HEADER TRANSFERASE 29-FEB-08 3CEJ
TITLE HUMAN GLYCOGEN PHOSPHORYLASE (TENSE STATE) IN COMPLEX WITH THE
TITLE 2 ALLOSTERIC INHIBITOR AVE2865
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 GENE: PYGL;
SOURCE 5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 7 EXPRESSION_SYSTEM_CELL_LINE: SF9;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS
KEYWDS PROTEIN LIGAND COMPLEX, TENSE STATE, ALLOSTERIC INHIBITOR, ALLOSTERIC
KEYWDS 2 ENZYME, CARBOHYDRATE METABOLISM, DISEASE MUTATION, GLYCOGEN
KEYWDS 3 METABOLISM, GLYCOGEN STORAGE DISEASE, GLYCOSYLTRANSFERASE,
KEYWDS 4 NUCLEOTIDE-BINDING, PHOSPHOPROTEIN, PYRIDOXAL PHOSPHATE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.U.WENDT,M.K.DREYER,O.ANDERKA,T.KLABUNDE,P.LOENZE,E.DEFOSSA,
AUTHOR 2 D.SCHMOLL
REVDAT 4 13-JUL-11 3CEJ 1 VERSN
REVDAT 3 24-FEB-09 3CEJ 1 VERSN
REVDAT 2 03-JUN-08 3CEJ 1 JRNL
REVDAT 1 27-MAY-08 3CEJ 0
JRNL AUTH O.ANDERKA,P.LOENZE,T.KLABUNDE,M.K.DREYER,E.DEFOSSA,
JRNL AUTH 2 K.U.WENDT,D.SCHMOLL
JRNL TITL THERMODYNAMIC CHARACTERIZATION OF ALLOSTERIC GLYCOGEN
JRNL TITL 2 PHOSPHORYLASE INHIBITORS.
JRNL REF BIOCHEMISTRY V. 47 4683 2008
JRNL REFN ISSN 0006-2960
JRNL PMID 18373353
JRNL DOI 10.1021/BI702397D
REMARK 2
REMARK 2 RESOLUTION. 3.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.47
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 81.2
REMARK 3 NUMBER OF REFLECTIONS : 25212
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 + TEST SET) : 0.181
REMARK 3 R VALUE (WORKING SET) : 0.176
REMARK 3 FREE R VALUE : 0.271
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1257
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.38
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1794
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 82.78
REMARK 3 BIN R VALUE (WORKING SET) : 0.2270
REMARK 3 BIN FREE R VALUE SET COUNT : 91
REMARK 3 BIN FREE R VALUE : 0.3540
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 12830
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 124
REMARK 3 SOLVENT ATOMS : 141
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 56.09
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.04000
REMARK 3 B22 (A**2) : 0.04000
REMARK 3 B33 (A**2) : -0.06000
REMARK 3 B12 (A**2) : 0.02000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.720
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.477
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 28.423
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.925
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.807
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 13250 ; 0.009 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 17932 ; 1.259 ; 1.969
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1574 ; 6.005 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 638 ;38.435 ;24.295
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2360 ;18.882 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 78 ;20.061 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1956 ; 0.081 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 10010 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 8031 ; 0.240 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 9013 ; 0.318 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 656 ; 0.185 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 73 ; 0.248 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 6 ; 0.152 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 8062 ; 0.354 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 12744 ; 0.644 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 5891 ; 0.728 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 5188 ; 1.220 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3CEJ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-MAR-08.
REMARK 100 THE RCSB ID CODE IS RCSB046679.
