HEADER ISOMERASE(INTRAMOLECULAR OXIDOREDUCTASE)22-MAR-94 1TMH
TITLE MODULAR MUTAGENESIS OF A TIM-BARREL ENZYME: THE CRYSTAL STRUCTURE OF A
TITLE 2 CHIMERIC E. COLI TIM HAVING THE EIGHTH (BETA-ALPHA)-UNIT REPLACED BY
TITLE 3 THE EQUIVALENT UNIT OF CHICKEN TIM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRIOSEPHOSPHATE ISOMERASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 EC: 5.3.1.1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562
KEYWDS ISOMERASE(INTRAMOLECULAR OXIDOREDUCTASE)
EXPDTA X-RAY DIFFRACTION
AUTHOR K.V.RADHA KISHAN,J.PH.ZEELEN,R.K.WIERENGA
REVDAT 5 14-FEB-24 1TMH 1 REMARK
REVDAT 4 03-NOV-21 1TMH 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1TMH 1 VERSN
REVDAT 2 31-JUL-94 1TMH 1 COMPND
REVDAT 1 22-JUN-94 1TMH 0
JRNL AUTH R.KISHAN,J.P.ZEELEN,M.E.NOBLE,T.V.BORCHERT,V.MAINFROID,
JRNL AUTH 2 K.GORAJ,J.A.MARTIAL,R.K.WIERENGA
JRNL TITL MODULAR MUTAGENESIS OF A TIM-BARREL ENZYME: THE CRYSTAL
JRNL TITL 2 STRUCTURE OF A CHIMERIC E. COLI TIM HAVING THE EIGHTH BETA
JRNL TITL 3 ALPHA-UNIT REPLACED BY THE EQUIVALENT UNIT OF CHICKEN TIM.
JRNL REF PROTEIN ENG. V. 7 945 1994
JRNL REFN ISSN 0269-2139
JRNL PMID 7809033
JRNL DOI 10.1093/PROTEIN/7.8.945
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.10
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 16883
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.166
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7604
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 20
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.004
REMARK 3 BOND ANGLES (DEGREES) : 1.310
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1TMH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000176731.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : NULL
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.89
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.05
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-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 59.15500
REMARK 290 SMTRY3 2 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: 3810 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18780 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -50.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
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: 3800 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18840 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -50.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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 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 HIS A 5 NE2 HIS A 5 CD2 -0.073
