HEADER TRANSFERASE 30-JUL-00 1GG8
TITLE DESIGN OF INHIBITORS OF GLYCOGEN PHOSPHORYLASE: A STUDY OF ALPHA-AND
TITLE 2 BETA-C-GLUCOSIDES AND 1-THIO-BETA-D-GLUCOSE COMPOUNDS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (GLYCOGEN PHOSPHORYLASE);
COMPND 3 CHAIN: A;
COMPND 4 EC: 2.4.1.1
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ORYCTOLAGUS CUNICULUS;
SOURCE 3 ORGANISM_COMMON: RABBIT;
SOURCE 4 ORGANISM_TAXID: 9986;
SOURCE 5 TISSUE: MUSCLE
KEYWDS GLYCOGEN PHOSPHORYLASE, INHIBITOR COMPLEX, CATALYTIC SITE, DESIGN,
KEYWDS 2 TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.A.WATSON,E.P.MITCHELL,L.N.JOHNSON,J.C.SON,C.J.BICHARD,M.G.ORCHARD,
AUTHOR 2 G.W.FLEET,N.G.OIKONOMAKOS,D.D.LEONIDAS,M.KONTOU,A.C.PAPAGEORGIOU
REVDAT 7 09-AUG-23 1GG8 1 REMARK
REVDAT 6 29-JUL-20 1GG8 1 REMARK SEQADV LINK SITE
REVDAT 5 22-FEB-12 1GG8 1 JRNL
REVDAT 4 13-JUL-11 1GG8 1 VERSN
REVDAT 3 24-FEB-09 1GG8 1 VERSN
REVDAT 2 01-APR-03 1GG8 1 JRNL
REVDAT 1 23-AUG-00 1GG8 0
JRNL AUTH K.A.WATSON,E.P.MITCHELL,L.N.JOHNSON,J.C.SON,C.J.BICHARD,
JRNL AUTH 2 M.G.ORCHARD,G.W.FLEET,N.G.OIKONOMAKOS,D.D.LEONIDAS,M.KONTOU,
JRNL AUTH 3 A.PAPAGEORGIOUI
JRNL TITL DESIGN OF INHIBITORS OF GLYCOGEN PHOSPHORYLASE: A STUDY OF
JRNL TITL 2 ALPHA- AND BETA-C-GLUCOSIDES AND 1-THIO-BETA-D-GLUCOSE
JRNL TITL 3 COMPOUNDS.
JRNL REF BIOCHEMISTRY V. 33 5745 1994
JRNL REFN ISSN 0006-2960
JRNL PMID 8180201
JRNL DOI 10.1021/BI00185A011
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH N.G.OIKONOMAKOS,M.KONTOU,S.E.ZOGRAPHOS,K.A.WATSON,
REMARK 1 AUTH 2 L.N.JOHNSON,C.J.BICHARD,G.W.FLEET,K.R.ACHARYA
REMARK 1 TITL N-ACETYL-BETA-D-GLUCOPYRANOSYLAMINE: A POTENT T-STATE
REMARK 1 TITL 2 INHIBITOR OF GLYCOGEN PHOSPHORYLASE. A COMPARISON WITH
REMARK 1 TITL 3 ALPHA-D-GLUCOSE
REMARK 1 REF PROTEIN SCI. V. 4 2469 1995
REMARK 1 REFN ISSN 0961-8368
REMARK 2
REMARK 2 RESOLUTION. 2.31 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.31
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 18.50
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) (%) : 79.6
REMARK 3 NUMBER OF REFLECTIONS : 34395
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 SET) : 0.202
REMARK 3 FREE R VALUE : 0.253
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 : 6749
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 52
REMARK 3 SOLVENT ATOMS : 248
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) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 25.40
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.700
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 1GG8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-AUG-00.