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 : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
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 : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25212
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.300
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 80.8
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: SINGLE WAVELENGTH
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 (%): 57.18
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.87
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOR DIFFUSION, HANGING DROP, 7 MG/ML
REMARK 280 IN 20 MM BES, 1 MM EDTA, 0.5 MM DTT, PH 6.5, 50 MM NBG, 2.5 MM
REMARK 280 AVF (AVE2865)
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 40.62667
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 81.25333
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: 6910 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 55150 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.7 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 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 THR A 324
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 THR B 324
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 NZ LYS B 680 O4A PLP B 832 1.94
REMARK 500 OG1 THR B 668 O PHE B 771 2.15
REMARK 500 O LYS B 680 N MET B 682 2.18
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 HIS A 62 36.27 -81.16
REMARK 500 LEU A 63 -40.16 -145.96
REMARK 500 CYS A 78 74.64 50.68
REMARK 500 ALA A 129 77.40 -67.77
REMARK 500 ASN A 133 -71.08 -82.23
REMARK 500 MET A 147 -35.55 -35.33
REMARK 500 TYR A 155 -156.00 -132.59
REMARK 500 ASP A 172 41.98 71.06
REMARK 500 ASP A 180 58.59 -94.89
REMARK 500 ASP A 181 54.63 -62.39
REMARK 500 TYR A 203 -152.25 67.11
REMARK 500 THR A 211 39.71 -84.93
REMARK 500 ASN A 235 -0.69 -156.05
REMARK 500 ASN A 236 -14.15 72.36
REMARK 500 ARG A 247 163.13 177.92
REMARK 500 ARG A 277 -72.06 -79.42
REMARK 500 ASN A 284 62.94 29.20
REMARK 500 SER A 314 -154.39 -80.74
REMARK 500 LYS A 315 42.39 -98.34
REMARK 500 ASP A 339 -172.49 64.56
REMARK 500 PHE A 353 -72.31 -79.72
REMARK 500 LYS A 358 36.50 39.86
REMARK 500 TRP A 361 -71.02 -36.66
REMARK 500 VAL A 379 -62.84 -127.86
REMARK 500 LEU A 380 124.73 -34.10
REMARK 500 GLU A 433 39.62 -81.72
REMARK 500 LYS A 457 -57.75 -27.36
REMARK 500 LYS A 464 -75.36 -67.28
REMARK 500 LYS A 466 -70.74 -105.65
REMARK 500 GLU A 475 101.44 -166.92
REMARK 500 ASP A 477 -2.23 -59.79
REMARK 500 ASN A 484 170.66 -55.82
REMARK 500 ILE A 486 114.54 -160.85
REMARK 500 PRO A 488 1.73 -66.70
REMARK 500 ARG A 489 -70.81 -80.49
REMARK 500 LEU A 492 -76.83 -129.43
REMARK 500 GLU A 509 17.33 -144.43
REMARK 500 SER A 516 34.21 -59.51
REMARK 500 LYS A 520 0.69 -63.55
REMARK 500 ASP A 527 112.15 -27.97
REMARK 500 LYS A 554 70.44 -104.60
