HEADER GLYCOGEN PHOSPHORYLASE 13-NOV-90 8GPB
TITLE STRUCTURAL MECHANISM FOR GLYCOGEN PHOSPHORYLASE CONTROL BY
TITLE 2 PHOSPHORYLATION AND AMP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLYCOGEN PHOSPHORYLASE B;
COMPND 3 CHAIN: A;
COMPND 4 EC: 2.4.1.1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ORYCTOLAGUS CUNICULUS;
SOURCE 3 ORGANISM_COMMON: RABBIT;
SOURCE 4 ORGANISM_TAXID: 9986
KEYWDS GLYCOGEN PHOSPHORYLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.BARFORD,S.-H.HU,L.N.JOHNSON
REVDAT 5 29-NOV-17 8GPB 1 HELIX
REVDAT 4 13-JUL-11 8GPB 1 VERSN
REVDAT 3 24-FEB-09 8GPB 1 VERSN
REVDAT 2 01-APR-03 8GPB 1 JRNL
REVDAT 1 15-OCT-92 8GPB 0
JRNL AUTH D.BARFORD,S.H.HU,L.N.JOHNSON
JRNL TITL STRUCTURAL MECHANISM FOR GLYCOGEN PHOSPHORYLASE CONTROL BY
JRNL TITL 2 PHOSPHORYLATION AND AMP.
JRNL REF J.MOL.BIOL. V. 218 233 1991
JRNL REFN ISSN 0022-2836
JRNL PMID 1900534
JRNL DOI 10.1016/0022-2836(91)90887-C
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH K.R.ACHARYA,D.I.STUART,K.M.VARVILL,L.N.JOHNSON
REMARK 1 TITL GLYCOGEN PHOSPHORYLASE B: DESCRIPTION OF THE PROTEIN
REMARK 1 TITL 2 STRUCTURE 1 1991
REMARK 1 REF GLYCOGEN PHOSPHORYLASE B:
REMARK 1 REF 2 DESCRIPTION OF THE PROTEIN
REMARK 1 REF 3 STRUCTURE
REMARK 1 PUBL WORLD SCIENTIFIC PUBLISHING CO.,SINGAPORE
REMARK 1 REFN
REMARK 1 REFERENCE 2
REMARK 1 AUTH L.N.JOHNSON,K.R.ACHARYA,M.D.JORDAN,P.J.MCLAUGHLIN
REMARK 1 TITL REFINED CRYSTAL STRUCTURE OF THE PHOSPHORYLASE-HEPTULOSE
REMARK 1 TITL 2 2-PHOSPHATE-OLIGOSACCHARIDE-AMP COMPLEX
REMARK 1 REF J.MOL.BIOL. V. 211 645 1990
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 3
REMARK 1 AUTH J.L.MARTIN,L.N.JOHNSON,S.G.WITHERS
REMARK 1 TITL COMPARISON OF THE BINDING OF GLUCOSE AND GLUCOSE-1-PHOSPHATE
REMARK 1 TITL 2 DERIVATIVES TO T-STATE GLYCOGEN PHOSPHORYLASE B
REMARK 1 REF BIOCHEMISTRY V. 29 10745 1990
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 4
REMARK 1 AUTH D.BARFORD,L.N.JOHNSON
REMARK 1 TITL THE ALLOSTERIC TRANSITION OF GLYCOGEN PHOSPHORYLASE
REMARK 1 REF NATURE V. 340 609 1989
REMARK 1 REFN ISSN 0028-0836
REMARK 1 REFERENCE 5
REMARK 1 AUTH S.R.SPRANG,K.R.ACHARYA,E.J.GOLDSMITH,D.I.STUART,K.VARVILL,
REMARK 1 AUTH 2 R.J.FLETTERICK,N.B.MADSEN,L.N.JOHNSON
REMARK 1 TITL STRUCTURAL CHANGES IN GLYCOGEN PHOSPHORYLASE INDUCED BY
REMARK 1 TITL 2 PHOSPHORYLATION
REMARK 1 REF NATURE V. 336 215 1988
REMARK 1 REFN ISSN 0028-0836
REMARK 2
REMARK 2 RESOLUTION. 2.20 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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : NULL
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
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 : NULL
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) : 0.206
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 : 6761
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 61
REMARK 3 SOLVENT ATOMS : 640
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) : 0.018
REMARK 3 BOND ANGLES (DEGREES) : 3.600
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 8GPB 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_1000179975.
