HEADER TRANSFERASE 25-AUG-05 2ATI
TITLE GLYCOGEN PHOSPHORYLASE INHIBITORS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLYCOGEN PHOSPHORYLASE, LIVER FORM;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: LIVER GLYCOGEN PHOSPHORYLASE A;
COMPND 5 EC: 2.4.1.1;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS GLYCOGEN PHOSPHORYLASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.KLABUNDE,K.U.WENDT,D.KADEREIT,V.BRACHVOGEL,H.J.BURGER,A.W.HERLING,
AUTHOR 2 N.G.OIKONOMAKOS,D.SCHMOLL,E.SARUBBI,E.VON ROEDERN,K.SCHOENAFINGER,
AUTHOR 3 E.DEFOSSA
REVDAT 3 13-JUL-11 2ATI 1 VERSN
REVDAT 2 24-FEB-09 2ATI 1 VERSN
REVDAT 1 25-AUG-06 2ATI 0
JRNL AUTH T.KLABUNDE,K.U.WENDT,D.KADEREIT,V.BRACHVOGEL,H.J.BURGER,
JRNL AUTH 2 A.W.HERLING,N.G.OIKONOMAKOS,M.N.KOSMOPOULOU,D.SCHMOLL,
JRNL AUTH 3 E.SARUBBI,E.VON ROEDERN,E.DEFOSSA
JRNL TITL ACYL UREAS AS HUMAN LIVER GLYCOGEN PHOSPHORYLASE INHIBITORS
JRNL TITL 2 FOR THE TREATMENT OF TYPE 2 DIABETES.
JRNL REF J.MED.CHEM. V. 48 6178 2005
JRNL REFN ISSN 0022-2623
JRNL PMID 16190745
JRNL DOI 10.1021/JM049034Y
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH N.G.OIKONOMAKOS,M.N.KOSMOPOULOU,E.D.CHRYSINA,D.D.LEONIDAS,
REMARK 1 AUTH 2 I.D.KOSTAS,K.U.WENDT,T.KLABUNDE,E.DEFOSSA
REMARK 1 TITL CRYSTALLOGRAPHIC STUDIES ON ACYL UREAS, A NEW CLASS OF
REMARK 1 TITL 2 GLYCOGEN PHOSPHORYLASE INHIBITORS, AS POTENTIAL ANTIDIABETIC
REMARK 1 TITL 3 DRUGS
REMARK 1 REF PROTEIN SCI. V. 14 1760 2005
REMARK 1 REFN ISSN 0961-8368
REMARK 1 PMID 15987904
REMARK 1 DOI 10.1110/PS.051432405
REMARK 1 REFERENCE 2
REMARK 1 AUTH V.L.RATH,M.AMMIRATI,P.K.LEMOTTE,K.F.FENNELL,M.N.MANSOUR,
REMARK 1 AUTH 2 D.E.DANLEY,T.R.HYNES,G.K.SCHULTE,D.J.WASILKO,J.PANDIT
REMARK 1 TITL ACTIVATION OF HUMAN LIVER GLYCOGEN PHOSPHORYLASE BY
REMARK 1 TITL 2 ALTERATION OF THE SECONDARY STRUCTURE AND PACKING OF THE
REMARK 1 TITL 3 CATALYTIC CORE
REMARK 1 REF MOL.CELL V. 6 139 2000
REMARK 1 REFN ISSN 1097-2765
REMARK 1 PMID 10949035
REMARK 1 DOI 10.1016/S1097-2765(00)00015-0
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNX
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : NULL
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) (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 167664
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.234
REMARK 3 R VALUE (WORKING SET) : 0.232
REMARK 3 FREE R VALUE : 0.256
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 8384
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
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 ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 167664
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 : 12842
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 100
REMARK 3 SOLVENT ATOMS : 759
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) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
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 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2ATI COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 30-AUG-05.