REMARK 500 LYS A 568 -177.28 176.99
REMARK 500 LYS A 591 -70.26 -65.14
REMARK 500 LYS A 592 -35.95 -37.98
REMARK 500 ASP A 593 102.91 -162.23
REMARK 500 ASN A 647 64.42 34.20
REMARK 500 ALA A 659 49.86 -100.08
REMARK 500 ILE A 666 47.96 -101.13
REMARK 500 ALA A 669 108.76 -50.04
REMARK 500 SER A 674 -48.04 -166.88
REMARK 500
REMARK 500 THIS ENTRY HAS 100 RAMACHANDRAN OUTLIERS.
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 A 894 DISTANCE = 5.69 ANGSTROMS
REMARK 525 HOH B 871 DISTANCE = 5.12 ANGSTROMS
REMARK 525 HOH B 897 DISTANCE = 5.19 ANGSTROMS
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 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NBG B 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP A 832
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP B 832
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AVF A 833
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AVF B 833
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3CEH RELATED DB: PDB
REMARK 900 RELATED ID: 3CEM RELATED DB: PDB
DBREF 3CEJ A 23 831 UNP P06737 PYGL_HUMAN 24 832
DBREF 3CEJ B 23 831 UNP P06737 PYGL_HUMAN 24 832
SEQRES 1 A 809 ASN VAL ALA GLU LEU LYS LYS SER PHE ASN ARG HIS LEU
SEQRES 2 A 809 HIS PHE THR LEU VAL LYS ASP ARG ASN VAL ALA THR THR
SEQRES 3 A 809 ARG ASP TYR TYR PHE ALA LEU ALA HIS THR VAL ARG ASP
SEQRES 4 A 809 HIS LEU VAL GLY ARG TRP ILE ARG THR GLN GLN HIS TYR
SEQRES 5 A 809 TYR ASP LYS CYS PRO LYS ARG VAL TYR TYR LEU SER LEU
SEQRES 6 A 809 GLU PHE TYR MET GLY ARG THR LEU GLN ASN THR MET ILE
SEQRES 7 A 809 ASN LEU GLY LEU GLN ASN ALA CYS ASP GLU ALA ILE TYR
SEQRES 8 A 809 GLN LEU GLY LEU ASP ILE GLU GLU LEU GLU GLU ILE GLU
SEQRES 9 A 809 GLU ASP ALA GLY LEU GLY ASN GLY GLY LEU GLY ARG LEU
SEQRES 10 A 809 ALA ALA CYS PHE LEU ASP SER MET ALA THR LEU GLY LEU
SEQRES 11 A 809 ALA ALA TYR GLY TYR GLY ILE ARG TYR GLU TYR GLY ILE
SEQRES 12 A 809 PHE ASN GLN LYS ILE ARG ASP GLY TRP GLN VAL GLU GLU
SEQRES 13 A 809 ALA ASP ASP TRP LEU ARG TYR GLY ASN PRO TRP GLU LYS
SEQRES 14 A 809 SER ARG PRO GLU PHE MET LEU PRO VAL HIS PHE TYR GLY
SEQRES 15 A 809 LYS VAL GLU HIS THR ASN THR GLY THR LYS TRP ILE ASP
SEQRES 16 A 809 THR GLN VAL VAL LEU ALA LEU PRO TYR ASP THR PRO VAL
SEQRES 17 A 809 PRO GLY TYR MET ASN ASN THR VAL ASN THR MET ARG LEU
SEQRES 18 A 809 TRP SER ALA ARG ALA PRO ASN ASP PHE ASN LEU ARG ASP
SEQRES 19 A 809 PHE ASN VAL GLY ASP TYR ILE GLN ALA VAL LEU ASP ARG
SEQRES 20 A 809 ASN LEU ALA GLU ASN ILE SER ARG VAL LEU TYR PRO ASN
SEQRES 21 A 809 ASP ASN PHE PHE GLU GLY LYS GLU LEU ARG LEU LYS GLN
SEQRES 22 A 809 GLU TYR PHE VAL VAL ALA ALA THR LEU GLN ASP ILE ILE
SEQRES 23 A 809 ARG ARG PHE LYS ALA SER LYS PHE GLY SER THR ARG GLY
SEQRES 24 A 809 ALA GLY THR VAL PHE ASP ALA PHE PRO ASP GLN VAL ALA
SEQRES 25 A 809 ILE GLN LEU ASN ASP THR HIS PRO ALA LEU ALA ILE PRO