REMARK 500 HIS A 19 NE2 HIS A 19 CD2 -0.066
REMARK 500 HIS A 22 NE2 HIS A 22 CD2 -0.071
REMARK 500 HIS A 60 NE2 HIS A 60 CD2 -0.069
REMARK 500 HIS A 97 NE2 HIS A 97 CD2 -0.098
REMARK 500 HIS A 104 NE2 HIS A 104 CD2 -0.074
REMARK 500 HIS A 189 NE2 HIS A 189 CD2 -0.071
REMARK 500 HIS A 195 NE2 HIS A 195 CD2 -0.073
REMARK 500 HIS B 19 NE2 HIS B 19 CD2 -0.070
REMARK 500 HIS B 60 NE2 HIS B 60 CD2 -0.072
REMARK 500 HIS B 104 NE2 HIS B 104 CD2 -0.072
REMARK 500 HIS C 5 NE2 HIS C 5 CD2 -0.073
REMARK 500 HIS C 97 NE2 HIS C 97 CD2 -0.084
REMARK 500 HIS C 189 NE2 HIS C 189 CD2 -0.070
REMARK 500 HIS C 195 NE2 HIS C 195 CD2 -0.079
REMARK 500 HIS D 22 NE2 HIS D 22 CD2 -0.067
REMARK 500 HIS D 60 NE2 HIS D 60 CD2 -0.068
REMARK 500 HIS D 104 NE2 HIS D 104 CD2 -0.070
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 TRP A 12 CD1 - CG - CD2 ANGL. DEV. = 7.0 DEGREES
REMARK 500 TRP A 12 CE2 - CD2 - CG ANGL. DEV. = -5.7 DEGREES
REMARK 500 ARG A 18 NE - CZ - NH1 ANGL. DEV. = 4.8 DEGREES
REMARK 500 ARG A 18 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG A 29 NE - CZ - NH1 ANGL. DEV. = 5.3 DEGREES
REMARK 500 ARG A 29 NE - CZ - NH2 ANGL. DEV. = -5.0 DEGREES
REMARK 500 CYS A 38 CA - CB - SG ANGL. DEV. = -11.8 DEGREES
REMARK 500 LEU A 63 CA - CB - CG ANGL. DEV. = -15.4 DEGREES
REMARK 500 VAL A 68 CB - CA - C ANGL. DEV. = -14.8 DEGREES
REMARK 500 HIS A 97 CB - CG - CD2 ANGL. DEV. = -10.2 DEGREES
REMARK 500 TYR A 103 CB - CG - CD2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 VAL A 117 CA - CB - CG1 ANGL. DEV. = -9.3 DEGREES
REMARK 500 CYS A 128 CA - CB - SG ANGL. DEV. = -12.5 DEGREES
REMARK 500 TRP A 172 CD1 - CG - CD2 ANGL. DEV. = 6.8 DEGREES
REMARK 500 TRP A 172 CE2 - CD2 - CG ANGL. DEV. = -6.3 DEGREES
REMARK 500 TRP A 172 CG - CD2 - CE3 ANGL. DEV. = 6.1 DEGREES
REMARK 500 VAL A 245 CG1 - CB - CG2 ANGL. DEV. = -11.8 DEGREES
REMARK 500 TRP B 12 CD1 - CG - CD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 TRP B 12 CE2 - CD2 - CG ANGL. DEV. = -5.1 DEGREES
REMARK 500 ARG B 18 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 CYS B 38 CA - CB - SG ANGL. DEV. = -13.7 DEGREES
REMARK 500 TYR B 48 CB - CG - CD2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 VAL B 68 CB - CA - C ANGL. DEV. = -13.4 DEGREES
REMARK 500 THR B 77 CA - C - N ANGL. DEV. = -12.6 DEGREES
REMARK 500 MET B 84 CG - SD - CE ANGL. DEV. = -11.8 DEGREES
REMARK 500 TYR B 92 CB - CG - CD1 ANGL. DEV. = -4.3 DEGREES
REMARK 500 ARG B 100 CA - CB - CG ANGL. DEV. = -13.4 DEGREES