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: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.13
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.47
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 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+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
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 58.15000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 64.25000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 64.25000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 87.22500
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 64.25000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 64.25000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 29.07500
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 64.25000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 64.25000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 87.22500
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 64.25000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 64.25000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 29.07500
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 58.15000
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,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 7880 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 59960 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 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 116.30000
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 SER A 1
REMARK 465 ARG A 2
REMARK 465 PRO A 3
REMARK 465 LEU A 4
REMARK 465 SER A 5
REMARK 465 ASP A 6
REMARK 465 GLN A 7
REMARK 465 GLU A 8
REMARK 465 LYS A 9
REMARK 465 ARG A 10
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 840 CG CD CE NZ
REMARK 470 ILE A 841 CG1 CG2 CD1
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 34 NE2 HIS A 34 CD2 -0.071
REMARK 500 HIS A 36 NE2 HIS A 36 CD2 -0.069
REMARK 500 HIS A 57 NE2 HIS A 57 CD2 -0.077
REMARK 500 HIS A 62 NE2 HIS A 62 CD2 -0.071
REMARK 500 HIS A 73 NE2 HIS A 73 CD2 -0.066
REMARK 500 HIS A 208 NE2 HIS A 208 CD2 -0.079
REMARK 500 HIS A 377 NE2 HIS A 377 CD2 -0.067
REMARK 500 HIS A 390 NE2 HIS A 390 CD2 -0.066
REMARK 500 HIS A 399 NE2 HIS A 399 CD2 -0.078
REMARK 500 HIS A 443 NE2 HIS A 443 CD2 -0.080
REMARK 500 HIS A 450 NE2 HIS A 450 CD2 -0.074
REMARK 500 HIS A 459 NE2 HIS A 459 CD2 -0.081
REMARK 500 HIS A 556 NE2 HIS A 556 CD2 -0.068
REMARK 500 HIS A 571 NE2 HIS A 571 CD2 -0.086
REMARK 500 HIS A 632 NE2 HIS A 632 CD2 -0.075
REMARK 500 HIS A 767 NE2 HIS A 767 CD2 -0.068
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 VAL A 15 CA - CB - CG1 ANGL. DEV. = -12.4 DEGREES
REMARK 500 VAL A 15 CA - C - O ANGL. DEV. = 14.9 DEGREES