SEQRES 26 A 809 GLU LEU MET ARG ILE PHE VAL ASP ILE GLU LYS LEU PRO
SEQRES 27 A 809 TRP SER LYS ALA TRP GLU LEU THR GLN LYS THR PHE ALA
SEQRES 28 A 809 TYR THR ASN HIS THR VAL LEU PRO GLU ALA LEU GLU ARG
SEQRES 29 A 809 TRP PRO VAL ASP LEU VAL GLU LYS LEU LEU PRO ARG HIS
SEQRES 30 A 809 LEU GLU ILE ILE TYR GLU ILE ASN GLN LYS HIS LEU ASP
SEQRES 31 A 809 ARG ILE VAL ALA LEU PHE PRO LYS ASP VAL ASP ARG LEU
SEQRES 32 A 809 ARG ARG MET SER LEU ILE GLU GLU GLU GLY SER LYS ARG
SEQRES 33 A 809 ILE ASN MET ALA HIS LEU CYS ILE VAL GLY SER HIS ALA
SEQRES 34 A 809 VAL ASN GLY VAL ALA LYS ILE HIS SER ASP ILE VAL LYS
SEQRES 35 A 809 THR LYS VAL PHE LYS ASP PHE SER GLU LEU GLU PRO ASP
SEQRES 36 A 809 LYS PHE GLN ASN LYS THR ASN GLY ILE THR PRO ARG ARG
SEQRES 37 A 809 TRP LEU LEU LEU CYS ASN PRO GLY LEU ALA GLU LEU ILE
SEQRES 38 A 809 ALA GLU LYS ILE GLY GLU ASP TYR VAL LYS ASP LEU SER
SEQRES 39 A 809 GLN LEU THR LYS LEU HIS SER PHE LEU GLY ASP ASP VAL
SEQRES 40 A 809 PHE LEU ARG GLU LEU ALA LYS VAL LYS GLN GLU ASN LYS
SEQRES 41 A 809 LEU LYS PHE SER GLN PHE LEU GLU THR GLU TYR LYS VAL
SEQRES 42 A 809 LYS ILE ASN PRO SER SER MET PHE ASP VAL GLN VAL LYS
SEQRES 43 A 809 ARG ILE HIS GLU TYR LYS ARG GLN LEU LEU ASN CYS LEU
SEQRES 44 A 809 HIS VAL ILE THR MET TYR ASN ARG ILE LYS LYS ASP PRO
SEQRES 45 A 809 LYS LYS LEU PHE VAL PRO ARG THR VAL ILE ILE GLY GLY
SEQRES 46 A 809 LYS ALA ALA PRO GLY TYR HIS MET ALA LYS MET ILE ILE
SEQRES 47 A 809 LYS LEU ILE THR SER VAL ALA ASP VAL VAL ASN ASN ASP
SEQRES 48 A 809 PRO MET VAL GLY SER LYS LEU LYS VAL ILE PHE LEU GLU
SEQRES 49 A 809 ASN TYR ARG VAL SER LEU ALA GLU LYS VAL ILE PRO ALA
SEQRES 50 A 809 THR ASP LEU SER GLU GLN ILE SER THR ALA GLY THR GLU
SEQRES 51 A 809 ALA SER GLY THR GLY ASN MET LYS PHE MET LEU ASN GLY
SEQRES 52 A 809 ALA LEU THR ILE GLY THR MET ASP GLY ALA ASN VAL GLU
SEQRES 53 A 809 MET ALA GLU GLU ALA GLY GLU GLU ASN LEU PHE ILE PHE
SEQRES 54 A 809 GLY MET ARG ILE ASP ASP VAL ALA ALA LEU ASP LYS LYS
SEQRES 55 A 809 GLY TYR GLU ALA LYS GLU TYR TYR GLU ALA LEU PRO GLU
SEQRES 56 A 809 LEU LYS LEU VAL ILE ASP GLN ILE ASP ASN GLY PHE PHE
SEQRES 57 A 809 SER PRO LYS GLN PRO ASP LEU PHE LYS ASP ILE ILE ASN
SEQRES 58 A 809 MET LEU PHE TYR HIS ASP ARG PHE LYS VAL PHE ALA ASP
SEQRES 59 A 809 TYR GLU ALA TYR VAL LYS CYS GLN ASP LYS VAL SER GLN
SEQRES 60 A 809 LEU TYR MET ASN PRO LYS ALA TRP ASN THR MET VAL LEU
SEQRES 61 A 809 LYS ASN ILE ALA ALA SER GLY LYS PHE SER SER ASP ARG
SEQRES 62 A 809 THR ILE LYS GLU TYR ALA GLN ASN ILE TRP ASN VAL GLU
SEQRES 63 A 809 PRO SER ASP
SEQRES 1 B 809 ASN VAL ALA GLU LEU LYS LYS SER PHE ASN ARG HIS LEU
SEQRES 2 B 809 HIS PHE THR LEU VAL LYS ASP ARG ASN VAL ALA THR THR
SEQRES 3 B 809 ARG ASP TYR TYR PHE ALA LEU ALA HIS THR VAL ARG ASP
SEQRES 4 B 809 HIS LEU VAL GLY ARG TRP ILE ARG THR GLN GLN HIS TYR
