HEADER TRANSFERASE 05-AUG-98 1BOT
TITLE CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN ESCHERICHIA COLI GLYCEROL
TITLE 2 KINASE AND THE ALLOSTERIC REGULATOR FRUCTOSE 1,6-BISPHOSPHATE.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (GLYCEROL KINASE);
COMPND 3 CHAIN: O, Z;
COMPND 4 EC: 2.7.1.30;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PET;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PET28B;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: GKWT(PET28B)
KEYWDS KINASE, ALLOSTERIC REGULATION, FRUCTOSE BISPHOSPHATE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.ORMO,C.E.BYSTROM,S.J.REMINGTON
REVDAT 5 09-AUG-23 1BOT 1 REMARK
REVDAT 4 13-JUL-11 1BOT 1 VERSN
REVDAT 3 24-FEB-09 1BOT 1 VERSN
REVDAT 2 14-JAN-00 1BOT 4 HEADER COMPND REMARK JRNL
REVDAT 2 2 4 ATOM SOURCE SEQRES
REVDAT 1 19-JAN-99 1BOT 0
JRNL AUTH M.ORMO,C.E.BYSTROM,S.J.REMINGTON
JRNL TITL CRYSTAL STRUCTURE OF A COMPLEX OF ESCHERICHIA COLI GLYCEROL
JRNL TITL 2 KINASE AND AN ALLOSTERIC EFFECTOR FRUCTOSE 1,6-BISPHOSPHATE.
JRNL REF BIOCHEMISTRY V. 37 16565 1998
JRNL REFN ISSN 0006-2960
JRNL PMID 9843423
JRNL DOI 10.1021/BI981616S
REMARK 2
REMARK 2 RESOLUTION. 3.05 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : TNT 5F
REMARK 3 AUTHORS : TRONRUD,TEN EYCK,MATTHEWS
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 81.0
REMARK 3 NUMBER OF REFLECTIONS : 48098
REMARK 3
REMARK 3 USING DATA ABOVE SIGMA CUTOFF.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.219
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
REMARK 3 USING ALL DATA, NO SIGMA CUTOFF.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.2190
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 174719
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7837
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 27
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 WILSON B VALUE (FROM FCALC, A**2) : 25.400
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. RMS WEIGHT COUNT
REMARK 3 BOND LENGTHS (A) : 0.016 ; 3.000 ; 8022
REMARK 3 BOND ANGLES (DEGREES) : 2.563 ; 6.000 ; 9649
REMARK 3 TORSION ANGLES (DEGREES) : 21.071; 0.000 ; 4786
REMARK 3 PSEUDOROTATION ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 TRIGONAL CARBON PLANES (A) : 0.015 ; 4.000 ; 209
REMARK 3 GENERAL PLANES (A) : 0.012 ; 20.000; 1171
REMARK 3 ISOTROPIC THERMAL FACTORS (A**2) : 3.755 ; 10.000; 7997
REMARK 3 NON-BONDED CONTACTS (A) : 0.024 ; 35.000; 367
REMARK 3
REMARK 3 INCORRECT CHIRAL-CENTERS (COUNT) : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : 0.75
REMARK 3 BSOL : 300.0
REMARK 3
REMARK 3 RESTRAINT LIBRARIES.
REMARK 3 STEREOCHEMISTRY : TNT PROTGEO
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS : TNT BCORREL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1BOT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB.
