HEADER TRANSFERASE 06-JUN-08 3DDS
TITLE CRYSTAL STRUCTURE OF GLYCOGEN PHOSPHORYLASE COMPLEXED WITH AN
TITLE 2 ANTHRANILIMIDE BASED INHIBITOR GSK261
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_TAXID: 9606;
SOURCE 4 TISSUE: LIVER ISOFORM;
SOURCE 5 GENE: PYGL;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: T7 PROMOTER
KEYWDS GP, GLYCOGEN PHOSPHORYLASE, DIABETES, ALLOSTERIC ENZYME, CARBOHYDRATE
KEYWDS 2 METABOLISM, DISEASE MUTATION, GLYCOGEN METABOLISM, GLYCOGEN STORAGE
KEYWDS 3 DISEASE, GLYCOSYLTRANSFERASE, NUCLEOTIDE-BINDING, PHOSPHOPROTEIN,
KEYWDS 4 PYRIDOXAL PHOSPHATE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.T.NOLTE
REVDAT 3 13-JUL-11 3DDS 1 VERSN
REVDAT 2 03-MAR-09 3DDS 1 JRNL
REVDAT 1 27-JAN-09 3DDS 0
JRNL AUTH S.A.THOMSON,P.BANKER,D.M.BICKETT,J.A.BOUCHERON,H.L.CARTER,
JRNL AUTH 2 D.C.CLANCY,J.P.COOPER,S.H.DICKERSON,D.M.GARRIDO,R.T.NOLTE,
JRNL AUTH 3 A.J.PEAT,L.R.SHECKLER,S.M.SPARKS,F.X.TAVARES,L.WANG,
JRNL AUTH 4 T.Y.WANG,J.E.WEIEL
JRNL TITL ANTHRANILIMIDE BASED GLYCOGEN PHOSPHORYLASE INHIBITORS FOR
JRNL TITL 2 THE TREATMENT OF TYPE 2 DIABETES. PART 3: X-RAY
JRNL TITL 3 CRYSTALLOGRAPHIC CHARACTERIZATION, CORE AND UREA
JRNL TITL 4 OPTIMIZATION AND IN VIVO EFFICACY.
JRNL REF BIOORG.MED.CHEM.LETT. V. 19 1177 2009
JRNL REFN ISSN 0960-894X
JRNL PMID 19138846
JRNL DOI 10.1016/J.BMCL.2008.12.085
REMARK 2
REMARK 2 RESOLUTION. 1.80 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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.66
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 3 NUMBER OF REFLECTIONS : 186135
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) : 0.175
REMARK 3 R VALUE (WORKING SET) : 0.174
REMARK 3 FREE R VALUE : 0.198
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5803
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) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.85
REMARK 3 REFLECTION IN BIN (WORKING SET) : 13498
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.60
REMARK 3 BIN R VALUE (WORKING SET) : 0.2520
REMARK 3 BIN FREE R VALUE SET COUNT : 436
REMARK 3 BIN FREE R VALUE : 0.2710
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 13003
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 224
REMARK 3 SOLVENT ATOMS : 1353
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 20.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.02
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.21000
REMARK 3 B22 (A**2) : -0.21000
REMARK 3 B33 (A**2) : 0.31000
REMARK 3 B12 (A**2) : -0.10000
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): 0.109
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.102
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.073
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.334
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.966
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.956
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 13659 ; 0.007 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 9226 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 18535 ; 1.113 ; 1.976
REMARK 3 BOND ANGLES OTHERS (DEGREES): 22479 ; 0.842 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1640 ; 5.469 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 651 ;34.990 ;24.363
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2382 ;11.917 ;15.006
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 79 ;14.066 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2013 ; 0.061 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 15219 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 2806 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2786 ; 0.204 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 9697 ; 0.179 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 6702 ; 0.178 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 6463 ; 0.081 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 1104 ; 0.117 ; 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): 21 ; 0.177 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 52 ; 0.254 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 44 ; 0.139 ; 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): 8535 ; 0.570 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3288 ; 0.099 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 13167 ; 0.903 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 6153 ; 1.295 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 5365 ; 1.967 ; 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 : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3DDS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-JUN-08.
