HEADER TRANSFERASE 17-JUL-00 1FC0
TITLE HUMAN LIVER GLYCOGEN PHOSPHORYLASE COMPLEXED WITH N-ACETYL-BETA-D-
TITLE 2 GLUCOPYRANOSYLAMINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLYCOGEN PHOSPHORYLASE, LIVER FORM;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 2.4.1.1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 TISSUE: LIVER;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: SF9;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR: BACULOVIRUS;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PBLUEBAC III
KEYWDS PHOSPHORYLATED PROTEIN, ALLOSTERIC, GLUCOSE ANALOG, INHIBITOR,
KEYWDS 2 TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR V.L.RATH,M.AMMIRATI,P.K.LEMOTTE,K.F.FENNELL,M.M.MANSOUR,D.E.DANLEY,
AUTHOR 2 T.R.HYNES,G.K.SCHULTE,D.J.WASILKO,J.PANDIT
REVDAT 4 13-JUL-11 1FC0 1 VERSN
REVDAT 3 24-FEB-09 1FC0 1 VERSN
REVDAT 2 01-APR-03 1FC0 1 JRNL
REVDAT 1 25-AUG-00 1FC0 0
JRNL AUTH V.L.RATH,M.AMMIRATI,P.K.LEMOTTE,K.F.FENNELL,M.N.MANSOUR,
JRNL AUTH 2 D.E.DANLEY,T.R.HYNES,G.K.SCHULTE,D.J.WASILKO,J.PANDIT
JRNL TITL ACTIVATION OF HUMAN LIVER GLYCOGEN PHOSPHORYLASE BY
JRNL TITL 2 ALTERATION OF THE SECONDARY STRUCTURE AND PACKING OF THE
JRNL TITL 3 CATALYTIC CORE.
JRNL REF MOL.CELL V. 6 139 2000
JRNL REFN ISSN 1097-2765
JRNL PMID 10949035
JRNL DOI 10.1016/S1097-2765(00)00015-0
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 0.5
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 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 549432.890
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.1
REMARK 3 NUMBER OF REFLECTIONS : 78076
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) : 0.198
REMARK 3 FREE R VALUE : 0.235
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 7804
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.003
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.55
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 85.70
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 10520
REMARK 3 BIN R VALUE (WORKING SET) : 0.2680
REMARK 3 BIN FREE R VALUE : 0.2830
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.10
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 1183
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.008
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 12854
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 60
REMARK 3 SOLVENT ATOMS : 255
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 26.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.72000
REMARK 3 B22 (A**2) : -2.72000
REMARK 3 B33 (A**2) : 5.43000
REMARK 3 B12 (A**2) : 0.99000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.28
REMARK 3 ESD FROM SIGMAA (A) : 0.32
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.33
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.32
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.012
REMARK 3 BOND ANGLES (DEGREES) : 2.00
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.80
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.52
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 2.580 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 3.950 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 4.020 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 5.780 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.36
REMARK 3 BSOL : 46.63
REMARK 3
REMARK 3 NCS MODEL : CONSTR
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : PLPPHO.PARAM
REMARK 3 PARAMETER FILE 4 : GNC.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : PLPPHO_PATCH.TOP
REMARK 3 TOPOLOGY FILE 4 : GNC.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1FC0 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-AUG-00.
REMARK 100 THE RCSB ID CODE IS RCSB011467.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-FEB-98
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
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) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
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 : 81720
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 5.300
REMARK 200 R MERGE (I) : 0.04700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.8
REMARK 200 DATA REDUNDANCY IN SHELL : 2.00
REMARK 200 R MERGE FOR SHELL (I) : 0.17400
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: CNS
REMARK 200 STARTING MODEL: 1FA9
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.96
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.79
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NAMES, MPD, N-ACETYL-BETA-D-
REMARK 280 GLYCOPYRANOSYLAMINE, PH 6.0, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 17K
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 40.76000
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 81.52000
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A DIMER RELATED BY A TWO FOLD
REMARK 300 NCS AXIS. MONOMER 1 CONSISTS OF RESIDUES A23-A831, MONOMER 2
REMARK 300 CONSISTS OF RESIDUES A1023-A1831.