REMARK 100 THE DEPOSITION ID IS D_1000008420.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-MAR-95
REMARK 200 TEMPERATURE (KELVIN) : 102
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : COLLIMATOR
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS II
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 45656
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.050
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 81.0
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : 0.09000
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: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: 1GLA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 81.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 6.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1M SODIUM CITRATE, 0.1M HEPES PH 7.5,
REMARK 280 1MM BME, CRYO PROTECTION WAS ACHIEVED BY SOAKING CRYSTAL IN
REMARK 280 MOTHER LIQUOR CONTAINING 20% GLYCEROL FOR 4 HOURS
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 101.35000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 84.40000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 84.40000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 50.67500
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 84.40000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 84.40000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 152.02500
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 84.40000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 84.40000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 50.67500
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 84.40000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 84.40000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 152.02500
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 101.35000
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,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 4030 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32480 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: O
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 202.70000
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,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 4070 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 33920 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: Z
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 202.70000
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 THR O 1
REMARK 465 GLU O 2
REMARK 465 ASP O 500
REMARK 465 GLU O 501
REMARK 465 THR Z 1
REMARK 465 ASP Z 500
REMARK 465 GLU Z 501
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 GLU O 34 CD GLU O 34 OE2 0.070
REMARK 500 GLU O 51 CD GLU O 51 OE1 0.082
REMARK 500 GLU O 62 CD GLU O 62 OE2 0.082
REMARK 500 GLU O 90 CD GLU O 90 OE2 0.072