REMARK 500 VAL A 15 CA - C - N ANGL. DEV. = -20.8 DEGREES
REMARK 500 ARG A 16 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 ARG A 43 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ARG A 60 NE - CZ - NH2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 TRP A 67 CD1 - CG - CD2 ANGL. DEV. = 6.4 DEGREES
REMARK 500 TRP A 67 CE2 - CD2 - CG ANGL. DEV. = -5.8 DEGREES
REMARK 500 TYR A 90 CB - CG - CD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 ARG A 93 NE - CZ - NH1 ANGL. DEV. = 5.2 DEGREES
REMARK 500 MET A 99 CG - SD - CE ANGL. DEV. = -17.3 DEGREES
REMARK 500 CYS A 108 CA - CB - SG ANGL. DEV. = 7.2 DEGREES
REMARK 500 TYR A 113 CB - CG - CD1 ANGL. DEV. = -3.6 DEGREES
REMARK 500 LEU A 117 N - CA - C ANGL. DEV. = 20.9 DEGREES
REMARK 500 MET A 119 CG - SD - CE ANGL. DEV. = -13.3 DEGREES
REMARK 500 ARG A 138 NE - CZ - NH1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ARG A 138 NE - CZ - NH2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 TYR A 155 CB - CG - CD1 ANGL. DEV. = -4.2 DEGREES
REMARK 500 TYR A 161 CB - CG - CD2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 TRP A 174 CD1 - CG - CD2 ANGL. DEV. = 5.2 DEGREES
REMARK 500 TRP A 174 CE2 - CD2 - CG ANGL. DEV. = -5.6 DEGREES
REMARK 500 ASP A 181 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 TRP A 182 CD1 - CG - CD2 ANGL. DEV. = 5.0 DEGREES
REMARK 500 TRP A 189 CD1 - CG - CD2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 TRP A 189 CE2 - CD2 - CG ANGL. DEV. = -5.6 DEGREES
REMARK 500 LEU A 198 CA - CB - CG ANGL. DEV. = 17.1 DEGREES
REMARK 500 TYR A 203 CB - CG - CD2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 ARG A 205 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ARG A 205 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 LYS A 214 N - CA - CB ANGL. DEV. = -12.6 DEGREES
REMARK 500 LYS A 214 CA - CB - CG ANGL. DEV. = 13.8 DEGREES
REMARK 500 TRP A 215 CD1 - CG - CD2 ANGL. DEV. = 5.2 DEGREES
REMARK 500 TRP A 215 CE2 - CD2 - CG ANGL. DEV. = -5.5 DEGREES
REMARK 500 TRP A 215 CG - CD2 - CE3 ANGL. DEV. = 6.6 DEGREES
REMARK 500 VAL A 220 CG1 - CB - CG2 ANGL. DEV. = -9.9 DEGREES
REMARK 500 ARG A 242 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ARG A 242 NE - CZ - NH2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 TRP A 244 CD1 - CG - CD2 ANGL. DEV. = 7.1 DEGREES
REMARK 500 TRP A 244 CB - CG - CD1 ANGL. DEV. = -8.2 DEGREES
REMARK 500 TRP A 244 CE2 - CD2 - CG ANGL. DEV. = -6.0 DEGREES
REMARK 500 TRP A 244 CG - CD2 - CE3 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ILE A 263 CG1 - CB - CG2 ANGL. DEV. = -16.6 DEGREES
REMARK 500 TYR A 280 CB - CG - CD2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 ARG A 292 CA - CB - CG ANGL. DEV. = -14.3 DEGREES