REMARK 100 THE DEPOSITION ID IS D_1000001487.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-AUG-93
REMARK 200 TEMPERATURE (KELVIN) : 298.0
REMARK 200 PH : 6.70
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 RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NI FILTER
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : NICOLET
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34397
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.310
REMARK 200 RESOLUTION RANGE LOW (A) : 18.500
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 79.6
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.09200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.31
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.42
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: OTHER
REMARK 200 SOFTWARE USED: CCP4
REMARK 200 STARTING MODEL: 2PRJ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.47
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: T-STATE GPB CRYSTALS (OIKONOMAKOS ET
REMARK 280 AL., 1985, BBA 832, 248) WERE SOAKED FOR 1 H IN A BUFFERED
REMARK 280 SOLUTION [10 MM BES, 0.1 MM EDTA, PH 6.7] CONTAINING A 100 MM
REMARK 280 CONCENTRATION OF THE COMPOUND. , PH 6.70
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: 8390 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 58770 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 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 465 LYS A 11
REMARK 465 GLN A 12
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 554 N - CA - C ANGL. DEV. = 20.3 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 SER A 14 177.42 152.53
REMARK 500 VAL A 15 54.35 -95.09
REMARK 500 ALA A 19 66.55 -106.51
REMARK 500 ARG A 43 -30.09 -39.33
REMARK 500 LEU A 131 45.37 -86.17
REMARK 500 TYR A 203 -138.47 59.91
REMARK 500 SER A 210 -79.73 27.60
REMARK 500 GLN A 211 59.06 -106.10
REMARK 500 ASP A 251 -99.58 -84.21
REMARK 500 LEU A 254 -43.41 161.98
REMARK 500 ASN A 258 64.34 96.86
REMARK 500 VAL A 259 140.56 65.03
REMARK 500 LEU A 271 -33.68 -156.02
REMARK 500 PRO A 281 31.59 -77.18
REMARK 500 SER A 314 -121.44 28.60
REMARK 500 CYS A 318 -58.53 -156.20
REMARK 500 ARG A 319 -104.50 -158.84
REMARK 500 ASP A 320 -148.50 68.58
REMARK 500 VAL A 322 102.65 69.74
REMARK 500 ARG A 323 113.29 138.71
REMARK 500 THR A 324 81.26 -51.51
REMARK 500 ASP A 339 -166.71 78.69
REMARK 500 ALA A 435 -70.75 -32.14
REMARK 500 THR A 466 -97.01 -113.41
REMARK 500 ASN A 484 170.14 -59.24
REMARK 500 LEU A 492 -74.35 -147.14
REMARK 500 GLU A 510 -9.21 -59.81
REMARK 500 ASP A 514 66.26 -156.49
REMARK 500 GLN A 517 -9.24 -58.97
REMARK 500 LYS A 554 95.46 59.18
REMARK 500 VAL A 555 42.33 159.57
REMARK 500 HIS A 556 144.89 37.70
REMARK 500 ILE A 666 42.04 -104.83
REMARK 500 SER A 674 -64.79 -152.59
REMARK 500 THR A 676 -22.30 -144.70
REMARK 500 PHE A 709 79.86 -100.42
REMARK 500 LYS A 772 69.17 27.35
REMARK 500 ASN A 793 76.75 -116.71
REMARK 500 ARG A 831 36.55 -97.73
REMARK 500 PRO A 835 72.33 -47.51
REMARK 500 ALA A 836 172.79 46.55
REMARK 500 ASP A 838 112.69 -9.50
REMARK 500 GLU A 839 -94.74 4.39
REMARK 500 LYS A 840 134.91 54.70
REMARK 500 ILE A 841 85.65 -154.24
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1GG8 A 1 842 UNP P00489 PHS2_RABIT 1 842
SEQADV 1GG8 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 GLG A 998 14
HET PLP A 999 15
HET IMP A 930 23
HETNAM GLG ALPHA-D-GLUCOPYRANOSYL-2-CARBOXYLIC ACID AMIDE
HETNAM PLP PYRIDOXAL-5'-PHOSPHATE