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: 6430 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 56140 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 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 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 1001
REMARK 465 LYS B 1002
REMARK 465 PRO B 1003
REMARK 465 LEU B 1004
REMARK 465 THR B 1005
REMARK 465 ASP B 1006
REMARK 465 GLN B 1007
REMARK 465 GLU B 1008
REMARK 465 LYS B 1009
REMARK 465 ARG B 1010
REMARK 465 ARG B 1011
REMARK 465 GLN B 1012
REMARK 465 ILE B 1013
REMARK 465 SER B 1014
REMARK 465 ILE B 1015
REMARK 465 ARG B 1016
REMARK 465 GLY B 1017
REMARK 465 ILE B 1018
REMARK 465 VAL B 1019
REMARK 465 GLY B 1020
REMARK 465 VAL B 1021
REMARK 465 GLU B 1022
REMARK 465 ASN B 1250
REMARK 465 ASP B 1251
REMARK 465 PHE B 1252
REMARK 465 ASN B 1253
REMARK 465 LEU B 1254
REMARK 465 ARG B 1255
REMARK 465 ASP B 1256
REMARK 465 PHE B 1257
REMARK 465 ASN B 1258
REMARK 465 VAL B 1259
REMARK 465 GLY B 1317
REMARK 465 SER B 1318
REMARK 465 THR B 1319
REMARK 465 ARG B 1320
REMARK 465 GLY B 1321
REMARK 465 ALA B 1322
REMARK 465 LEU B 1832
REMARK 465 LYS B 1833
REMARK 465 ILE B 1834
REMARK 465 SER B 1835
REMARK 465 LEU B 1836
REMARK 465 SER B 1837
REMARK 465 ASN B 1838
REMARK 465 GLU B 1839
REMARK 465 SER B 1840
REMARK 465 ASN B 1841
REMARK 465 LYS B 1842
REMARK 465 VAL B 1843
REMARK 465 ASN B 1844
REMARK 465 GLY B 1845
REMARK 465 ASN B 1846
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 CYS A 78 55.68 36.79
REMARK 500 LEU A 95 -76.06 -35.29
REMARK 500 ALA A 129 72.08 -101.34
REMARK 500 LEU A 131 40.96 -88.74
REMARK 500 PHE A 166 157.08 -46.50
REMARK 500 ARG A 193 77.95 -117.98
REMARK 500 TYR A 203 -131.28 69.11
REMARK 500 HIS A 208 71.15 -111.03
REMARK 500 MET A 234 62.84 37.59
REMARK 500 ASN A 235 10.89 -152.01
REMARK 500 ASN A 236 -6.78 77.85
REMARK 500 PRO A 281 35.42 -75.33
REMARK 500 PHE A 326 0.60 -62.73
REMARK 500 ASP A 339 -177.31 70.77
REMARK 500 PRO A 342 30.09 -97.48
REMARK 500 LEU A 344 -9.73 -56.37
REMARK 500 VAL A 379 -44.12 -143.42
REMARK 500 GLU A 434 107.23 -51.39
REMARK 500 LYS A 466 -82.78 -99.10
REMARK 500 ASN A 484 171.08 -56.45
REMARK 500 LEU A 492 -74.09 -152.11
REMARK 500 LYS A 568 178.28 175.48
REMARK 500 ASP A 593 65.13 -177.67
REMARK 500 SER A 674 -60.02 -156.32
REMARK 500 SER A 751 66.10 -156.00
REMARK 500 LYS A 753 0.48 -66.37
REMARK 500 GLN A 754 68.23 -156.36
REMARK 500 PHE A 758 31.09 -96.63
REMARK 500 HIS A 768 44.47 -142.75
REMARK 500 LYS A 772 67.67 30.92
REMARK 500 ILE A 824 -54.94 -125.37
REMARK 500 CYS B1078 56.06 36.05
REMARK 500 LEU B1095 -76.20 -36.03
REMARK 500 LEU B1131 39.59 -89.40
REMARK 500 PHE B1166 157.30 -46.67
REMARK 500 TYR B1203 -132.19 68.73
REMARK 500 THR B1209 -169.86 -109.39
REMARK 500 MET B1234 62.82 37.89