REMARK 100 THE RCSB ID CODE IS RCSB034292.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
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 : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 167664
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 500.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
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) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
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: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.63
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.84
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 41.06667
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 82.13333
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
REMARK 350 TOTAL BURIED SURFACE AREA: 8070 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 57060 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 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 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 ALA A 1
REMARK 465 LYS A 2
REMARK 465 PRO A 3
REMARK 465 LEU A 4
REMARK 465 THR 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 ARG A 11
REMARK 465 GLN A 12
REMARK 465 ILE A 13
REMARK 465 SER A 14
REMARK 465 ILE A 15
REMARK 465 ARG A 16
REMARK 465 GLY A 17
REMARK 465 ILE A 18
REMARK 465 VAL A 19
REMARK 465 GLY A 20
REMARK 465 VAL A 21
REMARK 465 GLU A 22
REMARK 465 ASN A 250
REMARK 465 ASP A 251
REMARK 465 PHE A 252
REMARK 465 ASN A 253
REMARK 465 LEU A 254
REMARK 465 ARG A 255
REMARK 465 ASP A 256
REMARK 465 PHE A 257
REMARK 465 ASN A 258
REMARK 465 VAL A 259
REMARK 465 GLY A 260
REMARK 465 GLY A 317
REMARK 465 SER A 318
REMARK 465 THR A 319
REMARK 465 ARG A 320
REMARK 465 GLY A 321
REMARK 465 ALA A 322
REMARK 465 GLY A 323
REMARK 465 LEU A 832
REMARK 465 LYS A 833
REMARK 465 ILE A 834
REMARK 465 SER A 835
REMARK 465 LEU A 836
REMARK 465 SER A 837
REMARK 465 ASN A 838
REMARK 465 GLU A 839
REMARK 465 SER A 840
REMARK 465 ASN A 841
REMARK 465 LYS A 842
REMARK 465 VAL A 843
REMARK 465 ASN A 844
REMARK 465 GLY A 845
REMARK 465 ASN A 846
REMARK 465 ALA B 1
REMARK 465 LYS B 2
REMARK 465 PRO B 3
REMARK 465 LEU B 4
REMARK 465 THR B 5
REMARK 465 ASP B 6
REMARK 465 GLN B 7
REMARK 465 GLU B 8
REMARK 465 LYS B 9
REMARK 465 ARG B 10
REMARK 465 ARG B 11
REMARK 465 GLN B 12
REMARK 465 ILE B 13
REMARK 465 SER B 14
REMARK 465 ILE B 15
REMARK 465 ARG B 16
REMARK 465 GLY B 17
REMARK 465 ILE B 18
REMARK 465 VAL B 19
REMARK 465 GLY B 20
REMARK 465 VAL B 21
REMARK 465 GLU B 22
REMARK 465 ASN B 250
REMARK 465 ASP B 251
REMARK 465 PHE B 252
REMARK 465 ASN B 253
REMARK 465 LEU B 254
REMARK 465 ARG B 255
REMARK 465 ASP B 256
REMARK 465 PHE B 257
REMARK 465 ASN B 258
REMARK 465 VAL B 259
REMARK 465 GLY B 260
REMARK 465 GLY B 317
REMARK 465 SER B 318
REMARK 465 THR B 319
REMARK 465 ARG B 320
REMARK 465 GLY B 321
REMARK 465 ALA B 322
REMARK 465 GLY B 323
REMARK 465 LEU B 832
REMARK 465 LYS B 833
REMARK 465 ILE B 834
REMARK 465 SER B 835
REMARK 465 LEU B 836
REMARK 465 SER B 837
REMARK 465 ASN B 838
REMARK 465 GLU B 839
REMARK 465 SER B 840
REMARK 465 ASN B 841
REMARK 465 LYS B 842