REMARK 500 TRP B 172 CD1 - CG - CD2 ANGL. DEV. = 6.9 DEGREES
REMARK 500 TRP B 172 CE2 - CD2 - CG ANGL. DEV. = -6.1 DEGREES
REMARK 500 ARG B 193 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG B 193 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 TYR B 211 CB - CG - CD2 ANGL. DEV. = -5.0 DEGREES
REMARK 500 TRP C 12 CD1 - CG - CD2 ANGL. DEV. = 6.6 DEGREES
REMARK 500 TRP C 12 CE2 - CD2 - CG ANGL. DEV. = -6.0 DEGREES
REMARK 500 ARG C 18 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ARG C 18 NE - CZ - NH2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 ARG C 29 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG C 29 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 MET C 47 CA - CB - CG ANGL. DEV. = 12.4 DEGREES
REMARK 500 LEU C 63 CA - CB - CG ANGL. DEV. = -14.8 DEGREES
REMARK 500 THR C 77 CA - C - N ANGL. DEV. = -15.7 DEGREES
REMARK 500 TYR C 92 CB - CG - CD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 TYR C 103 CB - CG - CD2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 TRP C 172 CD1 - CG - CD2 ANGL. DEV. = 7.0 DEGREES
REMARK 500 TRP C 172 CE2 - CD2 - CG ANGL. DEV. = -6.0 DEGREES
REMARK 500 ARG C 193 NE - CZ - NH2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 MET D 3 N - CA - C ANGL. DEV. = -16.2 DEGREES
REMARK 500 MET D 9 CA - CB - CG ANGL. DEV. = -10.5 DEGREES
REMARK 500 TRP D 12 CD1 - CG - CD2 ANGL. DEV. = 6.1 DEGREES
REMARK 500 TRP D 12 CE2 - CD2 - CG ANGL. DEV. = -5.0 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 60 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 LYS A 13 -152.46 60.47
REMARK 500 ASP A 69 -168.15 -111.22
REMARK 500 PRO A 170 106.47 -58.13
REMARK 500 LYS B 13 -134.80 52.67
REMARK 500 LEU B 14 67.22 -102.90
REMARK 500 THR B 102 -64.87 -97.12
REMARK 500 VAL B 199 -60.63 -93.00
REMARK 500 LYS C 13 -149.18 57.02
REMARK 500 SER C 59 -164.67 -107.96
REMARK 500 THR C 102 -63.68 -97.59
REMARK 500 SER C 214 54.45 34.11
REMARK 500 GLN C 256 48.44 -102.34
REMARK 500 LYS D 13 -151.73 59.52
REMARK 500 THR D 102 -65.08 -93.85
REMARK 500 LYS D 105 41.24 30.62
REMARK 500 TRP D 172 -8.55 -51.43
REMARK 500 ASP D 200 114.84 -161.63
REMARK 500 GLN D 256 48.49 -82.17
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 TYR A 168 0.07 SIDE CHAIN
REMARK 500 TYR A 211 0.09 SIDE CHAIN
REMARK 500 TYR D 211 0.09 SIDE CHAIN
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 SO4 A 555
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 556
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 557