REMARK 500 ARG A 309 NE - CZ - NH1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ARG A 309 NE - CZ - NH2 ANGL. DEV. = -9.1 DEGREES
REMARK 500 ARG A 319 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG A 319 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 THR A 340 N - CA - CB ANGL. DEV. = -13.9 DEGREES
REMARK 500 ARG A 351 NE - CZ - NH2 ANGL. DEV. = -4.4 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 102 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 GLN A 12 -99.06 50.97
REMARK 500 ILE A 13 39.38 27.47
REMARK 500 SER A 14 -161.56 -74.40
REMARK 500 HIS A 36 -75.13 -80.48
REMARK 500 VAL A 45 -8.47 -145.94
REMARK 500 ASP A 78 67.67 31.17
REMARK 500 ASP A 118 98.24 66.54
REMARK 500 LEU A 131 29.63 -78.61
REMARK 500 ASP A 181 56.81 -90.86
REMARK 500 TYR A 203 -125.55 61.61
REMARK 500 SER A 210 -101.48 63.84
REMARK 500 ASP A 217 53.83 38.70
REMARK 500 ASN A 236 15.57 58.31
REMARK 500 ASP A 251 -94.81 -83.70
REMARK 500 ASP A 256 -173.46 78.83
REMARK 500 VAL A 259 36.80 -88.22
REMARK 500 PRO A 281 24.49 -70.95
REMARK 500 SER A 313 47.56 -107.29
REMARK 500 LYS A 315 -5.06 53.99
REMARK 500 ASP A 320 -72.48 -90.44
REMARK 500 PRO A 321 41.21 -65.00
REMARK 500 VAL A 322 -41.51 -162.09
REMARK 500 ARG A 323 169.29 176.62
REMARK 500 ALA A 328 -21.32 -170.63
REMARK 500 ASP A 339 -161.40 70.17
REMARK 500 VAL A 436 88.74 122.26
REMARK 500 THR A 466 -79.76 -134.51
REMARK 500 LEU A 492 -77.65 -135.21
REMARK 500 ASP A 514 67.37 -153.72
REMARK 500 ASP A 527 122.17 -174.13
REMARK 500 ARG A 551 -76.85 -68.76
REMARK 500 TYR A 553 20.40 -144.53
REMARK 500 LYS A 554 106.47 42.00
REMARK 500 VAL A 555 -48.37 -138.29
REMARK 500 HIS A 556 74.93 32.70
REMARK 500 GLU A 593 73.16 -119.94
REMARK 500 SER A 674 -66.41 -141.92
REMARK 500 ASN A 678 -79.04 -3.80
REMARK 500 HIS A 768 59.32 -150.32
REMARK 500 ASN A 793 78.80 -103.55
REMARK 500 ILE A 824 -52.17 -126.15
REMARK 500 ALA A 836 81.79 -15.47
REMARK 500 PRO A 837 -118.70 -87.33
REMARK 500 ASP A 838 -125.24 -166.56
REMARK 500 GLU A 839 -162.92 -112.52
REMARK 500 LYS A 840 135.47 154.65
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ASP A 320 PRO A 321 -100.76
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 PLP A 999
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AMP A 930
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AMP A 940
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 RESIDUE 380 IS LEU IN THE SEQUENCE (K.NAKANO,P.K.HWANG,
REMARK 999 R.J.FLETTERICK, FEBS LETT., V. 204, P. 283, 1986) BUT IT
REMARK 999 HAS BEEN PRESENTED AS ILE IN THIS ENTRY. THIS ASSIGNMENT
REMARK 999 WAS MADE IN THE ORIGINAL STRUCTURE DETERMINATION AT 1.9
REMARK 999 ANGSTROMS (PRESENTED IN PROTEIN DATA BANK ENTRY 1GPB) AND