REMARK 100 THE RCSB ID CODE IS RCSB047912.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-AUG-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 17-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00000
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 190798
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.8
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : 0.08700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.86
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.5
REMARK 200 DATA REDUNDANCY IN SHELL : 2.60
REMARK 200 R MERGE FOR SHELL (I) : 0.48800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.500
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: PDB ENTRY 1EM6
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.64
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.84
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 12-25% MPD, 0.1M MES BUFFER PH 6.0,
REMARK 280 5MM CAFFEINE, 30MM GLCNAC, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
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 41.20467
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 82.40933
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 ACTIVE FORM IS A DIMER, AS SEEN IN THE ASYMMETRIC UNIT
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: 5020 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 58010 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.7 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 GLY A -1
REMARK 465 GLY A 0
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 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 ASP A 831
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 GLY B -1
REMARK 465 GLY B 0
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 SEP 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 PHE B 257
REMARK 465 ASN B 258
REMARK 465 VAL B 259
REMARK 465 ARG B 320
REMARK 465 GLY B 321
REMARK 465 ALA B 322
REMARK 465 ASP B 831
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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 420 CG CD CE NZ
REMARK 470 ARG A 532 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 595 CD CE NZ
REMARK 470 MET A 635 CG SD CE
REMARK 470 LYS A 723 CE NZ
REMARK 470 LYS A 724 CG CD CE NZ
REMARK 470 LYS A 759 CG CD CE NZ
REMARK 470 ARG B 171 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 255 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 420 CG CD CE NZ
REMARK 470 LYS B 466 CD CE NZ
REMARK 470 LYS B 554 CG CD CE NZ
REMARK 470 LYS B 595 CG CD CE NZ
REMARK 470 LYS B 723 CD CE NZ
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 OD1 ASN B 106 O HOH B 1591 1.91
REMARK 500 NE2 GLN A 547 O HOH A 1229 2.05
REMARK 500 NE2 HIS B 522 O HOH B 1094 2.11