SEQRES 5 B 809 TYR ASP LYS CYS PRO LYS ARG VAL TYR TYR LEU SER LEU
SEQRES 6 B 809 GLU PHE TYR MET GLY ARG THR LEU GLN ASN THR MET ILE
SEQRES 7 B 809 ASN LEU GLY LEU GLN ASN ALA CYS ASP GLU ALA ILE TYR
SEQRES 8 B 809 GLN LEU GLY LEU ASP ILE GLU GLU LEU GLU GLU ILE GLU
SEQRES 9 B 809 GLU ASP ALA GLY LEU GLY ASN GLY GLY LEU GLY ARG LEU
SEQRES 10 B 809 ALA ALA CYS PHE LEU ASP SER MET ALA THR LEU GLY LEU
SEQRES 11 B 809 ALA ALA TYR GLY TYR GLY ILE ARG TYR GLU TYR GLY ILE
SEQRES 12 B 809 PHE ASN GLN LYS ILE ARG ASP GLY TRP GLN VAL GLU GLU
SEQRES 13 B 809 ALA ASP ASP TRP LEU ARG TYR GLY ASN PRO TRP GLU LYS
SEQRES 14 B 809 SER ARG PRO GLU PHE MET LEU PRO VAL HIS PHE TYR GLY
SEQRES 15 B 809 LYS VAL GLU HIS THR ASN THR GLY THR LYS TRP ILE ASP
SEQRES 16 B 809 THR GLN VAL VAL LEU ALA LEU PRO TYR ASP THR PRO VAL
SEQRES 17 B 809 PRO GLY TYR MET ASN ASN THR VAL ASN THR MET ARG LEU
SEQRES 18 B 809 TRP SER ALA ARG ALA PRO ASN ASP PHE ASN LEU ARG ASP
SEQRES 19 B 809 PHE ASN VAL GLY ASP TYR ILE GLN ALA VAL LEU ASP ARG
SEQRES 20 B 809 ASN LEU ALA GLU ASN ILE SER ARG VAL LEU TYR PRO ASN
SEQRES 21 B 809 ASP ASN PHE PHE GLU GLY LYS GLU LEU ARG LEU LYS GLN
SEQRES 22 B 809 GLU TYR PHE VAL VAL ALA ALA THR LEU GLN ASP ILE ILE
SEQRES 23 B 809 ARG ARG PHE LYS ALA SER LYS PHE GLY SER THR ARG GLY
SEQRES 24 B 809 ALA GLY THR VAL PHE ASP ALA PHE PRO ASP GLN VAL ALA
SEQRES 25 B 809 ILE GLN LEU ASN ASP THR HIS PRO ALA LEU ALA ILE PRO
SEQRES 26 B 809 GLU LEU MET ARG ILE PHE VAL ASP ILE GLU LYS LEU PRO
SEQRES 27 B 809 TRP SER LYS ALA TRP GLU LEU THR GLN LYS THR PHE ALA
SEQRES 28 B 809 TYR THR ASN HIS THR VAL LEU PRO GLU ALA LEU GLU ARG
SEQRES 29 B 809 TRP PRO VAL ASP LEU VAL GLU LYS LEU LEU PRO ARG HIS
SEQRES 30 B 809 LEU GLU ILE ILE TYR GLU ILE ASN GLN LYS HIS LEU ASP
SEQRES 31 B 809 ARG ILE VAL ALA LEU PHE PRO LYS ASP VAL ASP ARG LEU
SEQRES 32 B 809 ARG ARG MET SER LEU ILE GLU GLU GLU GLY SER LYS ARG
SEQRES 33 B 809 ILE ASN MET ALA HIS LEU CYS ILE VAL GLY SER HIS ALA
SEQRES 34 B 809 VAL ASN GLY VAL ALA LYS ILE HIS SER ASP ILE VAL LYS
SEQRES 35 B 809 THR LYS VAL PHE LYS ASP PHE SER GLU LEU GLU PRO ASP
SEQRES 36 B 809 LYS PHE GLN ASN LYS THR ASN GLY ILE THR PRO ARG ARG
SEQRES 37 B 809 TRP LEU LEU LEU CYS ASN PRO GLY LEU ALA GLU LEU ILE
SEQRES 38 B 809 ALA GLU LYS ILE GLY GLU ASP TYR VAL LYS ASP LEU SER
SEQRES 39 B 809 GLN LEU THR LYS LEU HIS SER PHE LEU GLY ASP ASP VAL
SEQRES 40 B 809 PHE LEU ARG GLU LEU ALA LYS VAL LYS GLN GLU ASN LYS
SEQRES 41 B 809 LEU LYS PHE SER GLN PHE LEU GLU THR GLU TYR LYS VAL
SEQRES 42 B 809 LYS ILE ASN PRO SER SER MET PHE ASP VAL GLN VAL LYS
SEQRES 43 B 809 ARG ILE HIS GLU TYR LYS ARG GLN LEU LEU ASN CYS LEU
SEQRES 44 B 809 HIS VAL ILE THR MET TYR ASN ARG ILE LYS LYS ASP PRO
SEQRES 45 B 809 LYS LYS LEU PHE VAL PRO ARG THR VAL ILE ILE GLY GLY
SEQRES 46 B 809 LYS ALA ALA PRO GLY TYR HIS MET ALA LYS MET ILE ILE
