5 LEU A 43 SER A 45 0
SHEET 2 A 5 THR A 78 THR A 81 -1 O VAL A 79 N SER A 45
SHEET 3 A 5 ILE A 50 SER A 55 1 N VAL A 54 O ALA A 80
SHEET 4 A 5 VAL A 119 LEU A 125 1 O VAL A 119 N GLY A 51
SHEET 5 A 5 GLY A 145 ILE A 149 1 O ILE A 149 N GLY A 124
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 GLU A 248 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 THR B 81 N LEU B 43
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 VAL B 119 N GLY B 51
SHEET 5 D 5 GLY B 145 ILE B 149 1 O ILE B 149 N GLY B 124
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 GLU B 248 N ILE B 221
SHEET 1 G 5 LEU C 43 SER C 45 0
SHEET 2 G 5 THR C 78 THR C 81 -1 O THR C 81 N LEU C 43
SHEET 3 G 5 ILE C 50 SER C 55 1 N VAL C 54 O ALA C 80
SHEET 4 G 5 VAL C 119 LEU C 125 1 O VAL C 119 N GLY C 51
SHEET 5 G 5 GLY C 145 ILE C 149 1 O ILE C 149 N GLY C 124
SHEET 1 H 2 GLU C 172 PRO C 174 0
SHEET 2 H 2 VAL C 192 PRO C 194 -1 O THR C 193 N LEU C 173
SHEET 1 I 2 ALA C 219 SER C 224 0
SHEET 2 I 2 LYS C 247 LEU C 252 1 O LEU C 252 N GLN C 223
SHEET 1 J 5 LEU D 43 SER D 45 0
SHEET 2 J 5 THR D 78 THR D 81 -1 O VAL D 79 N SER D 45
SHEET 3 J 5 ILE D 50 SER D 55 1 N VAL D 54 O ALA D 80
SHEET 4 J 5 VAL D 119 LEU D 125 1 O VAL D 119 N GLY D 51
SHEET 5 J 5 GLY D 145 ILE D 149 1 O ILE D 149 N GLY D 124
SHEET 1 K 2 GLU D 172 PRO D 174 0
SHEET 2 K 2 VAL D 192 PRO D 194 -1 O THR D 193 N LEU D 173
SHEET 1 L 2 ALA D 219 SER D 224 0
SHEET 2 L 2 LYS D 247 LEU D 252 1 O LEU D 250 N ILE D 221
SITE 1 AC1 12 GLY A 57 PHE A 58 THR A 59 SER A 126
SITE 2 AC1 12 ILE A 176 GLY A 177 GLU A 187 ALA A 189
SITE 3 AC1 12 TYR A 190 HIS A 257 CL A 302 HOH A 423
SITE 1 AC2 5 PHE A 58 SER A 126 MET A 127 SPD A 301
SITE 2 AC2 5 HOH A 495
SITE 1 AC3 15 GLY B 57 PHE B 58 THR B 59 GLY B 60
SITE 2 AC3 15 SER B 126 ILE B 176 GLY B 177 SER B 178
SITE 3 AC3 15 ASP B 179 GLU B 187 VAL B 229 HIS B 257
SITE 4 AC3 15 VAL B 258 CL B 302 HOH B 419
SITE 1 AC4 5 PHE B 58 SER B 126 MET B 127 SPD B 301
SITE 2 AC4 5 HOH B 488
SITE 1 AC5 13 PHE C 58 GLY C 60 SER C 126 ILE C 176
SITE 2 AC5 13 GLY C 177 SER C 178 ASP C 179 GLU C 187
SITE 3 AC5 13 VAL C 229 HIS C 257 VAL C 258 CL C 302
SITE 4 AC5 13 HOH C 441
SITE 1 AC6 5 PHE C 58 SER C 126 MET C 127 SPD C 301
SITE 2 AC6 5 HOH C 568
SITE 1 AC7 4 PHE D 58 SER D 126 MET D 127 HOH D 464
CRYST1 105.270 105.270 120.980 90.00 90.00 90.00 P 4 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 0.009499 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009499 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008266 0.00000
TER 1851 HIS A 279
TER 3713 HIS B 279
TER 5581 HIS C 279
TER 7449 HIS D 279
MASTER 576 0 7 44 36 0 18 6 8060 4 30 88
END |