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 39.19 -90.23
REMARK 500 TYR A 203 -133.13 61.67
REMARK 500 PRO A 281 30.69 -86.24
REMARK 500 ASP A 339 -169.54 69.39
REMARK 500 ARG A 489 -73.44 -70.39
REMARK 500 LEU A 492 -62.34 -146.81
REMARK 500 LYS A 568 167.03 171.99
REMARK 500 SER A 674 -59.74 -139.33
REMARK 500 HIS A 768 31.88 -141.04
REMARK 500 ILE A 824 -54.38 -126.74
REMARK 500 LEU B 131 44.08 -93.19
REMARK 500 TYR B 203 -137.35 60.90
REMARK 500 PRO B 281 35.06 -87.07
REMARK 500 ASP B 339 -170.59 67.79
REMARK 500 ARG B 489 -74.10 -71.22
REMARK 500 LEU B 492 -64.68 -145.67
REMARK 500 LYS B 568 165.97 172.01
REMARK 500 SER B 674 -60.76 -141.18
REMARK 500 SER B 751 60.66 -151.04
REMARK 500 HIS B 768 35.10 -146.88
REMARK 500 ILE B 824 -55.80 -125.58
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 B1583 DISTANCE = 5.17 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 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NBG B 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP A 903
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP B 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CFF A 904
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CFF B 903
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES B 904
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 26B B 905
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 26B A 905
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 26B B 906
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 906
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3DD1 RELATED DB: PDB
REMARK 900 SAME PROTEIN IN COMPLEX WITH RELATED LIGAND
REMARK 900 RELATED ID: 3DDW RELATED DB: PDB
REMARK 900 SAME PROTEIN IN COMPLEX WITH RELATED LIGAND
DBREF 3DDS A 1 846 UNP P06737 PYGL_HUMAN 2 847
DBREF 3DDS B 1 846 UNP P06737 PYGL_HUMAN 2 847
SEQADV 3DDS GLY A -1 UNP P06737 EXPRESSION TAG
SEQADV 3DDS GLY A 0 UNP P06737 EXPRESSION TAG
SEQADV 3DDS GLY B -1 UNP P06737 EXPRESSION TAG
SEQADV 3DDS GLY B 0 UNP P06737 EXPRESSION TAG
SEQRES 1 A 848 GLY GLY ALA LYS PRO LEU THR ASP GLN GLU LYS ARG ARG
SEQRES 2 A 848 GLN ILE SEP ILE ARG GLY ILE VAL GLY VAL GLU ASN VAL
SEQRES 3 A 848 ALA GLU LEU LYS LYS SER PHE ASN ARG HIS LEU HIS PHE
SEQRES 4 A 848 THR LEU VAL LYS ASP ARG ASN VAL ALA THR THR ARG ASP
SEQRES 5 A 848 TYR TYR PHE ALA LEU ALA HIS THR VAL ARG ASP HIS LEU
SEQRES 6 A 848 VAL GLY ARG TRP ILE ARG THR GLN GLN HIS TYR TYR ASP
SEQRES 7 A 848 LYS CYS PRO LYS ARG VAL TYR TYR LEU SER LEU GLU PHE
SEQRES 8 A 848 TYR MET GLY ARG THR LEU GLN ASN THR MET ILE ASN LEU
SEQRES 9 A 848 GLY LEU GLN ASN ALA CYS ASP GLU ALA ILE TYR GLN LEU
SEQRES 10 A 848 GLY LEU ASP ILE GLU GLU LEU GLU GLU ILE GLU GLU ASP