REMARK 500 GLU O 92 CD GLU O 92 OE1 0.082
REMARK 500 GLU O 110 CD GLU O 110 OE1 0.076
REMARK 500 GLU O 113 CD GLU O 113 OE2 0.079
REMARK 500 GLU O 121 CD GLU O 121 OE2 0.072
REMARK 500 GLU O 149 CD GLU O 149 OE2 0.077
REMARK 500 GLU O 159 CD GLU O 159 OE2 0.071
REMARK 500 GLU O 205 CD GLU O 205 OE2 0.086
REMARK 500 GLU O 216 CD GLU O 216 OE2 0.117
REMARK 500 GLU O 258 CD GLU O 258 OE2 0.066
REMARK 500 GLU O 283 CD GLU O 283 OE2 0.073
REMARK 500 GLU O 303 CD GLU O 303 OE1 0.071
REMARK 500 GLU O 393 CD GLU O 393 OE1 0.077
REMARK 500 GLU O 431 CD GLU O 431 OE2 0.066
REMARK 500 GLU O 434 CD GLU O 434 OE2 0.074
REMARK 500 GLU O 437 CD GLU O 437 OE1 0.094
REMARK 500 GLU O 462 CD GLU O 462 OE1 0.092
REMARK 500 GLU O 467 CD GLU O 467 OE2 0.077
REMARK 500 GLU O 469 CD GLU O 469 OE1 0.074
REMARK 500 GLU O 478 CD GLU O 478 OE2 0.073
REMARK 500 GLU O 498 CD GLU O 498 OE2 0.076
REMARK 500 GLU Z 2 CD GLU Z 2 OE2 0.070
REMARK 500 GLU Z 34 CD GLU Z 34 OE2 0.123
REMARK 500 GLU Z 51 CD GLU Z 51 OE1 0.079
REMARK 500 GLU Z 62 CD GLU Z 62 OE1 0.079
REMARK 500 GLU Z 92 CD GLU Z 92 OE2 0.088
REMARK 500 GLU Z 110 CD GLU Z 110 OE2 0.081
REMARK 500 GLU Z 149 CD GLU Z 149 OE2 0.076
REMARK 500 GLU Z 153 CD GLU Z 153 OE2 0.072
REMARK 500 GLU Z 205 CD GLU Z 205 OE2 0.089
REMARK 500 GLU Z 216 CD GLU Z 216 OE1 0.071
REMARK 500 GLU Z 222 CD GLU Z 222 OE2 0.069
REMARK 500 GLU Z 258 CD GLU Z 258 OE1 0.079
REMARK 500 GLU Z 277 CD GLU Z 277 OE2 0.066
REMARK 500 GLU Z 330 CD GLU Z 330 OE1 0.086
REMARK 500 GLU Z 382 CD GLU Z 382 OE2 0.069
REMARK 500 GLU Z 393 CD GLU Z 393 OE1 0.087
REMARK 500 GLU Z 431 CD GLU Z 431 OE1 0.068
REMARK 500 GLU Z 434 CD GLU Z 434 OE1 0.078
REMARK 500 GLU Z 437 CD GLU Z 437 OE1 0.070
REMARK 500 GLU Z 459 CD GLU Z 459 OE1 0.069
REMARK 500 GLU Z 462 CD GLU Z 462 OE1 0.074
REMARK 500 GLU Z 475 CD GLU Z 475 OE2 0.093
REMARK 500 GLU Z 478 CD GLU Z 478 OE1 0.068
REMARK 500 GLU Z 498 CD GLU Z 498 OE2 0.076
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 ASP O 24 CB - CG - OD1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ASP O 24 CB - CG - OD2 ANGL. DEV. = -7.3 DEGREES
REMARK 500 PRO O 40 C - N - CD ANGL. DEV. = -14.7 DEGREES
REMARK 500 ASP O 72 CB - CG - OD1 ANGL. DEV. = -6.4 DEGREES
REMARK 500 ARG O 83 O - C - N ANGL. DEV. = -11.1 DEGREES
REMARK 500 THR O 85 CA - CB - CG2 ANGL. DEV. = -10.1 DEGREES
REMARK 500 ARG O 107 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG O 117 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ASP O 118 CB - CG - OD2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 ARG O 152 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ASP O 166 CB - CG - OD1 ANGL. DEV. = -6.7 DEGREES
REMARK 500 ASP O 182 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 ARG O 188 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 ASP O 200 CB - CG - OD1 ANGL. DEV. = -8.7 DEGREES