REMARK 500 ASN B1235 11.06 -152.60
REMARK 500 ASN B1236 -7.26 78.36
REMARK 500 PRO B1281 36.50 -75.54
REMARK 500 SER B1314 -172.20 -65.85
REMARK 500 ASP B1339 -179.03 69.78
REMARK 500 LEU B1344 -9.45 -56.53
REMARK 500 GLU B1434 106.52 -51.15
REMARK 500 LYS B1466 -82.48 -99.13
REMARK 500 ASN B1484 172.28 -57.51
REMARK 500 LEU B1492 -73.03 -150.38
REMARK 500 LYS B1568 179.39 175.73
REMARK 500 LYS B1592 1.51 -69.97
REMARK 500
REMARK 500 THIS ENTRY HAS 59 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 NBG A 861
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NBG B 1861
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP A 860
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP B 1860
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1FA9 RELATED DB: PDB
REMARK 900 HUMAN LIVER GLYCOGEN PHOSPHORYLASE COMPLEXED WITH AMP
DBREF 1FC0 A 1 846 UNP P06737 PHS1_HUMAN 2 847
DBREF 1FC0 B 1001 1846 UNP P06737 PHS1_HUMAN 2 847
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 NBG A 861 15
HET NBG B1861 15
HET PLP A 860 15
HET PLP B1860 15
HETNAM NBG 1-N-ACETYL-BETA-D-GLUCOSAMINE
HETNAM PLP PYRIDOXAL-5'-PHOSPHATE
HETSYN PLP VITAMIN B6 PHOSPHATE
FORMUL 3 NBG 2(C8 H15 N O6)
FORMUL 5 PLP 2(C8 H10 N O6 P)
FORMUL 7 HOH *255(H2 O)
HELIX 1 1 ASN A 23 THR A 38 1 16
HELIX 2 2 THR A 47 CYS A 78 1 32
HELIX 3 3 THR A 94 GLY A 103 1 10
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 MET A 197 5 4
HELIX 8 8 ASP A 261 ASP A 268 1 8
HELIX 9 9 ARG A 269 ASN A 274 1 6
HELIX 10 10 ILE A 275 ARG A 277 5 3
HELIX 11 11 LYS A 289 LYS A 312 1 24
HELIX 12 12 THR A 324 ASP A 327 5 4
HELIX 13 13 ALA A 328 GLN A 332 1 5
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 VAL A 389 LEU A 396 1 8
HELIX 17 17 LEU A 396 PHE A 418 1 23
HELIX 18 18 ASP A 421 SER A 429 1 9
HELIX 19 19 MET A 441 GLY A 448 1 8
HELIX 20 20 ALA A 456 LYS A 466 1 11
HELIX 21 21 PHE A 468 GLU A 475 1 8
HELIX 22 22 ASN A 496 GLY A 508 1 13
HELIX 23 23 GLU A 509 LYS A 513 5 5
HELIX 24 24 ASP A 514 LEU A 525 5 12
HELIX 25 25 ASP A 527 TYR A 553 1 27
HELIX 26 26 HIS A 571 LYS A 574 5 4
HELIX 27 27 ARG A 575 LYS A 592 1 18
HELIX 28 28 TYR A 613 ASP A 633 1 21
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 VAL A 773 ALA A 775 5 3
HELIX 40 40 ASP A 776 MET A 792 1 17
HELIX 41 41 ASN A 793 ALA A 806 1 14
HELIX 42 42 ALA A 807 PHE A 811 5 5
HELIX 43 43 SER A 812 ILE A 824 1 13
HELIX 44 44 ASN B 1023 THR B 1038 1 16
HELIX 45 45 THR B 1047 CYS B 1078 1 32
HELIX 46 46 THR B 1094 LEU B 1102 1 9
HELIX 47 47 LEU B 1104 LEU B 1115 1 12
HELIX 48 48 ASP B 1118 GLU B 1124 1 7
HELIX 49 49 GLY B 1134 LEU B 1150 1 17
HELIX 50 50 PRO B 1194 MET B 1197 5 4
HELIX 51 51 ASP B 1261 ASP B 1268 1 8
HELIX 52 52 ARG B 1269 ASN B 1274 1 6
HELIX 53 53 ILE B 1275 ARG B 1277 5 3
HELIX 54 54 LYS B 1289 SER B 1314 1 26