SEQRES 11 A 848 ALA GLY LEU GLY ASN GLY GLY LEU GLY ARG LEU ALA ALA
SEQRES 12 A 848 CYS PHE LEU ASP SER MET ALA THR LEU GLY LEU ALA ALA
SEQRES 13 A 848 TYR GLY TYR GLY ILE ARG TYR GLU TYR GLY ILE PHE ASN
SEQRES 14 A 848 GLN LYS ILE ARG ASP GLY TRP GLN VAL GLU GLU ALA ASP
SEQRES 15 A 848 ASP TRP LEU ARG TYR GLY ASN PRO TRP GLU LYS SER ARG
SEQRES 16 A 848 PRO GLU PHE MET LEU PRO VAL HIS PHE TYR GLY LYS VAL
SEQRES 17 A 848 GLU HIS THR ASN THR GLY THR LYS TRP ILE ASP THR GLN
SEQRES 18 A 848 VAL VAL LEU ALA LEU PRO TYR ASP THR PRO VAL PRO GLY
SEQRES 19 A 848 TYR MET ASN ASN THR VAL ASN THR MET ARG LEU TRP SER
SEQRES 20 A 848 ALA ARG ALA PRO ASN ASP PHE ASN LEU ARG ASP PHE ASN
SEQRES 21 A 848 VAL GLY ASP TYR ILE GLN ALA VAL LEU ASP ARG ASN LEU
SEQRES 22 A 848 ALA GLU ASN ILE SER ARG VAL LEU TYR PRO ASN ASP ASN
SEQRES 23 A 848 PHE PHE GLU GLY LYS GLU LEU ARG LEU LYS GLN GLU TYR
SEQRES 24 A 848 PHE VAL VAL ALA ALA THR LEU GLN ASP ILE ILE ARG ARG
SEQRES 25 A 848 PHE LYS ALA SER LYS PHE GLY SER THR ARG GLY ALA GLY
SEQRES 26 A 848 THR VAL PHE ASP ALA PHE PRO ASP GLN VAL ALA ILE GLN
SEQRES 27 A 848 LEU ASN ASP THR HIS PRO ALA LEU ALA ILE PRO GLU LEU
SEQRES 28 A 848 MET ARG ILE PHE VAL ASP ILE GLU LYS LEU PRO TRP SER
SEQRES 29 A 848 LYS ALA TRP GLU LEU THR GLN LYS THR PHE ALA TYR THR
SEQRES 30 A 848 ASN HIS THR VAL LEU PRO GLU ALA LEU GLU ARG TRP PRO
SEQRES 31 A 848 VAL ASP LEU VAL GLU LYS LEU LEU PRO ARG HIS LEU GLU
SEQRES 32 A 848 ILE ILE TYR GLU ILE ASN GLN LYS HIS LEU ASP ARG ILE
SEQRES 33 A 848 VAL ALA LEU PHE PRO LYS ASP VAL ASP ARG LEU ARG ARG
SEQRES 34 A 848 MET SER LEU ILE GLU GLU GLU GLY SER LYS ARG ILE ASN
SEQRES 35 A 848 MET ALA HIS LEU CYS ILE VAL GLY SER HIS ALA VAL ASN
SEQRES 36 A 848 GLY VAL ALA LYS ILE HIS SER ASP ILE VAL LYS THR LYS
SEQRES 37 A 848 VAL PHE LYS ASP PHE SER GLU LEU GLU PRO ASP LYS PHE
SEQRES 38 A 848 GLN ASN LYS THR ASN GLY ILE THR PRO ARG ARG TRP LEU
SEQRES 39 A 848 LEU LEU CYS ASN PRO GLY LEU ALA GLU LEU ILE ALA GLU
SEQRES 40 A 848 LYS ILE GLY GLU ASP TYR VAL LYS ASP LEU SER GLN LEU
SEQRES 41 A 848 THR LYS LEU HIS SER PHE LEU GLY ASP ASP VAL PHE LEU
SEQRES 42 A 848 ARG GLU LEU ALA LYS VAL LYS GLN GLU ASN LYS LEU LYS
SEQRES 43 A 848 PHE SER GLN PHE LEU GLU THR GLU TYR LYS VAL LYS ILE
SEQRES 44 A 848 ASN PRO SER SER MET PHE ASP VAL GLN VAL LYS ARG ILE
SEQRES 45 A 848 HIS GLU TYR LYS ARG GLN LEU LEU ASN CYS LEU HIS VAL
SEQRES 46 A 848 ILE THR MET TYR ASN ARG ILE LYS LYS ASP PRO LYS LYS
SEQRES 47 A 848 LEU PHE VAL PRO ARG THR VAL ILE ILE GLY GLY LYS ALA
SEQRES 48 A 848 ALA PRO GLY TYR HIS MET ALA LYS MET ILE ILE LYS LEU
SEQRES 49 A 848 ILE THR SER VAL ALA ASP VAL VAL ASN ASN ASP PRO MET
SEQRES 50 A 848 VAL GLY SER LYS LEU LYS VAL ILE PHE LEU GLU ASN TYR