REMARK 999 CARRIED THROUGH TO THE OTHER ENTRIES. ILE IS MORE
REMARK 999 CONSISTENT WITH THE ELECTRON DENSITY. HOWEVER, THE
REMARK 999 RESOLUTION AT 1.9 ANGSTROMS DOES NOT ALLOW A DEFINITIVE
REMARK 999 ASSIGNMENT.
DBREF 8GPB A 1 842 UNP P00489 PHS2_RABIT 1 842
SEQADV 8GPB ILE A 380 UNP P00489 LEU 380 CONFLICT
SEQRES 1 A 842 SER ARG PRO LEU SER ASP GLN GLU LYS ARG LYS GLN ILE
SEQRES 2 A 842 SER VAL ARG GLY LEU ALA GLY VAL GLU ASN VAL THR GLU
SEQRES 3 A 842 LEU LYS LYS ASN PHE ASN ARG HIS LEU HIS PHE THR LEU
SEQRES 4 A 842 VAL LYS ASP ARG ASN VAL ALA THR PRO ARG ASP TYR TYR
SEQRES 5 A 842 PHE ALA LEU ALA HIS THR VAL ARG ASP HIS LEU VAL GLY
SEQRES 6 A 842 ARG TRP ILE ARG THR GLN GLN HIS TYR TYR GLU LYS ASP
SEQRES 7 A 842 PRO LYS ARG ILE TYR TYR LEU SER LEU GLU PHE TYR MET
SEQRES 8 A 842 GLY ARG THR LEU GLN ASN THR MET VAL ASN LEU ALA LEU
SEQRES 9 A 842 GLU ASN ALA CYS ASP GLU ALA THR TYR GLN LEU GLY LEU
SEQRES 10 A 842 ASP MET GLU GLU LEU GLU GLU ILE GLU GLU ASP ALA GLY
SEQRES 11 A 842 LEU GLY ASN GLY GLY LEU GLY ARG LEU ALA ALA CYS PHE
SEQRES 12 A 842 LEU ASP SER MET ALA THR LEU GLY LEU ALA ALA TYR GLY
SEQRES 13 A 842 TYR GLY ILE ARG TYR GLU PHE GLY ILE PHE ASN GLN LYS
SEQRES 14 A 842 ILE CYS GLY GLY TRP GLN MET GLU GLU ALA ASP ASP TRP
SEQRES 15 A 842 LEU ARG TYR GLY ASN PRO TRP GLU LYS ALA ARG PRO GLU
SEQRES 16 A 842 PHE THR LEU PRO VAL HIS PHE TYR GLY ARG VAL GLU HIS
SEQRES 17 A 842 THR SER GLN GLY ALA LYS TRP VAL ASP THR GLN VAL VAL
SEQRES 18 A 842 LEU ALA MET PRO TYR ASP THR PRO VAL PRO GLY TYR ARG
SEQRES 19 A 842 ASN ASN VAL VAL ASN THR MET ARG LEU TRP SER ALA LYS
SEQRES 20 A 842 ALA PRO ASN ASP PHE ASN LEU LYS ASP PHE ASN VAL GLY
SEQRES 21 A 842 GLY TYR ILE GLN ALA VAL LEU ASP ARG ASN LEU ALA GLU
SEQRES 22 A 842 ASN ILE SER ARG VAL LEU TYR PRO ASN ASP ASN PHE PHE
SEQRES 23 A 842 GLU GLY LYS GLU LEU ARG LEU LYS GLN GLU TYR PHE VAL
SEQRES 24 A 842 VAL ALA ALA THR LEU GLN ASP ILE ILE ARG ARG PHE LYS
SEQRES 25 A 842 SER SER LYS PHE GLY CYS ARG ASP PRO VAL ARG THR ASN
SEQRES 26 A 842 PHE ASP ALA PHE PRO ASP LYS VAL ALA ILE GLN LEU ASN
SEQRES 27 A 842 ASP THR HIS PRO SER LEU ALA ILE PRO GLU LEU MET ARG
SEQRES 28 A 842 VAL LEU VAL ASP LEU GLU ARG LEU ASP TRP ASP LYS ALA
SEQRES 29 A 842 TRP GLU VAL THR VAL LYS THR CYS ALA TYR THR ASN HIS
SEQRES 30 A 842 THR VAL ILE PRO GLU ALA LEU GLU ARG TRP PRO VAL HIS
SEQRES 31 A 842 LEU LEU GLU THR LEU LEU PRO ARG HIS LEU GLN ILE ILE
SEQRES 32 A 842 TYR GLU ILE ASN GLN ARG PHE LEU ASN ARG VAL ALA ALA
SEQRES 33 A 842 ALA PHE PRO GLY ASP VAL ASP ARG LEU ARG ARG MET SER
SEQRES 34 A 842 LEU VAL GLU GLU GLY ALA VAL LYS ARG ILE ASN MET ALA
SEQRES 35 A 842 HIS LEU CYS ILE ALA GLY SER HIS ALA VAL ASN GLY VAL
SEQRES 36 A 842 ALA ARG ILE HIS SER GLU ILE LEU LYS LYS THR ILE PHE