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 558
DBREF 1TMH A 3 257 UNP P0A858 TPIS_ECOLI 1 255
DBREF 1TMH B 3 257 UNP P0A858 TPIS_ECOLI 1 255
DBREF 1TMH C 3 257 UNP P0A858 TPIS_ECOLI 1 255
DBREF 1TMH D 3 257 UNP P0A858 TPIS_ECOLI 1 255
SEQADV 1TMH HIS A 227 UNP P0A858 PRO 225 ENGINEERED MUTATION
SEQADV 1TMH VAL A 229 UNP P0A858 ILE 227 ENGINEERED MUTATION
SEQADV 1TMH PHE A 232 UNP P0A858 ALA 230 ENGINEERED MUTATION
SEQADV 1TMH PRO A 241 UNP P0A858 ALA 239 ENGINEERED MUTATION
SEQADV 1TMH A UNP P0A858 ASP 240 DELETION
SEQADV 1TMH GLU A 243 UNP P0A858 ALA 241 ENGINEERED MUTATION
SEQADV 1TMH VAL A 245 UNP P0A858 ALA 243 ENGINEERED MUTATION
SEQADV 1TMH ASP A 246 UNP P0A858 VAL 244 ENGINEERED MUTATION
SEQADV 1TMH ILE A 248 UNP P0A858 VAL 246 ENGINEERED MUTATION
SEQADV 1TMH ASN A 249 UNP P0A858 LYS 247 ENGINEERED MUTATION
SEQADV 1TMH HIS B 227 UNP P0A858 PRO 225 ENGINEERED MUTATION
SEQADV 1TMH VAL B 229 UNP P0A858 ILE 227 ENGINEERED MUTATION
SEQADV 1TMH PHE B 232 UNP P0A858 ALA 230 ENGINEERED MUTATION
SEQADV 1TMH PRO B 241 UNP P0A858 ALA 239 ENGINEERED MUTATION
SEQADV 1TMH B UNP P0A858 ASP 240 DELETION
SEQADV 1TMH GLU B 243 UNP P0A858 ALA 241 ENGINEERED MUTATION
SEQADV 1TMH VAL B 245 UNP P0A858 ALA 243 ENGINEERED MUTATION
SEQADV 1TMH ASP B 246 UNP P0A858 VAL 244 ENGINEERED MUTATION
SEQADV 1TMH ILE B 248 UNP P0A858 VAL 246 ENGINEERED MUTATION
SEQADV 1TMH ASN B 249 UNP P0A858 LYS 247 ENGINEERED MUTATION
SEQADV 1TMH HIS C 227 UNP P0A858 PRO 225 ENGINEERED MUTATION
SEQADV 1TMH VAL C 229 UNP P0A858 ILE 227 ENGINEERED MUTATION
SEQADV 1TMH PHE C 232 UNP P0A858 ALA 230 ENGINEERED MUTATION
SEQADV 1TMH PRO C 241 UNP P0A858 ALA 239 ENGINEERED MUTATION
SEQADV 1TMH C UNP P0A858 ASP 240 DELETION
SEQADV 1TMH GLU C 243 UNP P0A858 ALA 241 ENGINEERED MUTATION
SEQADV 1TMH VAL C 245 UNP P0A858 ALA 243 ENGINEERED MUTATION
SEQADV 1TMH ASP C 246 UNP P0A858 VAL 244 ENGINEERED MUTATION
SEQADV 1TMH ILE C 248 UNP P0A858 VAL 246 ENGINEERED MUTATION
SEQADV 1TMH ASN C 249 UNP P0A858 LYS 247 ENGINEERED MUTATION
SEQADV 1TMH HIS D 227 UNP P0A858 PRO 225 ENGINEERED MUTATION
SEQADV 1TMH VAL D 229 UNP P0A858 ILE 227 ENGINEERED MUTATION
SEQADV 1TMH PHE D 232 UNP P0A858 ALA 230 ENGINEERED MUTATION
SEQADV 1TMH PRO D 241 UNP P0A858 ALA 239 ENGINEERED MUTATION
SEQADV 1TMH D UNP P0A858 ASP 240 DELETION
SEQADV 1TMH GLU D 243 UNP P0A858 ALA 241 ENGINEERED MUTATION
SEQADV 1TMH VAL D 245 UNP P0A858 ALA 243 ENGINEERED MUTATION
SEQADV 1TMH ASP D 246 UNP P0A858 VAL 244 ENGINEERED MUTATION
SEQADV 1TMH ILE D 248 UNP P0A858 VAL 246 ENGINEERED MUTATION