HELIX 55 55 ALA B 1328 GLN B 1332 1 5
HELIX 56 56 LEU B 1344 ILE B 1356 1 13
HELIX 57 57 PRO B 1360 THR B 1371 1 12
HELIX 58 58 LEU B 1380 LEU B 1384 5 5
HELIX 59 59 VAL B 1389 LEU B 1396 1 8
HELIX 60 60 LEU B 1396 PHE B 1418 1 23
HELIX 61 61 ASP B 1421 SER B 1429 1 9
HELIX 62 62 MET B 1441 GLY B 1448 1 8
HELIX 63 63 ALA B 1456 LYS B 1466 1 11
HELIX 64 64 PHE B 1468 GLU B 1475 1 8
HELIX 65 65 ASN B 1496 GLY B 1508 1 13
HELIX 66 66 GLU B 1509 LYS B 1513 5 5
HELIX 67 67 ASP B 1514 LEU B 1525 5 12
HELIX 68 68 ASP B 1527 TYR B 1553 1 27
HELIX 69 69 HIS B 1571 LYS B 1574 5 4
HELIX 70 70 ARG B 1575 LYS B 1592 1 18
HELIX 71 71 TYR B 1613 ASP B 1633 1 21
HELIX 72 72 VAL B 1636 SER B 1638 5 3
HELIX 73 73 ARG B 1649 ILE B 1657 1 9
HELIX 74 74 PRO B 1658 THR B 1660 5 3
HELIX 75 75 THR B 1676 ASN B 1684 1 9
HELIX 76 76 ALA B 1695 GLY B 1704 1 10
HELIX 77 77 GLU B 1705 LEU B 1708 5 4
HELIX 78 78 ARG B 1714 GLY B 1725 1 12
HELIX 79 79 GLU B 1727 LEU B 1735 1 9
HELIX 80 80 LEU B 1735 ASN B 1747 1 13
HELIX 81 81 PHE B 1758 HIS B 1768 1 11
HELIX 82 82 VAL B 1773 ALA B 1775 5 3
HELIX 83 83 ASP B 1776 MET B 1792 1 17
HELIX 84 84 ASN B 1793 ALA B 1806 1 14
HELIX 85 85 ALA B 1807 PHE B 1811 5 5
HELIX 86 86 SER B 1812 ILE B 1824 1 13
SHEET 1 A 9 PHE A 479 ASN A 481 0
SHEET 2 A 9 ALA A 451 GLY A 454 1 O VAL A 452 N GLN A 480
SHEET 3 A 9 PHE A 372 THR A 375 1 O PHE A 372 N ALA A 451
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 O TYR A 155 N TYR A 84
SHEET 7 A 9 VAL A 238 ARG 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 ARG A 247
SHEET 9 A 9 LYS A 191 SER A 192 -1 O LYS A 191 N ASP A 227
SHEET 1 B 9 PHE A 479 ASN A 481 0
SHEET 2 B 9 ALA A 451 GLY A 454 1 O VAL A 452 N GLN A 480
SHEET 3 B 9 PHE A 372 THR A 375 1 O PHE A 372 N ALA A 451
SHEET 4 B 9 VAL A 333 ASN A 338 1 O ILE A 335 N ALA A 373
SHEET 5 B 9 ARG A 81 LEU A 85 1 O ARG A 81 N ALA A 334
SHEET 6 B 9 ALA A 154 ILE A 159 1 O TYR A 155 N TYR A 84
SHEET 7 B 9 VAL A 238 ARG A 247 1 O THR A 240 N GLY A 156
SHEET 8 B 9 GLN A 219 PRO A 231 -1 N LEU A 222 O ARG A 247
SHEET 9 B 9 LEU A 198 PHE A 202 -1 O LEU A 198 N ALA A 223
SHEET 1 C 2 PHE A 89 TYR A 90 0
SHEET 2 C 2 GLY A 130 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 TRP A 174 N ARG A 171
SHEET 1 E 2 LYS A 205 THR A 209 0
SHEET 2 E 2 GLY A 212 ILE A 216 -1 N GLY A 212 O THR A 209
SHEET 1 F 3 ARG A 386 PRO A 388 0
SHEET 2 F 3 ARG A 438 ASN A 440 -1 N ILE A 439 O 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 O ARG A 601 N LYS A 641
SHEET 3 G 6 MET A 562 VAL A 567 1 O MET A 562 N THR A 602
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 N PHE A 709 O THR A 688
SHEET 1 H 9 PHE B1479 ASN B1481 0
SHEET 2 H 9 ALA B1451 GLY B1454 1 O VAL B1452 N GLN B1480
SHEET 3 H 9 PHE B1372 THR B1375 1 O PHE B1372 N ALA B1451