REMARK 500 ASP O 200 CB - CG - OD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ASP O 201 CB - CG - OD1 ANGL. DEV. = -7.3 DEGREES
REMARK 500 ASP O 245 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 THR O 288 CA - CB - CG2 ANGL. DEV. = -8.9 DEGREES
REMARK 500 THR O 289 N - CA - CB ANGL. DEV. = 12.4 DEGREES
REMARK 500 THR O 289 CA - CB - CG2 ANGL. DEV. = -8.9 DEGREES
REMARK 500 ASP O 318 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP O 325 CB - CG - OD2 ANGL. DEV. = -5.7 DEGREES
REMARK 500 ASP O 328 CB - CG - OD1 ANGL. DEV. = -6.5 DEGREES
REMARK 500 PRO O 358 C - N - CD ANGL. DEV. = -38.1 DEGREES
REMARK 500 ASP O 390 CB - CG - OD1 ANGL. DEV. = -6.0 DEGREES
REMARK 500 ASP O 398 CB - CG - OD1 ANGL. DEV. = -7.6 DEGREES
REMARK 500 ASP O 398 CB - CG - OD2 ANGL. DEV. = 6.1 DEGREES
REMARK 500 ARG O 402 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ASP O 409 CB - CG - OD1 ANGL. DEV. = 6.1 DEGREES
REMARK 500 ASP O 409 CB - CG - OD2 ANGL. DEV. = -8.7 DEGREES
REMARK 500 ASP O 458 CB - CG - OD1 ANGL. DEV. = -5.9 DEGREES
REMARK 500 ASP Z 10 CB - CG - OD1 ANGL. DEV. = -8.0 DEGREES
REMARK 500 ASP Z 10 CB - CG - OD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP Z 24 CB - CG - OD2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 PRO Z 40 C - N - CD ANGL. DEV. = -13.1 DEGREES
REMARK 500 ASP Z 68 CB - CG - OD1 ANGL. DEV. = -6.7 DEGREES
REMARK 500 ASP Z 68 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ASP Z 72 CB - CG - OD1 ANGL. DEV. = -5.5 DEGREES
REMARK 500 ARG Z 83 NE - CZ - NH2 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG Z 83 O - C - N ANGL. DEV. = -9.7 DEGREES
REMARK 500 ASP Z 118 CB - CG - OD1 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ASP Z 118 CB - CG - OD2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 ASP Z 146 CB - CG - OD1 ANGL. DEV. = -7.3 DEGREES
REMARK 500 ASP Z 146 CB - CG - OD2 ANGL. DEV. = 6.3 DEGREES
REMARK 500 ARG Z 152 NE - CZ - NH1 ANGL. DEV. = 6.4 DEGREES
REMARK 500 ARG Z 152 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 THR Z 167 CA - CB - CG2 ANGL. DEV. = -10.2 DEGREES
REMARK 500 ASP Z 182 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 TYR Z 183 CB - CG - CD1 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ARG Z 188 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 69 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 TYR O 39 74.89 -114.50
REMARK 500 LYS O 41 144.08 172.61
REMARK 500 PRO O 42 114.07 -29.00
REMARK 500 ILE O 52 -74.34 -49.43
REMARK 500 ASP O 68 17.25 53.45
REMARK 500 ASP O 72 15.51 -61.68
REMARK 500 TYR O 98 141.03 177.75
REMARK 500 ASN O 99 155.17 -28.30
REMARK 500 ALA O 109 -80.84 28.66
REMARK 500 GLU O 110 -73.79 -34.65
REMARK 500 LYS O 116 -73.32 -27.34
REMARK 500 GLU O 121 -70.97 -20.80