SEQRES 51 A 848 ARG VAL SER LEU ALA GLU LYS VAL ILE PRO ALA THR ASP
SEQRES 52 A 848 LEU SER GLU GLN ILE SER THR ALA GLY THR GLU ALA SER
SEQRES 53 A 848 GLY THR GLY ASN MET LYS PHE MET LEU ASN GLY ALA LEU
SEQRES 54 A 848 THR ILE GLY THR MET ASP GLY ALA ASN VAL GLU MET ALA
SEQRES 55 A 848 GLU GLU ALA GLY GLU GLU ASN LEU PHE ILE PHE GLY MET
SEQRES 56 A 848 ARG ILE ASP ASP VAL ALA ALA LEU ASP LYS LYS GLY TYR
SEQRES 57 A 848 GLU ALA LYS GLU TYR TYR GLU ALA LEU PRO GLU LEU LYS
SEQRES 58 A 848 LEU VAL ILE ASP GLN ILE ASP ASN GLY PHE PHE SER PRO
SEQRES 59 A 848 LYS GLN PRO ASP LEU PHE LYS ASP ILE ILE ASN MET LEU
SEQRES 60 A 848 PHE TYR HIS ASP ARG PHE LYS VAL PHE ALA ASP TYR GLU
SEQRES 61 A 848 ALA TYR VAL LYS CYS GLN ASP LYS VAL SER GLN LEU TYR
SEQRES 62 A 848 MET ASN PRO LYS ALA TRP ASN THR MET VAL LEU LYS ASN
SEQRES 63 A 848 ILE ALA ALA SER GLY LYS PHE SER SER ASP ARG THR ILE
SEQRES 64 A 848 LYS GLU TYR ALA GLN ASN ILE TRP ASN VAL GLU PRO SER
SEQRES 65 A 848 ASP LEU LYS ILE SER LEU SER ASN GLU SER ASN LYS VAL
SEQRES 66 A 848 ASN GLY ASN
SEQRES 1 B 848 GLY GLY ALA LYS PRO LEU THR ASP GLN GLU LYS ARG ARG
SEQRES 2 B 848 GLN ILE SEP ILE ARG GLY ILE VAL GLY VAL GLU ASN VAL
SEQRES 3 B 848 ALA GLU LEU LYS LYS SER PHE ASN ARG HIS LEU HIS PHE
SEQRES 4 B 848 THR LEU VAL LYS ASP ARG ASN VAL ALA THR THR ARG ASP
SEQRES 5 B 848 TYR TYR PHE ALA LEU ALA HIS THR VAL ARG ASP HIS LEU
SEQRES 6 B 848 VAL GLY ARG TRP ILE ARG THR GLN GLN HIS TYR TYR ASP
SEQRES 7 B 848 LYS CYS PRO LYS ARG VAL TYR TYR LEU SER LEU GLU PHE
SEQRES 8 B 848 TYR MET GLY ARG THR LEU GLN ASN THR MET ILE ASN LEU
SEQRES 9 B 848 GLY LEU GLN ASN ALA CYS ASP GLU ALA ILE TYR GLN LEU
SEQRES 10 B 848 GLY LEU ASP ILE GLU GLU LEU GLU GLU ILE GLU GLU ASP
SEQRES 11 B 848 ALA GLY LEU GLY ASN GLY GLY LEU GLY ARG LEU ALA ALA
SEQRES 12 B 848 CYS PHE LEU ASP SER MET ALA THR LEU GLY LEU ALA ALA
SEQRES 13 B 848 TYR GLY TYR GLY ILE ARG TYR GLU TYR GLY ILE PHE ASN
SEQRES 14 B 848 GLN LYS ILE ARG ASP GLY TRP GLN VAL GLU GLU ALA ASP
SEQRES 15 B 848 ASP TRP LEU ARG TYR GLY ASN PRO TRP GLU LYS SER ARG
SEQRES 16 B 848 PRO GLU PHE MET LEU PRO VAL HIS PHE TYR GLY LYS VAL
SEQRES 17 B 848 GLU HIS THR ASN THR GLY THR LYS TRP ILE ASP THR GLN
SEQRES 18 B 848 VAL VAL LEU ALA LEU PRO TYR ASP THR PRO VAL PRO GLY
SEQRES 19 B 848 TYR MET ASN ASN THR VAL ASN THR MET ARG LEU TRP SER
SEQRES 20 B 848 ALA ARG ALA PRO ASN ASP PHE ASN LEU ARG ASP PHE ASN
SEQRES 21 B 848 VAL GLY ASP TYR ILE GLN ALA VAL LEU ASP ARG ASN LEU
SEQRES 22 B 848 ALA GLU ASN ILE SER ARG VAL LEU TYR PRO ASN ASP ASN
SEQRES 23 B 848 PHE PHE GLU GLY LYS GLU LEU ARG LEU LYS GLN GLU TYR
SEQRES 24 B 848 PHE VAL VAL ALA ALA THR LEU GLN ASP ILE ILE ARG ARG
SEQRES 25 B 848 PHE LYS ALA SER LYS PHE GLY SER THR ARG GLY ALA GLY