SEQRES 47 B 809 LYS LEU ILE THR SER VAL ALA ASP VAL VAL ASN ASN ASP
SEQRES 48 B 809 PRO MET VAL GLY SER LYS LEU LYS VAL ILE PHE LEU GLU
SEQRES 49 B 809 ASN TYR ARG VAL SER LEU ALA GLU LYS VAL ILE PRO ALA
SEQRES 50 B 809 THR ASP LEU SER GLU GLN ILE SER THR ALA GLY THR GLU
SEQRES 51 B 809 ALA SER GLY THR GLY ASN MET LYS PHE MET LEU ASN GLY
SEQRES 52 B 809 ALA LEU THR ILE GLY THR MET ASP GLY ALA ASN VAL GLU
SEQRES 53 B 809 MET ALA GLU GLU ALA GLY GLU GLU ASN LEU PHE ILE PHE
SEQRES 54 B 809 GLY MET ARG ILE ASP ASP VAL ALA ALA LEU ASP LYS LYS
SEQRES 55 B 809 GLY TYR GLU ALA LYS GLU TYR TYR GLU ALA LEU PRO GLU
SEQRES 56 B 809 LEU LYS LEU VAL ILE ASP GLN ILE ASP ASN GLY PHE PHE
SEQRES 57 B 809 SER PRO LYS GLN PRO ASP LEU PHE LYS ASP ILE ILE ASN
SEQRES 58 B 809 MET LEU PHE TYR HIS ASP ARG PHE LYS VAL PHE ALA ASP
SEQRES 59 B 809 TYR GLU ALA TYR VAL LYS CYS GLN ASP LYS VAL SER GLN
SEQRES 60 B 809 LEU TYR MET ASN PRO LYS ALA TRP ASN THR MET VAL LEU
SEQRES 61 B 809 LYS ASN ILE ALA ALA SER GLY LYS PHE SER SER ASP ARG
SEQRES 62 B 809 THR ILE LYS GLU TYR ALA GLN ASN ILE TRP ASN VAL GLU
SEQRES 63 B 809 PRO SER ASP
HET NBG A 1 15
HET NBG B 2 15
HET PLP A 832 16
HET AVF A 833 31
HET PLP B 832 16
HET AVF B 833 31
HETNAM NBG 1-N-ACETYL-BETA-D-GLUCOSAMINE
HETNAM PLP PYRIDOXAL-5'-PHOSPHATE
HETNAM AVF 1-{2-[3-(2-CHLORO-4,5-DIFLUORO-BENZOYL)-UREIDO]-4-
HETNAM 2 AVF FLUORO-PHENYL}-PIPERIDINE-4-CARBOXYLIC ACID
HETSYN PLP VITAMIN B6 PHOSPHATE
HETSYN AVF 1-[2-({[(2-CHLORO-4,5-DIFLUOROPHENYL)
HETSYN 2 AVF CARBONYL]CARBAMOYL}AMINO)-4-FLUOROPHENYL]PIPERIDINE-4-
HETSYN 3 AVF CARBOXYLIC ACID
FORMUL 3 NBG 2(C8 H15 N O6)
FORMUL 5 PLP 2(C8 H10 N O6 P)
FORMUL 6 AVF 2(C20 H17 CL F3 N3 O4)
FORMUL 9 HOH *141(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 LEU A 102 1 9
HELIX 4 4 LEU A 104 LEU A 115 1 12
HELIX 5 5 ASP A 118 GLU A 126 1 9
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 ALA A 272 5 4
HELIX 10 10 LYS A 289 SER A 314 1 26
HELIX 11 11 ALA A 328 GLN A 332 1 5
HELIX 12 12 LEU A 344 ASP A 355 1 12
HELIX 13 13 PRO A 360 THR A 371 1 12
HELIX 14 14 LEU A 380 LEU A 384 5 5
HELIX 15 15 VAL A 389 LEU A 396 1 8
HELIX 16 16 LEU A 396 PHE A 418 1 23
HELIX 17 17 ARG A 424 SER A 429 1 6
HELIX 18 18 MET A 441 SER A 449 1 9
HELIX 19 19 ALA A 456 LYS A 466 1 11
HELIX 20 20 PHE A 468 GLU A 475 1 8
HELIX 21 21 ASN A 496 ILE A 507 1 12
HELIX 22 22 GLU A 509 LYS A 513 5 5
HELIX 23 23 GLN A 517 LEU A 525 5 9
HELIX 24 24 ASP A 527 TYR A 553 1 27
HELIX 25 25 ARG A 575 ASP A 593 1 19
HELIX 26 26 TYR A 613 ASP A 633 1 21
HELIX 27 27 VAL A 636 SER A 638 5 3
HELIX 28 28 ARG A 649 ILE A 657 1 9
HELIX 29 29 PRO A 658 THR A 660 5 3
HELIX 30 30 THR A 676 LEU A 683 1 8
HELIX 31 31 ALA A 695 GLY A 704 1 10
HELIX 32 32 ARG A 714 GLY A 725 1 12
HELIX 33 33 ALA A 728 ALA A 734 1 7
HELIX 34 34 LEU A 735 GLY A 748 1 14