REMARK 465 VAL B 843
REMARK 465 ASN B 844
REMARK 465 GLY B 845
REMARK 465 ASN B 846
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 LEU A 136 CA - CB - CG ANGL. DEV. = 14.6 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 LEU A 131 38.86 -92.70
REMARK 500 TYR A 203 -132.89 58.92
REMARK 500 PRO A 281 27.19 -70.31
REMARK 500 VAL A 325 -12.40 42.60
REMARK 500 ASP A 339 -168.66 73.66
REMARK 500 VAL A 379 -40.95 -131.40
REMARK 500 LEU A 492 -68.22 -152.69
REMARK 500 ILE A 666 30.21 -99.14
REMARK 500 SER A 674 -69.71 -148.89
REMARK 500 PHE A 709 73.66 -103.22
REMARK 500 SER A 751 76.87 -150.38
REMARK 500 LYS A 772 61.77 27.90
REMARK 500 LEU B 131 40.10 -89.78
REMARK 500 PHE B 166 150.02 -49.20
REMARK 500 ARG B 193 76.79 -119.84
REMARK 500 TYR B 203 -132.51 57.84
REMARK 500 PRO B 281 31.81 -72.62
REMARK 500 ASP B 339 -175.51 75.05
REMARK 500 LYS B 466 -73.07 -118.16
REMARK 500 LEU B 492 -65.96 -153.40
REMARK 500 SER B 674 -64.75 -149.78
REMARK 500 PHE B 709 78.28 -101.63
REMARK 500 LYS B 772 62.24 36.02
REMARK 500 ILE B 824 -57.58 -121.56
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 52 0.07 SIDE CHAIN
REMARK 500 TYR B 52 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 VAL A 325 22.3 L L OUTSIDE RANGE
REMARK 500 TRP A 491 24.9 L L OUTSIDE RANGE
REMARK 500 THR B 94 24.0 L L OUTSIDE RANGE
REMARK 500 TRP B 491 24.3 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A2493 DISTANCE = 5.21 ANGSTROMS
REMARK 525 HOH A2637 DISTANCE = 5.92 ANGSTROMS
REMARK 525 HOH A2736 DISTANCE = 7.40 ANGSTROMS
REMARK 525 HOH A2775 DISTANCE = 5.95 ANGSTROMS
REMARK 525 HOH A2834 DISTANCE = 5.61 ANGSTROMS
REMARK 525 HOH B2844 DISTANCE = 5.88 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 847
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC B 847
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IHU A 848
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IHU B 848
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP B 1001
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1WUT RELATED DB: PDB
REMARK 900 RELATED ID: 1WUY RELATED DB: PDB
REMARK 900 RELATED ID: 1WV0 RELATED DB: PDB
REMARK 900 RELATED ID: 1WV1 RELATED DB: PDB
DBREF 2ATI A 1 846 UNP P06737 PYGL_HUMAN 1 846
DBREF 2ATI B 1 846 UNP P06737 PYGL_HUMAN 1 846
SEQRES 1 A 846 ALA LYS PRO LEU THR ASP GLN GLU LYS ARG ARG GLN ILE
SEQRES 2 A 846 SER ILE ARG GLY ILE VAL GLY VAL GLU ASN VAL ALA GLU
SEQRES 3 A 846 LEU LYS LYS SER PHE ASN ARG HIS LEU HIS PHE THR LEU
SEQRES 4 A 846 VAL LYS ASP ARG ASN VAL ALA THR THR ARG ASP TYR TYR
SEQRES 5 A 846 PHE ALA LEU ALA HIS THR VAL ARG ASP HIS LEU VAL GLY
SEQRES 6 A 846 ARG TRP ILE ARG THR GLN GLN HIS TYR TYR ASP LYS CYS
SEQRES 7 A 846 PRO LYS ARG VAL TYR TYR LEU SER LEU GLU PHE TYR MET
SEQRES 8 A 846 GLY ARG THR LEU GLN ASN THR MET ILE ASN LEU GLY LEU
SEQRES 9 A 846 GLN ASN ALA CYS ASP GLU ALA ILE TYR GLN LEU GLY LEU
SEQRES 10 A 846 ASP ILE GLU GLU LEU GLU GLU ILE GLU GLU ASP ALA GLY
SEQRES 11 A 846 LEU GLY ASN GLY GLY LEU GLY ARG LEU ALA ALA CYS PHE
SEQRES 12 A 846 LEU ASP SER MET ALA THR LEU GLY LEU ALA ALA TYR GLY
SEQRES 13 A 846 TYR GLY ILE ARG TYR GLU TYR GLY ILE PHE ASN GLN LYS