SEQRES 26 B 848 THR VAL PHE ASP ALA PHE PRO ASP GLN VAL ALA ILE GLN
SEQRES 27 B 848 LEU ASN ASP THR HIS PRO ALA LEU ALA ILE PRO GLU LEU
SEQRES 28 B 848 MET ARG ILE PHE VAL ASP ILE GLU LYS LEU PRO TRP SER
SEQRES 29 B 848 LYS ALA TRP GLU LEU THR GLN LYS THR PHE ALA TYR THR
SEQRES 30 B 848 ASN HIS THR VAL LEU PRO GLU ALA LEU GLU ARG TRP PRO
SEQRES 31 B 848 VAL ASP LEU VAL GLU LYS LEU LEU PRO ARG HIS LEU GLU
SEQRES 32 B 848 ILE ILE TYR GLU ILE ASN GLN LYS HIS LEU ASP ARG ILE
SEQRES 33 B 848 VAL ALA LEU PHE PRO LYS ASP VAL ASP ARG LEU ARG ARG
SEQRES 34 B 848 MET SER LEU ILE GLU GLU GLU GLY SER LYS ARG ILE ASN
SEQRES 35 B 848 MET ALA HIS LEU CYS ILE VAL GLY SER HIS ALA VAL ASN
SEQRES 36 B 848 GLY VAL ALA LYS ILE HIS SER ASP ILE VAL LYS THR LYS
SEQRES 37 B 848 VAL PHE LYS ASP PHE SER GLU LEU GLU PRO ASP LYS PHE
SEQRES 38 B 848 GLN ASN LYS THR ASN GLY ILE THR PRO ARG ARG TRP LEU
SEQRES 39 B 848 LEU LEU CYS ASN PRO GLY LEU ALA GLU LEU ILE ALA GLU
SEQRES 40 B 848 LYS ILE GLY GLU ASP TYR VAL LYS ASP LEU SER GLN LEU
SEQRES 41 B 848 THR LYS LEU HIS SER PHE LEU GLY ASP ASP VAL PHE LEU
SEQRES 42 B 848 ARG GLU LEU ALA LYS VAL LYS GLN GLU ASN LYS LEU LYS
SEQRES 43 B 848 PHE SER GLN PHE LEU GLU THR GLU TYR LYS VAL LYS ILE
SEQRES 44 B 848 ASN PRO SER SER MET PHE ASP VAL GLN VAL LYS ARG ILE
SEQRES 45 B 848 HIS GLU TYR LYS ARG GLN LEU LEU ASN CYS LEU HIS VAL
SEQRES 46 B 848 ILE THR MET TYR ASN ARG ILE LYS LYS ASP PRO LYS LYS
SEQRES 47 B 848 LEU PHE VAL PRO ARG THR VAL ILE ILE GLY GLY LYS ALA
SEQRES 48 B 848 ALA PRO GLY TYR HIS MET ALA LYS MET ILE ILE LYS LEU
SEQRES 49 B 848 ILE THR SER VAL ALA ASP VAL VAL ASN ASN ASP PRO MET
SEQRES 50 B 848 VAL GLY SER LYS LEU LYS VAL ILE PHE LEU GLU ASN TYR
SEQRES 51 B 848 ARG VAL SER LEU ALA GLU LYS VAL ILE PRO ALA THR ASP
SEQRES 52 B 848 LEU SER GLU GLN ILE SER THR ALA GLY THR GLU ALA SER
SEQRES 53 B 848 GLY THR GLY ASN MET LYS PHE MET LEU ASN GLY ALA LEU
SEQRES 54 B 848 THR ILE GLY THR MET ASP GLY ALA ASN VAL GLU MET ALA
SEQRES 55 B 848 GLU GLU ALA GLY GLU GLU ASN LEU PHE ILE PHE GLY MET
SEQRES 56 B 848 ARG ILE ASP ASP VAL ALA ALA LEU ASP LYS LYS GLY TYR
SEQRES 57 B 848 GLU ALA LYS GLU TYR TYR GLU ALA LEU PRO GLU LEU LYS
SEQRES 58 B 848 LEU VAL ILE ASP GLN ILE ASP ASN GLY PHE PHE SER PRO
SEQRES 59 B 848 LYS GLN PRO ASP LEU PHE LYS ASP ILE ILE ASN MET LEU
SEQRES 60 B 848 PHE TYR HIS ASP ARG PHE LYS VAL PHE ALA ASP TYR GLU
SEQRES 61 B 848 ALA TYR VAL LYS CYS GLN ASP LYS VAL SER GLN LEU TYR
SEQRES 62 B 848 MET ASN PRO LYS ALA TRP ASN THR MET VAL LEU LYS ASN
SEQRES 63 B 848 ILE ALA ALA SER GLY LYS PHE SER SER ASP ARG THR ILE
SEQRES 64 B 848 LYS GLU TYR ALA GLN ASN ILE TRP ASN VAL GLU PRO SER
SEQRES 65 B 848 ASP LEU LYS ILE SER LEU SER ASN GLU SER ASN LYS VAL