SEQADV 1TMH ASN D 249 UNP P0A858 LYS 247 ENGINEERED MUTATION
SEQRES 1 A 254 MET ARG HIS PRO LEU VAL MET GLY ASN TRP LYS LEU ASN
SEQRES 2 A 254 GLY SER ARG HIS MET VAL HIS GLU LEU VAL SER ASN LEU
SEQRES 3 A 254 ARG LYS GLU LEU ALA GLY VAL ALA GLY CYS ALA VAL ALA
SEQRES 4 A 254 ILE ALA PRO PRO GLU MET TYR ILE ASP MET ALA LYS ARG
SEQRES 5 A 254 GLU ALA GLU GLY SER HIS ILE MET LEU GLY ALA GLN ASN
SEQRES 6 A 254 VAL ASP LEU ASN LEU SER GLY ALA PHE THR GLY GLU THR
SEQRES 7 A 254 SER ALA ALA MET LEU LYS ASP ILE GLY ALA GLN TYR ILE
SEQRES 8 A 254 ILE ILE GLY HIS SER GLU ARG ARG THR TYR HIS LYS GLU
SEQRES 9 A 254 SER ASP GLU LEU ILE ALA LYS LYS PHE ALA VAL LEU LYS
SEQRES 10 A 254 GLU GLN GLY LEU THR PRO VAL LEU CYS ILE GLY GLU THR
SEQRES 11 A 254 GLU ALA GLU ASN GLU ALA GLY LYS THR GLU GLU VAL CYS
SEQRES 12 A 254 ALA ARG GLN ILE ASP ALA VAL LEU LYS THR GLN GLY ALA
SEQRES 13 A 254 ALA ALA PHE GLU GLY ALA VAL ILE ALA TYR GLU PRO VAL
SEQRES 14 A 254 TRP ALA ILE GLY THR GLY LYS SER ALA THR PRO ALA GLN
SEQRES 15 A 254 ALA GLN ALA VAL HIS LYS PHE ILE ARG ASP HIS ILE ALA
SEQRES 16 A 254 LYS VAL ASP ALA ASN ILE ALA GLU GLN VAL ILE ILE GLN
SEQRES 17 A 254 TYR GLY GLY SER VAL ASN ALA SER ASN ALA ALA GLU LEU
SEQRES 18 A 254 PHE ALA GLN HIS ASP VAL ASP GLY PHE LEU VAL GLY GLY
SEQRES 19 A 254 ALA SER LEU LYS PRO GLU PHE VAL ASP ILE ILE ASN ALA
SEQRES 20 A 254 ALA GLU ALA ALA LYS GLN ALA
SEQRES 1 B 254 MET ARG HIS PRO LEU VAL MET GLY ASN TRP LYS LEU ASN
SEQRES 2 B 254 GLY SER ARG HIS MET VAL HIS GLU LEU VAL SER ASN LEU
SEQRES 3 B 254 ARG LYS GLU LEU ALA GLY VAL ALA GLY CYS ALA VAL ALA
SEQRES 4 B 254 ILE ALA PRO PRO GLU MET TYR ILE ASP MET ALA LYS ARG
SEQRES 5 B 254 GLU ALA GLU GLY SER HIS ILE MET LEU GLY ALA GLN ASN
SEQRES 6 B 254 VAL ASP LEU ASN LEU SER GLY ALA PHE THR GLY GLU THR
SEQRES 7 B 254 SER ALA ALA MET LEU LYS ASP ILE GLY ALA GLN TYR ILE
SEQRES 8 B 254 ILE ILE GLY HIS SER GLU ARG ARG THR TYR HIS LYS GLU
SEQRES 9 B 254 SER ASP GLU LEU ILE ALA LYS LYS PHE ALA VAL LEU LYS
SEQRES 10 B 254 GLU GLN GLY LEU THR PRO VAL LEU CYS ILE GLY GLU THR
SEQRES 11 B 254 GLU ALA GLU ASN GLU ALA GLY LYS THR GLU GLU VAL CYS
SEQRES 12 B 254 ALA ARG GLN ILE ASP ALA VAL LEU LYS THR GLN GLY ALA
SEQRES 13 B 254 ALA ALA PHE GLU GLY ALA VAL ILE ALA TYR GLU PRO VAL
SEQRES 14 B 254 TRP ALA ILE GLY THR GLY LYS SER ALA THR PRO ALA GLN
SEQRES 15 B 254 ALA GLN ALA VAL HIS LYS PHE ILE ARG ASP HIS ILE ALA
SEQRES 16 B 254 LYS VAL ASP ALA ASN ILE ALA GLU GLN VAL ILE ILE GLN
SEQRES 17 B 254 TYR GLY GLY SER VAL ASN ALA SER ASN ALA ALA GLU LEU