SHEET 4 H 9 VAL B1333 ASN B1338 1 O ILE B1335 N ALA B1373
SHEET 5 H 9 ARG B1081 LEU B1085 1 O ARG B1081 N ALA B1334
SHEET 6 H 9 ALA B1154 ILE B1159 1 O TYR B1155 N TYR B1084
SHEET 7 H 9 VAL B1238 ARG B1247 1 O THR B1240 N GLY B1156
SHEET 8 H 9 GLN B1219 PRO B1231 -1 N LEU B1222 O ARG B1247
SHEET 9 H 9 LYS B1191 SER B1192 -1 O LYS B1191 N ASP B1227
SHEET 1 I 9 PHE B1479 ASN B1481 0
SHEET 2 I 9 ALA B1451 GLY B1454 1 O VAL B1452 N GLN B1480
SHEET 3 I 9 PHE B1372 THR B1375 1 O PHE B1372 N ALA B1451
SHEET 4 I 9 VAL B1333 ASN B1338 1 O ILE B1335 N ALA B1373
SHEET 5 I 9 ARG B1081 LEU B1085 1 O ARG B1081 N ALA B1334
SHEET 6 I 9 ALA B1154 ILE B1159 1 O TYR B1155 N TYR B1084
SHEET 7 I 9 VAL B1238 ARG B1247 1 O THR B1240 N GLY B1156
SHEET 8 I 9 GLN B1219 PRO B1231 -1 N LEU B1222 O ARG B1247
SHEET 9 I 9 LEU B1198 PHE B1202 -1 O LEU B1198 N ALA B1223
SHEET 1 J 2 PHE B1089 GLY B1092 0
SHEET 2 J 2 ALA B1129 LEU B1131 -1 O ALA B1129 N GLY B1092
SHEET 1 K 2 ASN B1167 ARG B1171 0
SHEET 2 K 2 TRP B1174 GLU B1178 -1 O TRP B1174 N ARG B1171
SHEET 1 L 2 LYS B1205 HIS B1208 0
SHEET 2 L 2 THR B1213 ILE B1216 -1 N LYS B1214 O GLU B1207
SHEET 1 M 3 ARG B1386 PRO B1388 0
SHEET 2 M 3 ARG B1438 ASN B1440 -1 N ILE B1439 O TRP B1387
SHEET 3 M 3 ILE B1431 GLU B1432 -1 N GLU B1432 O ARG B1438
SHEET 1 N 6 LEU B1640 LEU B1645 0
SHEET 2 N 6 ARG B1601 GLY B1606 1 O ARG B1601 N LYS B1641
SHEET 3 N 6 MET B1562 VAL B1567 1 O MET B1562 N THR B1602
SHEET 4 N 6 LEU B1662 GLN B1665 1 O LEU B1662 N VAL B1565
SHEET 5 N 6 LEU B1687 GLY B1690 1 O LEU B1687 N SER B1663
SHEET 6 N 6 PHE B1709 ILE B1710 1 N PHE B1709 O THR B1688
LINK C4A PLP A 860 NZ LYS A 680 1555 1555 1.47
LINK C4A PLP B1860 NZ LYS B1680 1555 1555 1.44
SITE 1 AC1 14 LEU A 136 ASN A 284 HIS A 377 THR A 378
SITE 2 AC1 14 VAL A 455 ASN A 484 TYR A 573 GLU A 672
SITE 3 AC1 14 ALA A 673 SER A 674 GLY A 675 HOH A2052
SITE 4 AC1 14 HOH A2173 HOH A2225
SITE 1 AC2 17 GLY B1135 LEU B1136 LEU B1139 ASN B1284
SITE 2 AC2 17 ASP B1339 HIS B1377 VAL B1455 ASN B1484
SITE 3 AC2 17 TYR B1573 GLU B1672 ALA B1673 SER B1674
SITE 4 AC2 17 GLY B1675 HOH B2142 HOH B2153 HOH B2207
SITE 5 AC2 17 HOH B2253
SITE 1 AC3 14 TYR A 90 GLY A 135 TRP A 491 LYS A 568
SITE 2 AC3 14 LYS A 574 ARG A 649 VAL A 650 GLY A 675
SITE 3 AC3 14 THR A 676 GLY A 677 LYS A 680 HOH A2014
SITE 4 AC3 14 HOH A2055 HOH A2162
SITE 1 AC4 14 GLY B1134 TRP B1491 LYS B1568 LYS B1574
SITE 2 AC4 14 ARG B1649 VAL B1650 ALA B1653 GLY B1675
SITE 3 AC4 14 THR B1676 GLY B1677 LYS B1680 HOH B2049
SITE 4 AC4 14 HOH B2056 HOH B2239
CRYST1 124.000 124.000 122.280 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 0.008065 0.004656 0.000000 0.00000
SCALE2 0.000000 0.009312 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008178 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