SEQRES 66 B 848 ASN GLY ASN
MODRES 3DDS SEP A 14 SER PHOSPHOSERINE
HET SEP A 14 10
HET NBG A 901 15
HET NBG B 901 15
HET PO4 A 902 5
HET PLP A 903 15
HET CFF A 904 14
HET 26B A 905 37
HET PLP B 902 15
HET CFF B 903 14
HET MES B 904 12
HET 26B B 905 37
HET 26B B 906 37
HET MPD A 906 8
HETNAM SEP PHOSPHOSERINE
HETNAM NBG 1-N-ACETYL-BETA-D-GLUCOSAMINE
HETNAM PO4 PHOSPHATE ION
HETNAM PLP PYRIDOXAL-5'-PHOSPHATE
HETNAM CFF CAFFEINE
HETNAM 26B O-TERT-BUTYL-N-[(3-{[(2,4,6-TRIMETHYLPHENYL)
HETNAM 2 26B CARBAMOYL]AMINO}NAPHTHALEN-2-YL)CARBONYL]-L-THREONINE
HETNAM MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID
HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL
HETSYN SEP PHOSPHONOSERINE
HETSYN PLP VITAMIN B6 PHOSPHATE
HETSYN CFF 3,7-DIHYDRO-1,3,7-TRIMETHYL-1H-PURINE-2,6-DIONE
FORMUL 1 SEP C3 H8 N O6 P
FORMUL 3 NBG 2(C8 H15 N O6)
FORMUL 5 PO4 O4 P 3-
FORMUL 6 PLP 2(C8 H10 N O6 P)
FORMUL 7 CFF 2(C8 H10 N4 O2)
FORMUL 8 26B 3(C29 H35 N3 O5)
FORMUL 11 MES C6 H13 N O4 S
FORMUL 14 MPD C6 H14 O2
FORMUL 15 HOH *1353(H2 O)
HELIX 1 1 GLY A 17 THR A 38 1 22
HELIX 2 2 ASP A 42 ALA A 46 5 5
HELIX 3 3 THR A 47 HIS A 62 1 16
HELIX 4 4 LEU A 63 CYS A 78 1 16
HELIX 5 5 THR A 94 LEU A 102 1 9
HELIX 6 6 LEU A 104 LEU A 115 1 12
HELIX 7 7 ASP A 118 ILE A 125 1 8
HELIX 8 8 GLY A 134 LEU A 150 1 17
HELIX 9 9 PRO A 194 MET A 197 5 4
HELIX 10 10 ASP A 261 ASP A 268 1 8
HELIX 11 11 ASP A 268 ASN A 274 1 7
HELIX 12 12 ILE A 275 ARG A 277 5 3
HELIX 13 13 LYS A 289 SER A 314 1 26
HELIX 14 14 ALA A 328 GLN A 332 1 5
HELIX 15 15 LEU A 344 ILE A 356 1 13
HELIX 16 16 PRO A 360 THR A 371 1 12
HELIX 17 17 LEU A 380 LEU A 384 5 5
HELIX 18 18 VAL A 389 LEU A 396 1 8
HELIX 19 19 LEU A 396 PHE A 418 1 23
HELIX 20 20 ASP A 421 SER A 429 1 9
HELIX 21 21 MET A 441 GLY A 448 1 8
HELIX 22 22 ALA A 456 LYS A 466 1 11
HELIX 23 23 PHE A 468 GLU A 475 1 8
HELIX 24 24 ASN A 496 GLY A 508 1 13
HELIX 25 25 GLU A 509 LYS A 513 5 5
HELIX 26 26 ASP A 514 LEU A 525 5 12
HELIX 27 27 ASP A 527 TYR A 553 1 27
HELIX 28 28 ARG A 575 ASP A 593 1 19
HELIX 29 29 TYR A 613 ASP A 633 1 21
HELIX 30 30 VAL A 636 SER A 638 5 3
HELIX 31 31 ARG A 649 ILE A 657 1 9
HELIX 32 32 PRO A 658 THR A 660 5 3
HELIX 33 33 THR A 676 ASN A 684 1 9
HELIX 34 34 ALA A 695 GLY A 704 1 10
HELIX 35 35 GLU A 705 LEU A 708 5 4
HELIX 36 36 ARG A 714 GLY A 725 1 12
HELIX 37 37 GLU A 727 LEU A 735 1 9
HELIX 38 38 LEU A 735 GLY A 748 1 14
HELIX 39 39 PHE A 758 HIS A 768 1 11
HELIX 40 40 LYS A 772 MET A 792 1 21
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 23 THR B 38 1 16
HELIX 45 45 ASP B 42 ALA B 46 5 5
HELIX 46 46 THR B 47 HIS B 62 1 16
HELIX 47 47 LEU B 63 CYS B 78 1 16
HELIX 48 48 THR B 94 LEU B 102 1 9
HELIX 49 49 LEU B 104 LEU B 115 1 12