SEQRES 18 B 254 PHE ALA GLN HIS ASP VAL ASP GLY PHE LEU VAL GLY GLY
SEQRES 19 B 254 ALA SER LEU LYS PRO GLU PHE VAL ASP ILE ILE ASN ALA
SEQRES 20 B 254 ALA GLU ALA ALA LYS GLN ALA
SEQRES 1 C 254 MET ARG HIS PRO LEU VAL MET GLY ASN TRP LYS LEU ASN
SEQRES 2 C 254 GLY SER ARG HIS MET VAL HIS GLU LEU VAL SER ASN LEU
SEQRES 3 C 254 ARG LYS GLU LEU ALA GLY VAL ALA GLY CYS ALA VAL ALA
SEQRES 4 C 254 ILE ALA PRO PRO GLU MET TYR ILE ASP MET ALA LYS ARG
SEQRES 5 C 254 GLU ALA GLU GLY SER HIS ILE MET LEU GLY ALA GLN ASN
SEQRES 6 C 254 VAL ASP LEU ASN LEU SER GLY ALA PHE THR GLY GLU THR
SEQRES 7 C 254 SER ALA ALA MET LEU LYS ASP ILE GLY ALA GLN TYR ILE
SEQRES 8 C 254 ILE ILE GLY HIS SER GLU ARG ARG THR TYR HIS LYS GLU
SEQRES 9 C 254 SER ASP GLU LEU ILE ALA LYS LYS PHE ALA VAL LEU LYS
SEQRES 10 C 254 GLU GLN GLY LEU THR PRO VAL LEU CYS ILE GLY GLU THR
SEQRES 11 C 254 GLU ALA GLU ASN GLU ALA GLY LYS THR GLU GLU VAL CYS
SEQRES 12 C 254 ALA ARG GLN ILE ASP ALA VAL LEU LYS THR GLN GLY ALA
SEQRES 13 C 254 ALA ALA PHE GLU GLY ALA VAL ILE ALA TYR GLU PRO VAL
SEQRES 14 C 254 TRP ALA ILE GLY THR GLY LYS SER ALA THR PRO ALA GLN
SEQRES 15 C 254 ALA GLN ALA VAL HIS LYS PHE ILE ARG ASP HIS ILE ALA
SEQRES 16 C 254 LYS VAL ASP ALA ASN ILE ALA GLU GLN VAL ILE ILE GLN
SEQRES 17 C 254 TYR GLY GLY SER VAL ASN ALA SER ASN ALA ALA GLU LEU
SEQRES 18 C 254 PHE ALA GLN HIS ASP VAL ASP GLY PHE LEU VAL GLY GLY
SEQRES 19 C 254 ALA SER LEU LYS PRO GLU PHE VAL ASP ILE ILE ASN ALA
SEQRES 20 C 254 ALA GLU ALA ALA LYS GLN ALA
SEQRES 1 D 254 MET ARG HIS PRO LEU VAL MET GLY ASN TRP LYS LEU ASN
SEQRES 2 D 254 GLY SER ARG HIS MET VAL HIS GLU LEU VAL SER ASN LEU
SEQRES 3 D 254 ARG LYS GLU LEU ALA GLY VAL ALA GLY CYS ALA VAL ALA
SEQRES 4 D 254 ILE ALA PRO PRO GLU MET TYR ILE ASP MET ALA LYS ARG
SEQRES 5 D 254 GLU ALA GLU GLY SER HIS ILE MET LEU GLY ALA GLN ASN
SEQRES 6 D 254 VAL ASP LEU ASN LEU SER GLY ALA PHE THR GLY GLU THR
SEQRES 7 D 254 SER ALA ALA MET LEU LYS ASP ILE GLY ALA GLN TYR ILE
SEQRES 8 D 254 ILE ILE GLY HIS SER GLU ARG ARG THR TYR HIS LYS GLU
SEQRES 9 D 254 SER ASP GLU LEU ILE ALA LYS LYS PHE ALA VAL LEU LYS
SEQRES 10 D 254 GLU GLN GLY LEU THR PRO VAL LEU CYS ILE GLY GLU THR
SEQRES 11 D 254 GLU ALA GLU ASN GLU ALA GLY LYS THR GLU GLU VAL CYS
SEQRES 12 D 254 ALA ARG GLN ILE ASP ALA VAL LEU LYS THR GLN GLY ALA
SEQRES 13 D 254 ALA ALA PHE GLU GLY ALA VAL ILE ALA TYR GLU PRO VAL
SEQRES 14 D 254 TRP ALA ILE GLY THR GLY LYS SER ALA THR PRO ALA GLN
SEQRES 15 D 254 ALA GLN ALA VAL HIS LYS PHE ILE ARG ASP HIS ILE ALA