REMARK 500 ASP O 122 -73.65 -55.86
REMARK 500 TYR O 123 -69.31 -27.87
REMARK 500 LYS O 142 -73.58 -46.07
REMARK 500 TRP O 143 -54.86 -27.59
REMARK 500 GLU O 149 -99.84 -20.92
REMARK 500 SER O 151 -93.42 0.20
REMARK 500 THR O 167 -72.26 -45.83
REMARK 500 ALA O 186 -39.09 -38.68
REMARK 500 LEU O 197 42.07 80.06
REMARK 500 ASP O 208 74.87 62.27
REMARK 500 GLU O 222 163.70 165.44
REMARK 500 SER O 240 31.16 -147.58
REMARK 500 TYR O 265 76.97 -101.16
REMARK 500 ALA O 291 -165.93 -128.45
REMARK 500 PRO O 294 -3.23 -44.06
REMARK 500 THR O 295 39.05 -161.04
REMARK 500 ALA O 309 -84.71 -131.76
REMARK 500 GLU O 319 -72.29 -88.56
REMARK 500 TYR O 331 -64.78 -29.77
REMARK 500 ALA O 333 -53.00 -21.40
REMARK 500 ASN O 338 163.07 177.31
REMARK 500 THR O 339 0.99 -65.32
REMARK 500 PRO O 346 47.83 -76.46
REMARK 500 ALA O 347 35.03 -75.98
REMARK 500 LEU O 351 -73.75 -106.17
REMARK 500 ALA O 379 -39.84 -38.73
REMARK 500 TYR O 386 -72.09 -46.97
REMARK 500 ASP O 390 -80.33 -29.92
REMARK 500 LEU O 392 -72.78 -41.98
REMARK 500 GLN O 396 -76.73 -36.84
REMARK 500 ALA O 397 -79.86 -18.31
REMARK 500 GLU O 437 6.20 -67.52
REMARK 500 ALA O 444 -76.69 -46.36
REMARK 500 TYR O 445 -70.35 -28.01
REMARK 500 LEU O 446 -80.58 -37.48
REMARK 500 PHE O 453 -52.97 -23.69
REMARK 500 ASN O 456 152.92 174.77
REMARK 500 THR O 476 -91.06 -2.25
REMARK 500
REMARK 500 THIS ENTRY HAS 93 RAMACHANDRAN OUTLIERS.
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 EPE O 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL O 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL Z 603
DBREF 1BOT O 1 501 UNP P0A6F3 GLPK_ECOLI 1 501
DBREF 1BOT Z 1 501 UNP P0A6F3 GLPK_ECOLI 1 501
SEQRES 1 O 501 THR GLU LYS LYS TYR ILE VAL ALA LEU ASP GLN GLY THR
SEQRES 2 O 501 THR SER SER ARG ALA VAL VAL MET ASP HIS ASP ALA ASN
SEQRES 3 O 501 ILE ILE SER VAL SER GLN ARG GLU PHE GLU GLN ILE TYR
SEQRES 4 O 501 PRO LYS PRO GLY TRP VAL GLU HIS ASP PRO MET GLU ILE
SEQRES 5 O 501 TRP ALA THR GLN SER SER THR LEU VAL GLU VAL LEU ALA
SEQRES 6 O 501 LYS ALA ASP ILE SER SER ASP GLN ILE ALA ALA ILE GLY
SEQRES 7 O 501 ILE THR ASN GLN ARG GLU THR THR ILE VAL TRP GLU LYS
SEQRES 8 O 501 GLU THR GLY LYS PRO ILE TYR ASN ALA ILE VAL TRP GLN
SEQRES 9 O 501 CYS ARG ARG THR ALA GLU ILE CYS GLU HIS LEU LYS ARG
SEQRES 10 O 501 ASP GLY LEU GLU ASP TYR ILE ARG SER ASN THR GLY LEU
SEQRES 11 O 501 VAL ILE ASP PRO TYR PHE SER GLY THR LYS VAL LYS TRP
SEQRES 12 O 501 ILE LEU ASP HIS VAL GLU GLY SER ARG GLU ARG ALA ARG
SEQRES 13 O 501 ARG GLY GLU LEU LEU PHE GLY THR VAL ASP THR TRP LEU
SEQRES 14 O 501 ILE TRP LYS MET THR GLN GLY ARG VAL HIS VAL THR ASP
SEQRES 15 O 501 TYR THR ASN ALA SER ARG THR MET LEU PHE ASN ILE HIS
SEQRES 16 O 501 THR LEU ASP TRP ASP ASP LYS MET LEU GLU VAL LEU ASP
SEQRES 17 O 501 ILE PRO ARG GLU MET LEU PRO GLU VAL ARG ARG SER SER