SEQRES 14 A 846 ILE ARG ASP GLY TRP GLN VAL GLU GLU ALA ASP ASP TRP
SEQRES 15 A 846 LEU ARG TYR GLY ASN PRO TRP GLU LYS SER ARG PRO GLU
SEQRES 16 A 846 PHE MET LEU PRO VAL HIS PHE TYR GLY LYS VAL GLU HIS
SEQRES 17 A 846 THR ASN THR GLY THR LYS TRP ILE ASP THR GLN VAL VAL
SEQRES 18 A 846 LEU ALA LEU PRO TYR ASP THR PRO VAL PRO GLY TYR MET
SEQRES 19 A 846 ASN ASN THR VAL ASN THR MET ARG LEU TRP SER ALA ARG
SEQRES 20 A 846 ALA PRO ASN ASP PHE ASN LEU ARG ASP PHE ASN VAL GLY
SEQRES 21 A 846 ASP TYR ILE GLN ALA VAL LEU ASP ARG ASN LEU ALA GLU
SEQRES 22 A 846 ASN ILE SER ARG VAL LEU TYR PRO ASN ASP ASN PHE PHE
SEQRES 23 A 846 GLU GLY LYS GLU LEU ARG LEU LYS GLN GLU TYR PHE VAL
SEQRES 24 A 846 VAL ALA ALA THR LEU GLN ASP ILE ILE ARG ARG PHE LYS
SEQRES 25 A 846 ALA SER LYS PHE GLY SER THR ARG GLY ALA GLY THR VAL
SEQRES 26 A 846 PHE ASP ALA PHE PRO ASP GLN VAL ALA ILE GLN LEU ASN
SEQRES 27 A 846 ASP THR HIS PRO ALA LEU ALA ILE PRO GLU LEU MET ARG
SEQRES 28 A 846 ILE PHE VAL ASP ILE GLU LYS LEU PRO TRP SER LYS ALA
SEQRES 29 A 846 TRP GLU LEU THR GLN LYS THR PHE ALA TYR THR ASN HIS
SEQRES 30 A 846 THR VAL LEU PRO GLU ALA LEU GLU ARG TRP PRO VAL ASP
SEQRES 31 A 846 LEU VAL GLU LYS LEU LEU PRO ARG HIS LEU GLU ILE ILE
SEQRES 32 A 846 TYR GLU ILE ASN GLN LYS HIS LEU ASP ARG ILE VAL ALA
SEQRES 33 A 846 LEU PHE PRO LYS ASP VAL ASP ARG LEU ARG ARG MET SER
SEQRES 34 A 846 LEU ILE GLU GLU GLU GLY SER LYS ARG ILE ASN MET ALA
SEQRES 35 A 846 HIS LEU CYS ILE VAL GLY SER HIS ALA VAL ASN GLY VAL
SEQRES 36 A 846 ALA LYS ILE HIS SER ASP ILE VAL LYS THR LYS VAL PHE
SEQRES 37 A 846 LYS ASP PHE SER GLU LEU GLU PRO ASP LYS PHE GLN ASN
SEQRES 38 A 846 LYS THR ASN GLY ILE THR PRO ARG ARG TRP LEU LEU LEU
SEQRES 39 A 846 CYS ASN PRO GLY LEU ALA GLU LEU ILE ALA GLU LYS ILE
SEQRES 40 A 846 GLY GLU ASP TYR VAL LYS ASP LEU SER GLN LEU THR LYS
SEQRES 41 A 846 LEU HIS SER PHE LEU GLY ASP ASP VAL PHE LEU ARG GLU
SEQRES 42 A 846 LEU ALA LYS VAL LYS GLN GLU ASN LYS LEU LYS PHE SER
SEQRES 43 A 846 GLN PHE LEU GLU THR GLU TYR LYS VAL LYS ILE ASN PRO
SEQRES 44 A 846 SER SER MET PHE ASP VAL GLN VAL LYS ARG ILE HIS GLU
SEQRES 45 A 846 TYR LYS ARG GLN LEU LEU ASN CYS LEU HIS VAL ILE THR
SEQRES 46 A 846 MET TYR ASN ARG ILE LYS LYS ASP PRO LYS LYS LEU PHE
SEQRES 47 A 846 VAL PRO ARG THR VAL ILE ILE GLY GLY LYS ALA ALA PRO
SEQRES 48 A 846 GLY TYR HIS MET ALA LYS MET ILE ILE LYS LEU ILE THR
SEQRES 49 A 846 SER VAL ALA ASP VAL VAL ASN ASN ASP PRO MET VAL GLY
SEQRES 50 A 846 SER LYS LEU LYS VAL ILE PHE LEU GLU ASN TYR ARG VAL
SEQRES 51 A 846 SER LEU ALA GLU LYS VAL ILE PRO ALA THR ASP LEU SER
SEQRES 52 A 846 GLU GLN ILE SER THR ALA GLY THR GLU ALA SER GLY THR
SEQRES 53 A 846 GLY ASN MET LYS PHE MET LEU ASN GLY ALA LEU THR ILE
SEQRES 54 A 846 GLY THR MET ASP GLY ALA ASN VAL GLU MET ALA GLU GLU
SEQRES 55 A 846 ALA GLY GLU GLU ASN LEU PHE ILE PHE GLY MET ARG ILE
SEQRES 56 A 846 ASP ASP VAL ALA ALA LEU ASP LYS LYS GLY TYR GLU ALA
SEQRES 57 A 846 LYS GLU TYR TYR GLU ALA LEU PRO GLU LEU LYS LEU VAL
SEQRES 58 A 846 ILE ASP GLN ILE ASP ASN GLY PHE PHE SER PRO LYS GLN
SEQRES 59 A 846 PRO ASP LEU PHE LYS ASP ILE ILE ASN MET LEU PHE TYR