SEQRES 16 D 254 LYS VAL ASP ALA ASN ILE ALA GLU GLN VAL ILE ILE GLN
SEQRES 17 D 254 TYR GLY GLY SER VAL ASN ALA SER ASN ALA ALA GLU LEU
SEQRES 18 D 254 PHE ALA GLN HIS ASP VAL ASP GLY PHE LEU VAL GLY GLY
SEQRES 19 D 254 ALA SER LEU LYS PRO GLU PHE VAL ASP ILE ILE ASN ALA
SEQRES 20 D 254 ALA GLU ALA ALA LYS GLN ALA
HET SO4 A 555 5
HET SO4 B 556 5
HET SO4 C 557 5
HET SO4 D 558 5
HETNAM SO4 SULFATE ION
FORMUL 5 SO4 4(O4 S 2-)
HELIX 1 1 SER A 17 LEU A 32 1 16
HELIX 2 2 PRO A 45 MET A 47 5 3
HELIX 3 3 TYR A 48 GLU A 57 1 10
HELIX 4 4 SER A 81 GLY A 89 1 9
HELIX 5 5 HIS A 97 THR A 102 1 6
HELIX 6 6 SER A 107 GLY A 122 1 16
HELIX 7 7 THR A 132 GLY A 139 1 8
HELIX 8 8 LYS A 140 LYS A 154 1 15
HELIX 9 9 GLY A 157 GLU A 162 5 6
HELIX 10 10 PRO A 170 ILE A 174 5 5
HELIX 11 11 THR A 181 LYS A 198 1 18
HELIX 12 12 ASP A 200 VAL A 207 1 8
HELIX 13 13 ASN A 216 ALA A 225 1 10
HELIX 14 14 GLY A 235 LYS A 240 5 6
HELIX 15 15 PRO A 241 GLN A 256 1 15
HELIX 16 16 SER B 17 LEU B 32 1 16
HELIX 17 17 PRO B 45 MET B 47 5 3
HELIX 18 18 TYR B 48 GLU B 57 1 10
HELIX 19 19 SER B 81 GLY B 89 1 9
HELIX 20 20 HIS B 97 THR B 102 1 6
HELIX 21 21 SER B 107 GLY B 122 1 16
HELIX 22 22 THR B 132 GLY B 139 1 8
HELIX 23 23 LYS B 140 GLY B 157 1 18
HELIX 24 24 ALA B 158 GLU B 162 5 5
HELIX 25 25 PRO B 170 ILE B 174 5 5
HELIX 26 26 THR B 181 LYS B 198 1 18
HELIX 27 27 ASP B 200 VAL B 207 1 8
HELIX 28 28 ASN B 216 ALA B 225 1 10
HELIX 29 29 GLY B 235 LYS B 240 5 6
HELIX 30 30 PRO B 241 GLN B 256 1 15
HELIX 31 31 SER C 17 LEU C 32 1 16
HELIX 32 32 PRO C 45 MET C 47 5 3
HELIX 33 33 TYR C 48 GLU C 57 1 10
HELIX 34 34 SER C 81 GLY C 89 1 9
HELIX 35 35 HIS C 97 HIS C 104 1 8
HELIX 36 36 SER C 107 GLY C 122 1 16
HELIX 37 37 THR C 132 GLY C 139 1 8
HELIX 38 38 LYS C 140 GLY C 157 1 18
HELIX 39 39 ALA C 158 GLU C 162 5 5
HELIX 40 40 PRO C 170 ILE C 174 5 5
HELIX 41 41 THR C 181 LYS C 198 1 18
HELIX 42 42 ASP C 200 VAL C 207 1 8
HELIX 43 43 ASN C 216 ALA C 225 1 10
HELIX 44 44 GLY C 235 LYS C 240 5 6
HELIX 45 45 PRO C 241 GLN C 256 1 15
HELIX 46 46 SER D 17 LEU D 32 1 16
HELIX 47 47 PRO D 45 MET D 47 5 3
HELIX 48 48 TYR D 48 GLU D 57 1 10
HELIX 49 49 SER D 81 GLY D 89 1 9
HELIX 50 50 HIS D 97 THR D 102 1 6
HELIX 51 51 SER D 107 GLN D 121 1 15
HELIX 52 52 THR D 132 ALA D 138 1 7
HELIX 53 53 LYS D 140 GLY D 157 1 18
HELIX 54 54 ALA D 158 GLU D 162 5 5
HELIX 55 55 PRO D 170 ILE D 174 5 5
HELIX 56 56 THR D 181 ASP D 200 1 20
HELIX 57 57 ASP D 200 VAL D 207 1 8
HELIX 58 58 ASN D 216 ALA D 225 1 10
HELIX 59 59 GLY D 235 LYS D 240 5 6