HELIX 35 35 PHE A 758 HIS A 768 1 11
HELIX 36 36 ASP A 776 ASN A 793 1 18
HELIX 37 37 ASN A 793 ALA A 807 1 15
HELIX 38 38 SER A 808 PHE A 811 5 4
HELIX 39 39 SER A 812 ILE A 824 1 13
HELIX 40 40 ASN B 23 THR B 38 1 16
HELIX 41 41 THR B 47 CYS B 78 1 32
HELIX 42 42 THR B 94 LEU B 102 1 9
HELIX 43 43 LEU B 104 LEU B 115 1 12
HELIX 44 44 ASP B 118 GLU B 126 1 9
HELIX 45 45 GLY B 134 LEU B 150 1 17
HELIX 46 46 ASP B 261 ASN B 274 1 14
HELIX 47 47 LYS B 289 SER B 314 1 26
HELIX 48 48 ALA B 328 GLN B 332 1 5
HELIX 49 49 THR B 340 ALA B 343 5 4
HELIX 50 50 LEU B 344 ASP B 355 1 12
HELIX 51 51 PRO B 360 THR B 371 1 12
HELIX 52 52 VAL B 389 LEU B 396 1 8
HELIX 53 53 LEU B 396 PHE B 418 1 23
HELIX 54 54 ASP B 421 MET B 428 1 8
HELIX 55 55 MET B 441 SER B 449 1 9
HELIX 56 56 ALA B 456 LYS B 466 1 11
HELIX 57 57 PHE B 468 GLU B 473 1 6
HELIX 58 58 GLU B 475 ASP B 477 5 3
HELIX 59 59 ASN B 496 ILE B 507 1 12
HELIX 60 60 ASP B 514 LEU B 525 5 12
HELIX 61 61 ASP B 527 TYR B 553 1 27
HELIX 62 62 HIS B 571 LYS B 574 5 4
HELIX 63 63 ARG B 575 LYS B 592 1 18
HELIX 64 64 TYR B 613 ASP B 633 1 21
HELIX 65 65 ARG B 649 ILE B 657 1 9
HELIX 66 66 PRO B 658 THR B 660 5 3
HELIX 67 67 THR B 676 LEU B 683 1 8
HELIX 68 68 ALA B 695 GLY B 704 1 10
HELIX 69 69 GLU B 705 LEU B 708 5 4
HELIX 70 70 ARG B 714 GLY B 725 1 12
HELIX 71 71 ALA B 728 GLU B 733 1 6
HELIX 72 72 LEU B 735 GLY B 748 1 14
HELIX 73 73 PHE B 758 HIS B 768 1 11
HELIX 74 74 ASP B 776 MET B 792 1 17
HELIX 75 75 ASN B 793 SER B 808 1 16
HELIX 76 76 GLY B 809 PHE B 811 5 3
HELIX 77 77 SER B 812 ILE B 824 1 13
SHEET 1 A 5 ARG A 81 LEU A 85 0
SHEET 2 A 5 VAL A 333 ASN A 338 1 O GLN A 336 N TYR A 83
SHEET 3 A 5 PHE A 372 ASN A 376 1 O ALA A 373 N LEU A 337
SHEET 4 A 5 VAL A 452 GLY A 454 1 O ASN A 453 N ASN A 376
SHEET 5 A 5 PHE A 479 ASN A 481 1 O GLN A 480 N VAL A 452
SHEET 1 B 2 PHE A 89 GLY A 92 0
SHEET 2 B 2 ALA A 129 LEU A 131 -1 O LEU A 131 N PHE A 89
SHEET 1 C 4 TYR A 157 ILE A 159 0
SHEET 2 C 4 VAL A 238 ARG A 247 1 O ARG A 242 N GLY A 158
SHEET 3 C 4 GLN A 219 PRO A 231 -1 N TYR A 226 O LEU A 243
SHEET 4 C 4 LYS A 191 SER A 192 -1 N LYS A 191 O ASP A 227
SHEET 1 D 4 TYR A 157 ILE A 159 0
SHEET 2 D 4 VAL A 238 ARG A 247 1 O ARG A 242 N GLY A 158
SHEET 3 D 4 GLN A 219 PRO A 231 -1 N TYR A 226 O LEU A 243
SHEET 4 D 4 LEU A 198 PHE A 202 -1 N LEU A 198 O ALA A 223
SHEET 1 E 2 ASN A 167 ILE A 170 0
SHEET 2 E 2 GLN A 175 GLU A 178 -1 O VAL A 176 N LYS A 169
SHEET 1 F 2 GLU A 207 THR A 209 0
SHEET 2 F 2 GLY A 212 LYS A 214 -1 O LYS A 214 N GLU A 207
SHEET 1 G 3 ARG A 386 PRO A 388 0
SHEET 2 G 3 ARG A 438 ASN A 440 -1 O ILE A 439 N TRP A 387
SHEET 3 G 3 ILE A 431 GLU A 432 -1 N GLU A 432 O ARG A 438
SHEET 1 H 6 LEU A 640 LEU A 645 0
SHEET 2 H 6 ARG A 601 GLY A 606 1 N VAL A 603 O ILE A 643
SHEET 3 H 6 MET A 562 VAL A 567 1 N GLN A 566 O ILE A 604