SEQRES 60 A 846 HIS ASP ARG PHE LYS VAL PHE ALA ASP TYR GLU ALA TYR
SEQRES 61 A 846 VAL LYS CYS GLN ASP LYS VAL SER GLN LEU TYR MET ASN
SEQRES 62 A 846 PRO LYS ALA TRP ASN THR MET VAL LEU LYS ASN ILE ALA
SEQRES 63 A 846 ALA SER GLY LYS PHE SER SER ASP ARG THR ILE LYS GLU
SEQRES 64 A 846 TYR ALA GLN ASN ILE TRP ASN VAL GLU PRO SER ASP LEU
SEQRES 65 A 846 LYS ILE SER LEU SER ASN GLU SER ASN LYS VAL ASN GLY
SEQRES 66 A 846 ASN
SEQRES 1 B 846 ALA LYS PRO LEU THR ASP GLN GLU LYS ARG ARG GLN ILE
SEQRES 2 B 846 SER ILE ARG GLY ILE VAL GLY VAL GLU ASN VAL ALA GLU
SEQRES 3 B 846 LEU LYS LYS SER PHE ASN ARG HIS LEU HIS PHE THR LEU
SEQRES 4 B 846 VAL LYS ASP ARG ASN VAL ALA THR THR ARG ASP TYR TYR
SEQRES 5 B 846 PHE ALA LEU ALA HIS THR VAL ARG ASP HIS LEU VAL GLY
SEQRES 6 B 846 ARG TRP ILE ARG THR GLN GLN HIS TYR TYR ASP LYS CYS
SEQRES 7 B 846 PRO LYS ARG VAL TYR TYR LEU SER LEU GLU PHE TYR MET
SEQRES 8 B 846 GLY ARG THR LEU GLN ASN THR MET ILE ASN LEU GLY LEU
SEQRES 9 B 846 GLN ASN ALA CYS ASP GLU ALA ILE TYR GLN LEU GLY LEU
SEQRES 10 B 846 ASP ILE GLU GLU LEU GLU GLU ILE GLU GLU ASP ALA GLY
SEQRES 11 B 846 LEU GLY ASN GLY GLY LEU GLY ARG LEU ALA ALA CYS PHE
SEQRES 12 B 846 LEU ASP SER MET ALA THR LEU GLY LEU ALA ALA TYR GLY
SEQRES 13 B 846 TYR GLY ILE ARG TYR GLU TYR GLY ILE PHE ASN GLN LYS
SEQRES 14 B 846 ILE ARG ASP GLY TRP GLN VAL GLU GLU ALA ASP ASP TRP
SEQRES 15 B 846 LEU ARG TYR GLY ASN PRO TRP GLU LYS SER ARG PRO GLU
SEQRES 16 B 846 PHE MET LEU PRO VAL HIS PHE TYR GLY LYS VAL GLU HIS
SEQRES 17 B 846 THR ASN THR GLY THR LYS TRP ILE ASP THR GLN VAL VAL
SEQRES 18 B 846 LEU ALA LEU PRO TYR ASP THR PRO VAL PRO GLY TYR MET
SEQRES 19 B 846 ASN ASN THR VAL ASN THR MET ARG LEU TRP SER ALA ARG
SEQRES 20 B 846 ALA PRO ASN ASP PHE ASN LEU ARG ASP PHE ASN VAL GLY
SEQRES 21 B 846 ASP TYR ILE GLN ALA VAL LEU ASP ARG ASN LEU ALA GLU
SEQRES 22 B 846 ASN ILE SER ARG VAL LEU TYR PRO ASN ASP ASN PHE PHE
SEQRES 23 B 846 GLU GLY LYS GLU LEU ARG LEU LYS GLN GLU TYR PHE VAL
SEQRES 24 B 846 VAL ALA ALA THR LEU GLN ASP ILE ILE ARG ARG PHE LYS
SEQRES 25 B 846 ALA SER LYS PHE GLY SER THR ARG GLY ALA GLY THR VAL
SEQRES 26 B 846 PHE ASP ALA PHE PRO ASP GLN VAL ALA ILE GLN LEU ASN
SEQRES 27 B 846 ASP THR HIS PRO ALA LEU ALA ILE PRO GLU LEU MET ARG
SEQRES 28 B 846 ILE PHE VAL ASP ILE GLU LYS LEU PRO TRP SER LYS ALA
SEQRES 29 B 846 TRP GLU LEU THR GLN LYS THR PHE ALA TYR THR ASN HIS
SEQRES 30 B 846 THR VAL LEU PRO GLU ALA LEU GLU ARG TRP PRO VAL ASP
SEQRES 31 B 846 LEU VAL GLU LYS LEU LEU PRO ARG HIS LEU GLU ILE ILE
SEQRES 32 B 846 TYR GLU ILE ASN GLN LYS HIS LEU ASP ARG ILE VAL ALA
SEQRES 33 B 846 LEU PHE PRO LYS ASP VAL ASP ARG LEU ARG ARG MET SER
SEQRES 34 B 846 LEU ILE GLU GLU GLU GLY SER LYS ARG ILE ASN MET ALA
SEQRES 35 B 846 HIS LEU CYS ILE VAL GLY SER HIS ALA VAL ASN GLY VAL
SEQRES 36 B 846 ALA LYS ILE HIS SER ASP ILE VAL LYS THR LYS VAL PHE
SEQRES 37 B 846 LYS ASP PHE SER GLU LEU GLU PRO ASP LYS PHE GLN ASN
SEQRES 38 B 846 LYS THR ASN GLY ILE THR PRO ARG ARG TRP LEU LEU LEU
SEQRES 39 B 846 CYS ASN PRO GLY LEU ALA GLU LEU ILE ALA GLU LYS ILE
SEQRES 40 B 846 GLY GLU ASP TYR VAL LYS ASP LEU SER GLN LEU THR LYS