HETNAM IMP INOSINIC ACID
HETSYN PLP VITAMIN B6 PHOSPHATE
FORMUL 2 GLG C7 H13 N O6
FORMUL 3 PLP C8 H10 N O6 P
FORMUL 4 IMP C10 H13 N4 O8 P
FORMUL 5 HOH *248(H2 O)
HELIX 1 1 GLY A 20 THR A 38 1 19
HELIX 2 2 THR A 47 ASP A 78 1 32
HELIX 3 3 THR A 94 LEU A 102 1 9
HELIX 4 4 LEU A 104 LEU A 115 1 12
HELIX 5 5 ASP A 118 GLU A 124 1 7
HELIX 6 6 GLY A 134 LEU A 150 1 17
HELIX 7 7 PRO A 194 THR A 197 5 4
HELIX 8 8 ASP A 251 ASP A 256 1 6
HELIX 9 9 GLY A 261 ASP A 268 1 8
HELIX 10 10 ALA A 272 ARG A 277 5 6
HELIX 11 11 LYS A 289 SER A 314 1 26
HELIX 12 12 ASN A 325 ASP A 327 5 3
HELIX 13 13 ALA A 328 LYS A 332 1 5
HELIX 14 14 LEU A 344 LEU A 356 1 13
HELIX 15 15 ASP A 360 THR A 371 1 12
HELIX 16 16 ILE A 380 LEU A 384 5 5
HELIX 17 17 VAL A 389 LEU A 396 1 8
HELIX 18 18 LEU A 396 PHE A 418 1 23
HELIX 19 19 ASP A 421 SER A 429 1 9
HELIX 20 20 MET A 441 GLY A 448 1 8
HELIX 21 21 ALA A 456 THR A 466 1 11
HELIX 22 22 PHE A 468 GLU A 475 1 8
HELIX 23 23 THR A 487 LEU A 492 1 6
HELIX 24 24 ASN A 496 GLY A 508 1 13
HELIX 25 25 GLU A 509 ASP A 514 5 6
HELIX 26 26 ASP A 514 VAL A 525 5 12
HELIX 27 27 ASP A 527 TYR A 553 1 27
HELIX 28 28 ARG A 575 GLU A 593 1 19
HELIX 29 29 TYR A 613 ASN A 631 1 19
HELIX 30 30 ARG A 649 ILE A 657 1 9
HELIX 31 31 PRO A 658 ALA A 660 5 3
HELIX 32 32 THR A 676 ASN A 684 1 9
HELIX 33 33 ALA A 695 GLY A 704 1 10
HELIX 34 34 GLU A 705 PHE A 708 5 4
HELIX 35 35 ARG A 714 GLY A 725 1 12
HELIX 36 36 ASN A 727 ILE A 735 1 9
HELIX 37 37 ILE A 735 SER A 747 1 13
HELIX 38 38 PHE A 758 HIS A 768 1 11
HELIX 39 39 LYS A 772 LYS A 792 1 21
HELIX 40 40 ASN A 793 ALA A 806 1 14
HELIX 41 41 THR A 807 PHE A 811 5 5
HELIX 42 42 SER A 812 ILE A 824 1 13
SHEET 1 A 9 PHE A 479 ASN A 481 0
SHEET 2 A 9 VAL A 452 GLY A 454 1 O VAL A 452 N GLN A 480
SHEET 3 A 9 CYS A 372 THR A 375 1 O TYR A 374 N ASN A 453
SHEET 4 A 9 VAL A 333 ASN A 338 1 O ILE A 335 N ALA A 373
SHEET 5 A 9 ARG A 81 LEU A 85 1 O ARG A 81 N ALA A 334
SHEET 6 A 9 ALA A 154 ILE A 159 1 N TYR A 155 O ILE A 82
SHEET 7 A 9 VAL A 238 LYS A 247 1 O THR A 240 N GLY A 156
SHEET 8 A 9 GLN A 219 PRO A 231 -1 N LEU A 222 O LYS A 247
SHEET 9 A 9 LYS A 191 ALA A 192 -1 O LYS A 191 N ASP A 227
SHEET 1 A1 9 PHE A 479 ASN A 481 0
SHEET 2 A1 9 VAL A 452 GLY A 454 1 O VAL A 452 N GLN A 480
SHEET 3 A1 9 CYS A 372 THR A 375 1 O TYR A 374 N ASN A 453
SHEET 4 A1 9 VAL A 333 ASN A 338 1 O ILE A 335 N ALA A 373
SHEET 5 A1 9 ARG A 81 LEU A 85 1 O ARG A 81 N ALA A 334
SHEET 6 A1 9 ALA A 154 ILE A 159 1 N TYR A 155 O ILE A 82
SHEET 7 A1 9 VAL A 238 LYS A 247 1 O THR A 240 N GLY A 156
SHEET 8 A1 9 GLN A 219 PRO A 231 -1 N LEU A 222 O LYS A 247
SHEET 9 A1 9 LEU A 198 PHE A 202 -1 O LEU A 198 N ALA A 223
SHEET 1 B 2 ASN A 167 CYS A 171 0
SHEET 2 B 2 TRP A 174 GLU A 178 -1 O TRP A 174 N CYS A 171
SHEET 1 C 2 ARG A 205 HIS A 208 0
SHEET 2 C 2 ALA A 213 VAL A 216 -1 O LYS A 214 N GLU A 207
SHEET 1 D 3 ARG A 386 PRO A 388 0
SHEET 2 D 3 ARG A 438 ASN A 440 -1 N ILE A 439 O TRP A 387
SHEET 3 D 3 VAL A 431 GLU A 432 -1 N GLU A 432 O ARG A 438
SHEET 1 E 6 LEU A 640 LEU A 645 0
SHEET 2 E 6 ARG A 601 GLY A 606 1 O ARG A 601 N ARG A 641
SHEET 3 E 6 LEU A 562 VAL A 567 1 O LEU A 562 N THR A 602
SHEET 4 E 6 LEU A 662 GLN A 665 1 N LEU A 662 O PHE A 563
SHEET 5 E 6 LEU A 687 GLY A 690 1 O LEU A 687 N SER A 663
SHEET 6 E 6 PHE A 709 ILE A 710 1 N PHE A 709 O THR A 688
LINK NZ LYS A 680 C4A PLP A 999 1555 1555 1.34
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