HELIX 60 60 PRO D 241 GLN D 256 1 15
SHEET 1 A 9 LEU A 7 ASN A 11 0
SHEET 2 A 9 ALA A 39 ALA A 43 1 O ALA A 39 N VAL A 8
SHEET 3 A 9 MET A 62 ALA A 65 1 O MET A 62 N ILE A 42
SHEET 4 A 9 TYR A 92 ILE A 95 1 O TYR A 92 N ALA A 65
SHEET 5 A 9 THR A 124 ILE A 129 1 O THR A 124 N ILE A 93
SHEET 6 A 9 VAL A 165 TYR A 168 1 O VAL A 165 N LEU A 127
SHEET 7 A 9 ILE A 208 GLY A 212 1 O ILE A 208 N ILE A 166
SHEET 8 A 9 GLY A 231 VAL A 234 1 O GLY A 231 N TYR A 211
SHEET 9 A 9 LEU A 7 ASN A 11 1 O LEU A 7 N PHE A 232
SHEET 1 B 9 LEU B 7 ASN B 11 0
SHEET 2 B 9 ALA B 39 ALA B 43 1 O ALA B 39 N VAL B 8
SHEET 3 B 9 ILE B 61 ALA B 65 1 N MET B 62 O VAL B 40
SHEET 4 B 9 TYR B 92 ILE B 95 1 O TYR B 92 N ALA B 65
SHEET 5 B 9 THR B 124 ILE B 129 1 O THR B 124 N ILE B 93
SHEET 6 B 9 VAL B 165 TYR B 168 1 N VAL B 165 O PRO B 125
SHEET 7 B 9 ILE B 208 TYR B 211 1 O ILE B 208 N ILE B 166
SHEET 8 B 9 GLY B 231 VAL B 234 1 O GLY B 231 N TYR B 211
SHEET 9 B 9 LEU B 7 ASN B 11 1 O LEU B 7 N PHE B 232
SHEET 1 C 9 LEU C 7 ASN C 11 0
SHEET 2 C 9 VAL C 40 ALA C 43 1 O ALA C 41 N GLY C 10
SHEET 3 C 9 ILE C 61 ALA C 65 1 N MET C 62 O VAL C 40
SHEET 4 C 9 TYR C 92 ILE C 95 1 O TYR C 92 N ALA C 65
SHEET 5 C 9 THR C 124 ILE C 129 1 O THR C 124 N ILE C 93
SHEET 6 C 9 VAL C 165 TYR C 168 1 O VAL C 165 N LEU C 127
SHEET 7 C 9 ILE C 208 GLY C 212 1 O ILE C 208 N ILE C 166
SHEET 8 C 9 GLY C 231 VAL C 234 1 O GLY C 231 N TYR C 211
SHEET 9 C 9 LEU C 7 ASN C 11 1 O LEU C 7 N PHE C 232
SHEET 1 D 9 LEU D 7 ASN D 11 0
SHEET 2 D 9 ALA D 39 ALA D 43 1 O ALA D 39 N VAL D 8
SHEET 3 D 9 ILE D 61 ALA D 65 1 O MET D 62 N ILE D 42
SHEET 4 D 9 TYR D 92 ILE D 95 1 O TYR D 92 N ALA D 65
SHEET 5 D 9 THR D 124 ILE D 129 1 O THR D 124 N ILE D 93
SHEET 6 D 9 VAL D 165 TYR D 168 1 O VAL D 165 N LEU D 127
SHEET 7 D 9 ILE D 208 TYR D 211 1 O ILE D 208 N ILE D 166
SHEET 8 D 9 GLY D 231 VAL D 234 1 O GLY D 231 N TYR D 211
SHEET 9 D 9 LEU D 7 ASN D 11 1 O LEU D 7 N PHE D 232
SITE 1 AC1 6 ILE A 174 GLY A 175 GLY A 213 SER A 214
SITE 2 AC1 6 GLY A 235 GLY A 236
SITE 1 AC2 5 ILE B 174 GLY B 175 SER B 214 GLY B 235
SITE 2 AC2 5 GLY B 236
SITE 1 AC3 5 ILE C 174 GLY C 175 SER C 214 GLY C 235
SITE 2 AC3 5 GLY C 236
SITE 1 AC4 6 LYS D 13 ILE D 174 GLY D 175 SER D 214
SITE 2 AC4 6 GLY D 235 GLY D 236
CRYST1 63.640 118.310 58.980 90.00 90.30 90.00 P 1 21 1 8
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 0.015713 0.000000 0.000082 0.00000
SCALE2 0.000000 0.008452 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016955 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