SEQRES 41 B 846 LEU HIS SER PHE LEU GLY ASP ASP VAL PHE LEU ARG GLU
SEQRES 42 B 846 LEU ALA LYS VAL LYS GLN GLU ASN LYS LEU LYS PHE SER
SEQRES 43 B 846 GLN PHE LEU GLU THR GLU TYR LYS VAL LYS ILE ASN PRO
SEQRES 44 B 846 SER SER MET PHE ASP VAL GLN VAL LYS ARG ILE HIS GLU
SEQRES 45 B 846 TYR LYS ARG GLN LEU LEU ASN CYS LEU HIS VAL ILE THR
SEQRES 46 B 846 MET TYR ASN ARG ILE LYS LYS ASP PRO LYS LYS LEU PHE
SEQRES 47 B 846 VAL PRO ARG THR VAL ILE ILE GLY GLY LYS ALA ALA PRO
SEQRES 48 B 846 GLY TYR HIS MET ALA LYS MET ILE ILE LYS LEU ILE THR
SEQRES 49 B 846 SER VAL ALA ASP VAL VAL ASN ASN ASP PRO MET VAL GLY
SEQRES 50 B 846 SER LYS LEU LYS VAL ILE PHE LEU GLU ASN TYR ARG VAL
SEQRES 51 B 846 SER LEU ALA GLU LYS VAL ILE PRO ALA THR ASP LEU SER
SEQRES 52 B 846 GLU GLN ILE SER THR ALA GLY THR GLU ALA SER GLY THR
SEQRES 53 B 846 GLY ASN MET LYS PHE MET LEU ASN GLY ALA LEU THR ILE
SEQRES 54 B 846 GLY THR MET ASP GLY ALA ASN VAL GLU MET ALA GLU GLU
SEQRES 55 B 846 ALA GLY GLU GLU ASN LEU PHE ILE PHE GLY MET ARG ILE
SEQRES 56 B 846 ASP ASP VAL ALA ALA LEU ASP LYS LYS GLY TYR GLU ALA
SEQRES 57 B 846 LYS GLU TYR TYR GLU ALA LEU PRO GLU LEU LYS LEU VAL
SEQRES 58 B 846 ILE ASP GLN ILE ASP ASN GLY PHE PHE SER PRO LYS GLN
SEQRES 59 B 846 PRO ASP LEU PHE LYS ASP ILE ILE ASN MET LEU PHE TYR
SEQRES 60 B 846 HIS ASP ARG PHE LYS VAL PHE ALA ASP TYR GLU ALA TYR
SEQRES 61 B 846 VAL LYS CYS GLN ASP LYS VAL SER GLN LEU TYR MET ASN
SEQRES 62 B 846 PRO LYS ALA TRP ASN THR MET VAL LEU LYS ASN ILE ALA
SEQRES 63 B 846 ALA SER GLY LYS PHE SER SER ASP ARG THR ILE LYS GLU
SEQRES 64 B 846 TYR ALA GLN ASN ILE TRP ASN VAL GLU PRO SER ASP LEU
SEQRES 65 B 846 LYS ILE SER LEU SER ASN GLU SER ASN LYS VAL ASN GLY
SEQRES 66 B 846 ASN
HET GLC A 847 12
HET GLC B 847 12
HET IHU A 848 23
HET IHU B 848 23
HET PLP A1001 15
HET PLP B1001 15
HETNAM GLC ALPHA-D-GLUCOSE
HETNAM IHU N-(2-CHLORO-4-FLUOROBENZOYL)-N'-(5-HYDROXY-2-
HETNAM 2 IHU METHOXYPHENYL)UREA
HETNAM PLP PYRIDOXAL-5'-PHOSPHATE
HETSYN IHU 1-(2-CHLORO-4-FLUORO-BENZOYL)-3-(5-HYDROXY-2-METHOXY-
HETSYN 2 IHU PHENYL)-UREA
HETSYN PLP VITAMIN B6 PHOSPHATE
FORMUL 3 GLC 2(C6 H12 O6)
FORMUL 5 IHU 2(C15 H12 CL F N2 O4)
FORMUL 7 PLP 2(C8 H10 N O6 P)
FORMUL 9 HOH *759(H2 O)
HELIX 1 1 ASN A 23 THR A 38 1 16
HELIX 2 2 THR A 47 HIS A 62 1 16
HELIX 3 3 LEU A 63 CYS A 78 1 16
HELIX 4 4 THR A 94 LEU A 102 1 9
HELIX 5 5 LEU A 104 LEU A 115 1 12
HELIX 6 6 ASP A 118 GLU A 124 1 7
HELIX 7 7 GLY A 134 LEU A 150 1 17
HELIX 8 8 PRO A 194 MET A 197 5 4
HELIX 9 9 ASP A 261 ASP A 268 1 8
HELIX 10 10 ARG A 269 ASN A 274 1 6
HELIX 11 11 ILE A 275 ARG A 277 5 3
HELIX 12 12 LYS A 289 SER A 314 1 26
HELIX 13 13 ALA A 328 ASP A 331 5 4
HELIX 14 14 LEU A 344 ILE A 356 1 13
HELIX 15 15 PRO A 360 THR A 371 1 12
HELIX 16 16 LEU 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 LYS A 466 1 11
HELIX 22 22 PHE A 468 GLU A 473 1 6
HELIX 23 23 ASN A 496 GLY A 508 1 13
HELIX 24 24 GLU A 509 LYS A 513 5 5
HELIX 25 25 ASP A 514 LEU A 525 5 12
HELIX 26 26 ASP A 527 TYR A 553 1 27
HELIX 27 27 ARG A 575 ASP A 593 1 19
HELIX 28 28 TYR A 613 ASN A 632 1 20
HELIX 29 29 VAL A 636 SER A 638 5 3
HELIX 30 30 ARG A 649 ILE A 657 1 9