SEQRES 18 O 501 GLU VAL TYR GLY GLN THR ASN ILE GLY GLY LYS GLY GLY
SEQRES 19 O 501 THR ARG ILE PRO ILE SER GLY ILE ALA GLY ASP GLN GLN
SEQRES 20 O 501 ALA ALA LEU PHE GLY GLN LEU CYS VAL LYS GLU GLY MET
SEQRES 21 O 501 ALA LYS ASN THR TYR GLY THR GLY CYS PHE MET LEU MET
SEQRES 22 O 501 ASN THR GLY GLU LYS ALA VAL LYS SER GLU ASN GLY LEU
SEQRES 23 O 501 LEU THR THR ILE ALA CYS GLY PRO THR GLY GLU VAL ASN
SEQRES 24 O 501 TYR ALA LEU GLU GLY ALA VAL PHE MET ALA GLY ALA SER
SEQRES 25 O 501 ILE GLN TRP LEU ARG ASP GLU MET LYS LEU ILE ASN ASP
SEQRES 26 O 501 ALA TYR ASP SER GLU TYR PHE ALA THR LYS VAL GLN ASN
SEQRES 27 O 501 THR ASN GLY VAL TYR VAL VAL PRO ALA PHE THR GLY LEU
SEQRES 28 O 501 GLY ALA PRO TYR TRP ASP PRO TYR ALA ARG GLY ALA ILE
SEQRES 29 O 501 PHE GLY LEU THR ARG GLY VAL ASN ALA ASN HIS ILE ILE
SEQRES 30 O 501 ARG ALA THR LEU GLU SER ILE ALA TYR GLN THR ARG ASP
SEQRES 31 O 501 VAL LEU GLU ALA MET GLN ALA ASP SER GLY ILE ARG LEU
SEQRES 32 O 501 HIS ALA LEU ARG VAL ASP GLY GLY ALA VAL ALA ASN ASN
SEQRES 33 O 501 PHE LEU MET GLN PHE GLN SER ASP ILE LEU GLY THR ARG
SEQRES 34 O 501 VAL GLU ARG PRO GLU VAL ARG GLU VAL THR ALA LEU GLY
SEQRES 35 O 501 ALA ALA TYR LEU ALA GLY LEU ALA VAL GLY PHE TRP GLN
SEQRES 36 O 501 ASN LEU ASP GLU LEU GLN GLU LYS ALA VAL ILE GLU ARG
SEQRES 37 O 501 GLU PHE ARG PRO GLY ILE GLU THR THR GLU ARG ASN TYR
SEQRES 38 O 501 ARG TYR ALA GLY TRP LYS LYS ALA VAL LYS ARG ALA MET
SEQRES 39 O 501 ALA TRP GLU GLU HIS ASP GLU
SEQRES 1 Z 501 THR GLU LYS LYS TYR ILE VAL ALA LEU ASP GLN GLY THR
SEQRES 2 Z 501 THR SER SER ARG ALA VAL VAL MET ASP HIS ASP ALA ASN
SEQRES 3 Z 501 ILE ILE SER VAL SER GLN ARG GLU PHE GLU GLN ILE TYR
SEQRES 4 Z 501 PRO LYS PRO GLY TRP VAL GLU HIS ASP PRO MET GLU ILE
SEQRES 5 Z 501 TRP ALA THR GLN SER SER THR LEU VAL GLU VAL LEU ALA
SEQRES 6 Z 501 LYS ALA ASP ILE SER SER ASP GLN ILE ALA ALA ILE GLY
SEQRES 7 Z 501 ILE THR ASN GLN ARG GLU THR THR ILE VAL TRP GLU LYS
SEQRES 8 Z 501 GLU THR GLY LYS PRO ILE TYR ASN ALA ILE VAL TRP GLN
SEQRES 9 Z 501 CYS ARG ARG THR ALA GLU ILE CYS GLU HIS LEU LYS ARG
SEQRES 10 Z 501 ASP GLY LEU GLU ASP TYR ILE ARG SER ASN THR GLY LEU
SEQRES 11 Z 501 VAL ILE ASP PRO TYR PHE SER GLY THR LYS VAL LYS TRP
SEQRES 12 Z 501 ILE LEU ASP HIS VAL GLU GLY SER ARG GLU ARG ALA ARG
SEQRES 13 Z 501 ARG GLY GLU LEU LEU PHE GLY THR VAL ASP THR TRP LEU
SEQRES 14 Z 501 ILE TRP LYS MET THR GLN GLY ARG VAL HIS VAL THR ASP
SEQRES 15 Z 501 TYR THR ASN ALA SER ARG THR MET LEU PHE ASN ILE HIS
SEQRES 16 Z 501 THR LEU ASP TRP ASP ASP LYS MET LEU GLU VAL LEU ASP
SEQRES 17 Z 501 ILE PRO ARG GLU MET LEU PRO GLU VAL ARG ARG SER SER
SEQRES 18 Z 501 GLU VAL TYR GLY GLN THR ASN ILE GLY GLY LYS GLY GLY
SEQRES 19 Z 501 THR ARG ILE PRO ILE SER GLY ILE ALA GLY ASP GLN GLN
SEQRES 20 Z 501 ALA ALA LEU PHE GLY GLN LEU CYS VAL LYS GLU GLY MET