SHEET 4 H 6 LEU A 662 GLN A 665 1 O LEU A 662 N PHE A 563
SHEET 5 H 6 LEU A 687 GLY A 690 1 O LEU A 687 N SER A 663
SHEET 6 H 6 PHE A 709 ILE A 710 1 O PHE A 709 N THR A 688
SHEET 1 I 3 LYS B 191 SER B 192 0
SHEET 2 I 3 GLN B 219 PRO B 231 -1 O ASP B 227 N LYS B 191
SHEET 3 I 3 LEU B 198 PHE B 202 -1 N PHE B 202 O GLN B 219
SHEET 1 J 9 LYS B 191 SER B 192 0
SHEET 2 J 9 GLN B 219 PRO B 231 -1 O ASP B 227 N LYS B 191
SHEET 3 J 9 VAL B 238 ARG B 247 -1 O LEU B 243 N TYR B 226
SHEET 4 J 9 ALA B 154 ILE B 159 1 N GLY B 156 O ARG B 242
SHEET 5 J 9 ARG B 81 LEU B 85 1 N VAL B 82 O TYR B 155
SHEET 6 J 9 VAL B 333 ASN B 338 1 O ALA B 334 N TYR B 83
SHEET 7 J 9 PHE B 372 THR B 375 1 O ALA B 373 N LEU B 337
SHEET 8 J 9 VAL B 452 GLY B 454 1 O ASN B 453 N TYR B 374
SHEET 9 J 9 PHE B 479 ASN B 481 1 O GLN B 480 N VAL B 452
SHEET 1 K 2 PHE B 89 TYR B 90 0
SHEET 2 K 2 GLY B 130 LEU B 131 -1 O LEU B 131 N PHE B 89
SHEET 1 L 2 ASN B 167 ARG B 171 0
SHEET 2 L 2 TRP B 174 GLU B 178 -1 O GLU B 178 N ASN B 167
SHEET 1 M 2 LYS B 205 THR B 209 0
SHEET 2 M 2 GLY B 212 ILE B 216 -1 O LYS B 214 N GLU B 207
SHEET 1 N 3 ARG B 386 PRO B 388 0
SHEET 2 N 3 ARG B 438 ASN B 440 -1 O ILE B 439 N TRP B 387
SHEET 3 N 3 ILE B 431 GLU B 432 -1 N GLU B 432 O ARG B 438
SHEET 1 O 6 LEU B 640 LEU B 645 0
SHEET 2 O 6 ARG B 601 GLY B 606 1 N ILE B 605 O LEU B 645
SHEET 3 O 6 MET B 562 VAL B 567 1 N ASP B 564 O ILE B 604
SHEET 4 O 6 LEU B 662 GLN B 665 1 O LEU B 662 N PHE B 563
SHEET 5 O 6 LEU B 687 THR B 691 1 O ILE B 689 N GLN B 665
SHEET 6 O 6 PHE B 709 PHE B 711 1 O PHE B 709 N GLY B 690
LINK NZ LYS A 680 C4A PLP A 832 1555 1555 1.85
LINK NZ LYS B 680 C4A PLP B 832 1555 1555 1.49
SITE 1 AC1 12 LEU A 136 LEU A 139 ASN A 284 HIS A 377
SITE 2 AC1 12 THR A 378 ASN A 484 TYR A 573 GLU A 672
SITE 3 AC1 12 ALA A 673 SER A 674 GLY A 675 THR A 676
SITE 1 AC2 9 LEU B 136 ASN B 284 HIS B 377 ASN B 484
SITE 2 AC2 9 TYR B 573 GLU B 672 ALA B 673 SER B 674
SITE 3 AC2 9 GLY B 675
SITE 1 AC3 11 GLY A 135 TRP A 491 LYS A 568 LYS A 574
SITE 2 AC3 11 TYR A 648 ARG A 649 GLY A 675 THR A 676
SITE 3 AC3 11 GLY A 677 ASN A 678 LYS A 680
SITE 1 AC4 9 GLY B 135 LYS B 568 LYS B 574 TYR B 648
SITE 2 AC4 9 ARG B 649 ALA B 653 THR B 676 GLY B 677
SITE 3 AC4 9 LYS B 680
SITE 1 AC5 12 TRP A 67 ILE A 68 GLN A 71 GLN A 72
SITE 2 AC5 12 LYS A 191 ARG A 193 ARG A 309 ARG A 310
SITE 3 AC5 12 LEU B 39 LYS B 41 ASP B 42 ASN B 44
SITE 1 AC6 12 LEU A 39 LYS A 41 ASP A 42 ASN A 44
SITE 2 AC6 12 TRP B 67 ILE B 68 GLN B 71 GLN B 72
SITE 3 AC6 12 LYS B 191 ARG B 193 PHE B 196 ARG B 310
CRYST1 123.270 123.270 121.880 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 0.008112 0.004684 0.000000 0.00000
SCALE2 0.000000 0.009367 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008205 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