SEQRES 37 A 842 LYS ASP PHE TYR GLU LEU GLU PRO HIS LYS PHE GLN ASN
SEQRES 38 A 842 LYS THR ASN GLY ILE THR PRO ARG ARG TRP LEU VAL LEU
SEQRES 39 A 842 CYS ASN PRO GLY LEU ALA GLU ILE ILE ALA GLU ARG ILE
SEQRES 40 A 842 GLY GLU GLU TYR ILE SER ASP LEU ASP GLN LEU ARG LYS
SEQRES 41 A 842 LEU LEU SER TYR VAL ASP ASP GLU ALA PHE ILE ARG ASP
SEQRES 42 A 842 VAL ALA LYS VAL LYS GLN GLU ASN LYS LEU LYS PHE ALA
SEQRES 43 A 842 ALA TYR LEU GLU ARG GLU TYR LYS VAL HIS ILE ASN PRO
SEQRES 44 A 842 ASN SER LEU PHE ASP VAL GLN VAL LYS ARG ILE HIS GLU
SEQRES 45 A 842 TYR LYS ARG GLN LEU LEU ASN CYS LEU HIS VAL ILE THR
SEQRES 46 A 842 LEU TYR ASN ARG ILE LYS LYS GLU PRO ASN LYS PHE VAL
SEQRES 47 A 842 VAL PRO ARG THR VAL MET ILE GLY GLY LYS ALA ALA PRO
SEQRES 48 A 842 GLY TYR HIS MET ALA LYS MET ILE ILE LYS LEU ILE THR
SEQRES 49 A 842 ALA ILE GLY ASP VAL VAL ASN HIS ASP PRO VAL VAL GLY
SEQRES 50 A 842 ASP ARG LEU ARG VAL ILE PHE LEU GLU ASN TYR ARG VAL
SEQRES 51 A 842 SER LEU ALA GLU LYS VAL ILE PRO ALA ALA ASP LEU SER
SEQRES 52 A 842 GLU GLN ILE SER THR ALA GLY THR GLU ALA SER GLY THR
SEQRES 53 A 842 GLY ASN MET LYS PHE MET LEU ASN GLY ALA LEU THR ILE
SEQRES 54 A 842 GLY THR MET ASP GLY ALA ASN VAL GLU MET ALA GLU GLU
SEQRES 55 A 842 ALA GLY GLU GLU ASN PHE PHE ILE PHE GLY MET ARG VAL
SEQRES 56 A 842 GLU ASP VAL ASP ARG LEU ASP GLN ARG GLY TYR ASN ALA
SEQRES 57 A 842 GLN GLU TYR TYR ASP ARG ILE PRO GLU LEU ARG GLN ILE
SEQRES 58 A 842 ILE GLU GLN LEU SER SER GLY PHE PHE SER PRO LYS GLN
SEQRES 59 A 842 PRO ASP LEU PHE LYS ASP ILE VAL ASN MET LEU MET HIS
SEQRES 60 A 842 HIS ASP ARG PHE LYS VAL PHE ALA ASP TYR GLU GLU TYR
SEQRES 61 A 842 VAL LYS CYS GLN GLU ARG VAL SER ALA LEU TYR LYS ASN
SEQRES 62 A 842 PRO ARG GLU TRP THR ARG MET VAL ILE ARG ASN ILE ALA
SEQRES 63 A 842 THR SER GLY LYS PHE SER SER ASP ARG THR ILE ALA GLN
SEQRES 64 A 842 TYR ALA ARG GLU ILE TRP GLY VAL GLU PRO SER ARG GLN
SEQRES 65 A 842 ARG LEU PRO ALA PRO ASP GLU LYS ILE PRO
HET PLP A 999 15
HET AMP A 930 23
HET AMP A 940 23
HETNAM PLP PYRIDOXAL-5'-PHOSPHATE
HETNAM AMP ADENOSINE MONOPHOSPHATE
HETSYN PLP VITAMIN B6 PHOSPHATE
FORMUL 2 PLP C8 H10 N O6 P
FORMUL 3 AMP 2(C10 H14 N5 O7 P)
FORMUL 5 HOH *640(H2 O)
HELIX 1 H1 GLY A 20 THR A 38 1 19
HELIX 2 H2 THR A 47 ASP A 78 1 32
HELIX 3 H3 THR A 94 LEU A 102 1 9
HELIX 4 H4 LEU A 104 LEU A 115 1 12
HELIX 5 H5 ASP A 118 GLU A 124 1 7
HELIX 6 H6 GLY A 134 LEU A 150 1 17
HELIX 7 H7 GLY A 261 ASN A 274 1 14
HELIX 8 H8 LYS A 289 SER A 314 1 26
HELIX 9 H8B ALA A 328 VAL A 333 1 6
HELIX 10 H9 LEU A 344 ASP A 355 1 12
HELIX 11 H10 ASP A 360 CYS A 372 1 13
HELIX 12 H11 PRO A 388 LEU A 396 1 9
HELIX 13 H12 LEU A 396 PHE A 418 1 23
HELIX 14 H13 GLY A 420 SER A 429 1 10
HELIX 15 H14 ASN A 440 GLY A 448 1 9
HELIX 16 H15 ALA A 456 THR A 466 1 11