HELIX 31 31 PRO A 658 THR 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 LEU A 708 5 4
HELIX 35 35 ARG A 714 GLY A 725 1 12
HELIX 36 36 GLU A 727 LEU A 735 1 9
HELIX 37 37 LEU A 735 ASN A 747 1 13
HELIX 38 38 PHE A 758 HIS A 768 1 11
HELIX 39 39 LYS A 772 MET A 792 1 21
HELIX 40 40 ASN A 793 ALA A 807 1 15
HELIX 41 41 SER A 808 PHE A 811 5 4
HELIX 42 42 SER A 812 ILE A 824 1 13
HELIX 43 43 ASN B 23 THR B 38 1 16
HELIX 44 44 THR B 47 HIS B 62 1 16
HELIX 45 45 LEU B 63 CYS B 78 1 16
HELIX 46 46 THR B 94 LEU B 102 1 9
HELIX 47 47 LEU B 104 LEU B 115 1 12
HELIX 48 48 ASP B 118 GLU B 124 1 7
HELIX 49 49 GLY B 134 LEU B 150 1 17
HELIX 50 50 PRO B 194 MET B 197 5 4
HELIX 51 51 ASP B 261 ASP B 268 1 8
HELIX 52 52 ARG B 269 ASN B 274 1 6
HELIX 53 53 ILE B 275 ARG B 277 5 3
HELIX 54 54 LYS B 289 SER B 314 1 26
HELIX 55 55 ALA B 328 GLN B 332 1 5
HELIX 56 56 LEU B 344 ILE B 356 1 13
HELIX 57 57 PRO B 360 THR B 371 1 12
HELIX 58 58 LEU B 380 LEU B 384 5 5
HELIX 59 59 VAL B 389 LEU B 396 1 8
HELIX 60 60 LEU B 396 PHE B 418 1 23
HELIX 61 61 VAL B 422 SER B 429 1 8
HELIX 62 62 MET B 441 GLY B 448 1 8
HELIX 63 63 ALA B 456 LYS B 466 1 11
HELIX 64 64 PHE B 468 GLU B 475 1 8
HELIX 65 65 ASN B 496 GLY B 508 1 13
HELIX 66 66 GLU B 509 VAL B 512 5 4
HELIX 67 67 ASP B 514 LEU B 525 5 12
HELIX 68 68 ASP B 527 TYR B 553 1 27
HELIX 69 69 ARG B 575 ASP B 593 1 19
HELIX 70 70 TYR B 613 ASN B 632 1 20
HELIX 71 71 VAL B 636 SER B 638 5 3
HELIX 72 72 ARG B 649 ILE B 657 1 9
HELIX 73 73 PRO B 658 THR B 660 5 3
HELIX 74 74 THR B 676 ASN B 684 1 9
HELIX 75 75 ALA B 695 GLY B 704 1 10
HELIX 76 76 GLU B 705 LEU B 708 5 4
HELIX 77 77 ARG B 714 GLY B 725 1 12
HELIX 78 78 ALA B 728 LEU B 735 1 8
HELIX 79 79 LEU B 735 GLY B 748 1 14
HELIX 80 80 PHE B 758 HIS B 768 1 11
HELIX 81 81 ASP B 776 MET B 792 1 17
HELIX 82 82 ASN B 793 ALA B 806 1 14
HELIX 83 83 SER B 808 PHE B 811 5 4
HELIX 84 84 SER B 812 ILE B 824 1 13
SHEET 1 A 3 LYS A 191 SER A 192 0
SHEET 2 A 3 GLN A 219 PRO A 231 -1 O ASP A 227 N LYS A 191
SHEET 3 A 3 LEU A 198 PHE A 202 -1 N PHE A 202 O GLN A 219
SHEET 1 B 9 LYS A 191 SER A 192 0
SHEET 2 B 9 GLN A 219 PRO A 231 -1 O ASP A 227 N LYS A 191
SHEET 3 B 9 VAL A 238 ARG A 247 -1 O LEU A 243 N TYR A 226
SHEET 4 B 9 ALA A 154 ILE A 159 1 N GLY A 156 O ARG A 242
SHEET 5 B 9 ARG A 81 LEU A 85 1 N TYR A 84 O TYR A 155
SHEET 6 B 9 VAL A 333 ASN A 338 1 O ALA A 334 N TYR A 83
SHEET 7 B 9 PHE A 372 THR A 375 1 O ALA A 373 N LEU A 337
SHEET 8 B 9 ALA A 451 GLY A 454 1 O ALA A 451 N TYR A 374
SHEET 9 B 9 PHE A 479 ASN A 481 1 O GLN A 480 N VAL A 452
SHEET 1 C 2 PHE A 89 GLY A 92 0
SHEET 2 C 2 ALA A 129 LEU A 131 -1 O LEU A 131 N PHE A 89
SHEET 1 D 2 ASN A 167 ARG A 171 0
SHEET 2 D 2 TRP A 174 GLU A 178 -1 O GLU A 178 N ASN A 167
SHEET 1 E 2 LYS A 205 THR A 209 0
SHEET 2 E 2 GLY A 212 ILE A 216 -1 O LYS A 214 N GLU A 207
SHEET 1 F 3 ARG A 386 PRO A 388 0
SHEET 2 F 3 ARG A 438 ASN A 440 -1 O ILE A 439 N TRP A 387
SHEET 3 F 3 ILE A 431 GLU A 432 -1 N GLU A 432 O ARG A 438
SHEET 1 G 6 LEU A 640 LEU A 645 0
SHEET 2 G 6 ARG A 601 GLY A 606 1 N VAL A 603 O LYS A 641
SHEET 3 G 6 MET A 562 VAL A 567 1 N ASP A 564 O ILE A 604