SEQRES 21 Z 501 ALA LYS ASN THR TYR GLY THR GLY CYS PHE MET LEU MET
SEQRES 22 Z 501 ASN THR GLY GLU LYS ALA VAL LYS SER GLU ASN GLY LEU
SEQRES 23 Z 501 LEU THR THR ILE ALA CYS GLY PRO THR GLY GLU VAL ASN
SEQRES 24 Z 501 TYR ALA LEU GLU GLY ALA VAL PHE MET ALA GLY ALA SER
SEQRES 25 Z 501 ILE GLN TRP LEU ARG ASP GLU MET LYS LEU ILE ASN ASP
SEQRES 26 Z 501 ALA TYR ASP SER GLU TYR PHE ALA THR LYS VAL GLN ASN
SEQRES 27 Z 501 THR ASN GLY VAL TYR VAL VAL PRO ALA PHE THR GLY LEU
SEQRES 28 Z 501 GLY ALA PRO TYR TRP ASP PRO TYR ALA ARG GLY ALA ILE
SEQRES 29 Z 501 PHE GLY LEU THR ARG GLY VAL ASN ALA ASN HIS ILE ILE
SEQRES 30 Z 501 ARG ALA THR LEU GLU SER ILE ALA TYR GLN THR ARG ASP
SEQRES 31 Z 501 VAL LEU GLU ALA MET GLN ALA ASP SER GLY ILE ARG LEU
SEQRES 32 Z 501 HIS ALA LEU ARG VAL ASP GLY GLY ALA VAL ALA ASN ASN
SEQRES 33 Z 501 PHE LEU MET GLN PHE GLN SER ASP ILE LEU GLY THR ARG
SEQRES 34 Z 501 VAL GLU ARG PRO GLU VAL ARG GLU VAL THR ALA LEU GLY
SEQRES 35 Z 501 ALA ALA TYR LEU ALA GLY LEU ALA VAL GLY PHE TRP GLN
SEQRES 36 Z 501 ASN LEU ASP GLU LEU GLN GLU LYS ALA VAL ILE GLU ARG
SEQRES 37 Z 501 GLU PHE ARG PRO GLY ILE GLU THR THR GLU ARG ASN TYR
SEQRES 38 Z 501 ARG TYR ALA GLY TRP LYS LYS ALA VAL LYS ARG ALA MET
SEQRES 39 Z 501 ALA TRP GLU GLU HIS ASP GLU
HET EPE O 602 15
HET GOL O 601 6
HET GOL Z 603 6
HETNAM EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID
HETNAM GOL GLYCEROL
HETSYN EPE HEPES
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 EPE C8 H18 N2 O4 S
FORMUL 4 GOL 2(C3 H8 O3)
HELIX 1 1 PRO O 49 ALA O 67 1 19
HELIX 2 2 SER O 71 GLN O 73 5 3
HELIX 3 3 THR O 108 ASP O 118 5 11
HELIX 4 4 GLU O 121 THR O 128 1 8
HELIX 5 5 SER O 137 HIS O 147 1 11
HELIX 6 6 SER O 151 ARG O 156 1 6
HELIX 7 7 VAL O 165 THR O 174 1 10
HELIX 8 8 TYR O 183 ARG O 188 1 6
HELIX 9 9 ASP O 201 LEU O 207 1 7
HELIX 10 10 ARG O 211 MET O 213 5 3
HELIX 11 11 ASP O 245 GLY O 252 1 8
HELIX 12 12 GLY O 310 ASP O 318 1 9
HELIX 13 13 SER O 329 LYS O 335 1 7
HELIX 14 14 ALA O 347 THR O 349 5 3
HELIX 15 15 ALA O 373 SER O 399 1 27
HELIX 16 16 GLY O 411 ALA O 414 5 4
HELIX 17 17 ASN O 416 LEU O 426 1 11
HELIX 18 18 GLU O 437 VAL O 451 5 15
HELIX 19 19 THR O 476 ALA O 493 1 18
HELIX 20 20 PRO Z 49 LYS Z 66 1 18
HELIX 21 21 SER Z 71 GLN Z 73 5 3
HELIX 22 22 ARG Z 107 ARG Z 117 5 11
HELIX 23 23 GLU Z 121 ASN Z 127 1 7
HELIX 24 24 SER Z 137 HIS Z 147 1 11
HELIX 25 25 ARG Z 152 ARG Z 157 1 6
HELIX 26 26 VAL Z 165 MET Z 173 1 9
HELIX 27 27 TYR Z 183 ARG Z 188 1 6
HELIX 28 28 ASP Z 201 LEU Z 207 1 7
HELIX 29 29 ASP Z 245 GLY Z 252 1 8
HELIX 30 30 GLY Z 310 ASP Z 318 1 9
HELIX 31 31 SER Z 329 THR Z 334 1 6
HELIX 32 32 ALA Z 347 THR Z 349 5 3
HELIX 33 33 ALA Z 373 SER Z 399 1 27
HELIX 34 34 GLY Z 411 ALA Z 414 5 4
HELIX 35 35 ASN Z 416 LEU Z 426 1 11