HELIX 17 15B PHE A 468 GLU A 475 1 8
HELIX 18 PI PRO A 488 CYS A 495 3 8
HELIX 19 H16 ASN A 496 GLY A 508 1 13
HELIX 20 3TA GLU A 509 ASP A 514 5 6
HELIX 21 3TB ASP A 514 VAL A 525 5 12
HELIX 22 H17 ASP A 527 TYR A 553 1 27
HELIX 23 H18 ARG A 575 GLU A 593 1 19
HELIX 24 H19 TYR A 613 ASN A 631 1 19
HELIX 25 H20 ARG A 649 ILE A 657 1 9
HELIX 26 H21 THR A 676 ASN A 684 1 9
HELIX 27 H22 ALA A 695 GLY A 704 1 10
HELIX 28 H23 ARG A 714 GLY A 725 1 12
HELIX 29 H24 ALA A 728 ILE A 735 1 8
HELIX 30 H25 ILE A 735 SER A 747 1 13
HELIX 31 H26 PHE A 758 HIS A 768 1 11
HELIX 32 H27 ASP A 776 LYS A 792 1 17
HELIX 33 H28 ASN A 793 ALA A 806 1 14
HELIX 34 H29 SER A 812 TRP A 825 1 14
SHEET 1 S1 9 LYS A 191 ARG A 193 0
SHEET 2 S1 9 LEU A 222 GLY A 232 -1 N ASP A 227 O LYS A 191
SHEET 3 S1 9 VAL A 237 LYS A 247 -1 N MET A 241 O THR A 228
SHEET 4 S1 9 ALA A 153 ARG A 160 1 N GLY A 158 O ARG A 242
SHEET 5 S1 9 ARG A 81 SER A 86 1 N TYR A 84 O TYR A 155
SHEET 6 S1 9 LYS A 332 ASP A 339 1 N GLN A 336 O TYR A 83
SHEET 7 S1 9 THR A 371 ASN A 376 1 N ALA A 373 O ILE A 335
SHEET 8 S1 9 ALA A 451 GLY A 454 1 N ASN A 453 O TYR A 374
SHEET 9 S1 9 LYS A 478 ASN A 484 1 N GLN A 480 O VAL A 452
SHEET 1 S2 2 ASN A 167 CYS A 171 0
SHEET 2 S2 2 TRP A 174 GLU A 178 -1 N MET A 176 O LYS A 169
SHEET 1 S3 2 GLU A 162 PHE A 163 0
SHEET 2 S3 2 SER A 276 LEU A 279 1 O SER A 276 N GLU A 162
SHEET 1 S4 2 LEU A 198 THR A 209 0
SHEET 2 S4 2 GLY A 212 ALA A 223 -1 N VAL A 216 O ARG A 205
SHEET 1 S5 2 PHE A 89 GLY A 92 0
SHEET 2 S5 2 ALA A 129 LEU A 131 -1 O LEU A 131 N PHE A 89
SHEET 1 S6 3 GLU A 385 VAL A 389 0
SHEET 2 S6 3 LYS A 437 MET A 441 -1 N ILE A 439 O TRP A 387
SHEET 3 S6 3 LEU A 430 GLU A 432 -1 N GLU A 432 O ARG A 438
SHEET 1 S7 6 ARG A 639 LEU A 645 0
SHEET 2 S7 6 PRO A 600 LYS A 608 1 N ILE A 605 O ILE A 643
SHEET 3 S7 6 LEU A 562 ILE A 570 1 N LYS A 568 O GLY A 606
SHEET 4 S7 6 ASP A 661 GLN A 665 1 N LEU A 662 O PHE A 563
SHEET 5 S7 6 LEU A 687 THR A 691 1 N LEU A 687 O ASP A 661
SHEET 6 S7 6 PHE A 709 PHE A 711 1 N PHE A 709 O THR A 688
LINK NZ LYS A 680 C4A PLP A 999 1555 1555 1.35
SITE 1 AC1 12 LYS A 568 TYR A 648 ARG A 649 VAL A 650
SITE 2 AC1 12 GLY A 675 THR A 676 GLY A 677 LYS A 680
SITE 3 AC1 12 HOH A1319 HOH A1474 HOH A1475 HOH A1486
SITE 1 AC2 6 ASN A 44 GLN A 72 TYR A 75 ARG A 309
SITE 2 AC2 6 ARG A 310 HOH A1532
SITE 1 AC3 7 ASN A 282 PHE A 285 PRO A 611 GLY A 612
SITE 2 AC3 7 TYR A 613 HOH A1479 HOH A1624
CRYST1 128.500 128.500 116.300 90.00 90.00 90.00 P 43 21 2 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 0.007782 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007782 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008598 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