SHEET 4 G 6 LEU A 662 GLN A 665 1 O LEU A 662 N VAL A 565
SHEET 5 G 6 LEU A 687 GLY A 690 1 O LEU A 687 N SER A 663
SHEET 6 G 6 PHE A 709 ILE A 710 1 O PHE A 709 N THR A 688
SHEET 1 H 3 LYS B 191 SER B 192 0
SHEET 2 H 3 GLN B 219 PRO B 231 -1 O ASP B 227 N LYS B 191
SHEET 3 H 3 LEU B 198 PHE B 202 -1 N PHE B 202 O GLN B 219
SHEET 1 I 9 LYS B 191 SER B 192 0
SHEET 2 I 9 GLN B 219 PRO B 231 -1 O ASP B 227 N LYS B 191
SHEET 3 I 9 VAL B 238 ARG B 247 -1 O SER B 245 N LEU B 224
SHEET 4 I 9 ALA B 154 ILE B 159 1 N GLY B 156 O ARG B 242
SHEET 5 I 9 ARG B 81 LEU B 85 1 N TYR B 84 O TYR B 155
SHEET 6 I 9 VAL B 333 ASN B 338 1 O ALA B 334 N TYR B 83
SHEET 7 I 9 PHE B 372 THR B 375 1 O ALA B 373 N LEU B 337
SHEET 8 I 9 ALA B 451 GLY B 454 1 O ASN B 453 N TYR B 374
SHEET 9 I 9 PHE B 479 ASN B 481 1 O GLN B 480 N VAL B 452
SHEET 1 J 2 PHE B 89 GLY B 92 0
SHEET 2 J 2 ALA B 129 LEU B 131 -1 O LEU B 131 N PHE B 89
SHEET 1 K 2 ASN B 167 ARG B 171 0
SHEET 2 K 2 TRP B 174 GLU B 178 -1 O TRP B 174 N ARG B 171
SHEET 1 L 2 LYS B 205 THR B 209 0
SHEET 2 L 2 GLY B 212 ILE B 216 -1 O ILE B 216 N LYS B 205
SHEET 1 M 3 ARG B 386 PRO B 388 0
SHEET 2 M 3 ARG B 438 ASN B 440 -1 O ILE B 439 N TRP B 387
SHEET 3 M 3 ILE B 431 GLU B 432 -1 N GLU B 432 O ARG B 438
SHEET 1 N 6 LEU B 640 LEU B 645 0
SHEET 2 N 6 ARG B 601 GLY B 606 1 N VAL B 603 O ILE B 643
SHEET 3 N 6 MET B 562 VAL B 567 1 N ASP B 564 O ILE B 604
SHEET 4 N 6 LEU B 662 GLN B 665 1 O LEU B 662 N PHE B 563
SHEET 5 N 6 LEU B 687 GLY B 690 1 O LEU B 687 N SER B 663
SHEET 6 N 6 PHE B 709 ILE B 710 1 O PHE B 709 N THR B 688
LINK C4A PLP A1001 NZ LYS A 680 1555 1555 1.29
LINK C4A PLP B1001 NZ LYS B 680 1555 1555 1.29
SITE 1 AC1 13 GLY A 135 LEU A 136 ASN A 284 HIS A 377
SITE 2 AC1 13 VAL A 455 ASN A 484 TYR A 573 GLU A 672
SITE 3 AC1 13 ALA A 673 SER A 674 GLY A 675 HOH A2111
SITE 4 AC1 13 HOH A2361
SITE 1 AC2 16 GLY B 135 LEU B 136 LEU B 139 ASN B 284
SITE 2 AC2 16 HIS B 377 VAL B 455 ASN B 484 TYR B 573
SITE 3 AC2 16 GLU B 672 ALA B 673 SER B 674 GLY B 675
SITE 4 AC2 16 HOH B2039 HOH B2318 HOH B2339 HOH B2829
SITE 1 AC3 11 VAL A 40 ASP A 42 ASN A 44 VAL A 45
SITE 2 AC3 11 HOH A2141 TRP B 67 ILE B 68 GLN B 71
SITE 3 AC3 11 GLN B 72 LYS B 191 ARG B 193
SITE 1 AC4 12 TRP A 67 ILE A 68 GLN A 71 GLN A 72
SITE 2 AC4 12 LYS A 191 ARG A 193 VAL B 40 LYS B 41
SITE 3 AC4 12 ASP B 42 ASN B 44 VAL B 45 HOH B2232
SITE 1 AC5 17 TYR A 90 TRP A 491 LYS A 568 LYS A 574
SITE 2 AC5 17 TYR A 648 ARG A 649 VAL A 650 ALA A 653
SITE 3 AC5 17 GLY A 675 THR A 676 GLY A 677 LYS A 680
SITE 4 AC5 17 HOH A2013 HOH A2098 HOH A2130 HOH A2170
SITE 5 AC5 17 HOH A2264
SITE 1 AC6 19 TYR B 90 GLY B 135 TRP B 491 LYS B 568
SITE 2 AC6 19 LYS B 574 TYR B 648 ARG B 649 VAL B 650
SITE 3 AC6 19 GLY B 675 THR B 676 GLY B 677 LYS B 680
SITE 4 AC6 19 HOH B2039 HOH B2085 HOH B2117 HOH B2136
SITE 5 AC6 19 HOH B2159 HOH B2188 HOH B2468
CRYST1 124.500 124.500 123.200 90.00 90.00 120.00 P 31 6
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 0.008032 0.004637 0.000000 0.00000
SCALE2 0.000000 0.009275 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008117 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