HELIX 36 36 VAL Z 438 VAL Z 451 1 14
HELIX 37 37 LEU Z 457 LEU Z 460 1 4
HELIX 38 38 THR Z 476 ALA Z 493 1 18
SHEET 1 A 6 GLY O 225 THR O 227 0
SHEET 2 A 6 ILE O 237 GLY O 244 -1 N ILE O 239 O GLY O 225
SHEET 3 A 6 ILE O 74 ASN O 81 1 N ILE O 77 O SER O 240
SHEET 4 A 6 TYR O 5 GLN O 11 1 N TYR O 5 O ALA O 75
SHEET 5 A 6 SER O 15 ASP O 22 -1 N MET O 21 O ILE O 6
SHEET 6 A 6 ILE O 27 GLU O 34 -1 N ARG O 33 O SER O 16
SHEET 1 B 2 ILE O 87 GLU O 90 0
SHEET 2 B 2 LEU O 160 GLY O 163 -1 N GLY O 163 O ILE O 87
SHEET 1 C 2 VAL O 180 ASP O 182 0
SHEET 2 C 2 GLU O 216 ARG O 218 1 N GLU O 216 O THR O 181
SHEET 1 D 4 ALA O 261 TYR O 265 0
SHEET 2 D 4 CYS O 269 ASN O 274 -1 N LEU O 272 O LYS O 262
SHEET 3 D 4 VAL O 298 VAL O 306 -1 N VAL O 306 O CYS O 269
SHEET 4 D 4 LEU O 287 CYS O 292 -1 N ALA O 291 O ASN O 299
SHEET 1 E 2 TYR O 343 VAL O 345 0
SHEET 2 E 2 ALA O 363 PHE O 365 -1 N PHE O 365 O TYR O 343
SHEET 1 F 3 ALA O 405 VAL O 408 0
SHEET 2 F 3 ARG O 429 ARG O 432 1 N ARG O 429 O LEU O 406
SHEET 3 F 3 ARG O 468 PHE O 470 -1 N PHE O 470 O VAL O 430
SHEET 1 G 6 VAL Z 30 GLU Z 34 0
SHEET 2 G 6 SER Z 15 ASP Z 22 -1 N ALA Z 18 O SER Z 31
SHEET 3 G 6 TYR Z 5 GLN Z 11 -1 N ASP Z 10 O ARG Z 17
SHEET 4 G 6 ILE Z 74 ASN Z 81 1 N ALA Z 75 O TYR Z 5
SHEET 5 G 6 ARG Z 236 GLY Z 244 1 N SER Z 240 O ILE Z 77
SHEET 6 G 6 GLY Z 225 ASN Z 228 -1 N THR Z 227 O ILE Z 237
SHEET 1 H 2 THR Z 86 GLU Z 90 0
SHEET 2 H 2 LEU Z 160 THR Z 164 -1 N GLY Z 163 O ILE Z 87
SHEET 1 I 2 VAL Z 180 ASP Z 182 0
SHEET 2 I 2 GLU Z 216 ARG Z 218 1 N GLU Z 216 O THR Z 181
SHEET 1 J 4 ALA Z 261 TYR Z 265 0
SHEET 2 J 4 CYS Z 269 GLY Z 276 -1 N LEU Z 272 O LYS Z 262
SHEET 3 J 4 GLU Z 297 VAL Z 306 -1 N VAL Z 306 O CYS Z 269
SHEET 4 J 4 LEU Z 287 GLY Z 293 -1 N GLY Z 293 O GLU Z 297
SHEET 1 K 2 TYR Z 343 VAL Z 345 0
SHEET 2 K 2 ALA Z 363 PHE Z 365 -1 N PHE Z 365 O TYR Z 343
SHEET 1 L 3 ALA Z 405 VAL Z 408 0
SHEET 2 L 3 ARG Z 429 PRO Z 433 1 N ARG Z 429 O LEU Z 406
SHEET 3 L 3 ILE Z 466 PHE Z 470 -1 N PHE Z 470 O VAL Z 430
CISPEP 1 ALA O 353 PRO O 354 0 3.50
CISPEP 2 ALA Z 353 PRO Z 354 0 -0.20
SITE 1 AC1 9 HIS O 179 ASP O 198 TRP O 199 ARG O 211
SITE 2 AC1 9 GLU O 212 LEU O 214 PRO O 215 GLU O 216
SITE 3 AC1 9 VAL O 217
SITE 1 AC2 7 ARG O 83 GLU O 84 TRP O 103 TYR O 135
SITE 2 AC2 7 ASP O 245 GLN O 246 PHE O 270
SITE 1 AC3 7 ARG Z 83 GLU Z 84 TRP Z 103 TYR Z 135
SITE 2 AC3 7 ASP Z 245 GLN Z 246 PHE Z 270
CRYST1 168.800 168.800 202.700 90.00 90.00 90.00 P 41 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 0.005924 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005924 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004933 0.00000
MTRIX1 1 -0.689940 -0.311658 -0.653338 155.99388 1
MTRIX2 1 -0.325823 -0.672259 0.664761 22.12158 1
MTRIX3 1 -0.646391 0.671518 0.362273 63.89221 1
(ATOM LINES ARE NOT SHOWN.)
END