HELIX 50 50 ASP B 118 GLU B 124 1 7
HELIX 51 51 GLY B 134 LEU B 150 1 17
HELIX 52 52 PRO B 194 MET B 197 5 4
HELIX 53 53 ASP B 261 ASP B 268 1 8
HELIX 54 54 ASP B 268 ASN B 274 1 7
HELIX 55 55 ILE B 275 ARG B 277 5 3
HELIX 56 56 LYS B 289 SER B 314 1 26
HELIX 57 57 LYS B 315 SER B 318 5 4
HELIX 58 58 THR B 324 ASP B 327 5 4
HELIX 59 59 ALA B 328 GLN B 332 1 5
HELIX 60 60 LEU B 344 ILE B 356 1 13
HELIX 61 61 PRO B 360 THR B 371 1 12
HELIX 62 62 LEU B 380 LEU B 384 5 5
HELIX 63 63 VAL B 389 LEU B 396 1 8
HELIX 64 64 LEU B 396 PHE B 418 1 23
HELIX 65 65 ASP B 421 SER B 429 1 9
HELIX 66 66 MET B 441 GLY B 448 1 8
HELIX 67 67 ALA B 456 LYS B 466 1 11
HELIX 68 68 PHE B 468 GLU B 475 1 8
HELIX 69 69 ASN B 496 GLY B 508 1 13
HELIX 70 70 GLU B 509 LYS B 513 5 5
HELIX 71 71 ASP B 514 LEU B 525 5 12
HELIX 72 72 ASP B 527 LYS B 554 1 28
HELIX 73 73 ARG B 575 ASP B 593 1 19
HELIX 74 74 TYR B 613 ASP B 633 1 21
HELIX 75 75 VAL B 636 SER B 638 5 3
HELIX 76 76 ARG B 649 ILE B 657 1 9
HELIX 77 77 PRO B 658 THR B 660 5 3
HELIX 78 78 THR B 676 ASN B 684 1 9
HELIX 79 79 ALA B 695 GLY B 704 1 10
HELIX 80 80 GLU B 705 LEU B 708 5 4
HELIX 81 81 ARG B 714 GLY B 725 1 12
HELIX 82 82 ALA B 728 LEU B 735 1 8
HELIX 83 83 LEU B 735 GLY B 748 1 14
HELIX 84 84 PHE B 758 HIS B 768 1 11
HELIX 85 85 LYS B 772 MET B 792 1 21
HELIX 86 86 ASN B 793 ALA B 807 1 15
HELIX 87 87 SER B 808 PHE B 811 5 4
HELIX 88 88 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 SER A 245 N LEU A 224
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 ALA A 129 N GLY A 92
SHEET 1 D 2 ASN A 167 ARG A 171 0
SHEET 2 D 2 TRP A 174 GLU A 178 -1 O VAL A 176 N LYS A 169
SHEET 1 E 2 LYS A 205 THR A 209 0
SHEET 2 E 2 GLY A 212 ILE A 216 -1 O ILE A 216 N LYS A 205
SHEET 1 F 2 THR A 319 ARG A 320 0
SHEET 2 F 2 GLY A 323 THR A 324 -1 O GLY A 323 N ARG A 320
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 LYS A 641
SHEET 3 H 6 MET A 562 VAL A 567 1 N ASP A 564 O ILE A 604
SHEET 4 H 6 LEU A 662 GLN A 665 1 O LEU A 662 N VAL A 565
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 LEU B 198 O ALA B 223
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 SER B 245 N LEU B 224
SHEET 4 J 9 ALA B 153 ILE B 159 1 N GLY B 156 O ARG B 242
SHEET 5 J 9 ARG B 81 LEU B 85 1 N TYR B 84 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 ALA B 451 GLY B 454 1 O ALA B 451 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 TRP B 174 N ARG B 171
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 VAL B 603 O LYS B 641
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 VAL B 565
SHEET 5 O 6 LEU B 687 GLY B 690 1 O LEU B 687 N SER B 663
SHEET 6 O 6 PHE B 709 ILE B 710 1 O PHE B 709 N THR B 688
LINK C ILE A 13 N SEP A 14 1555 1555 1.33
LINK C SEP A 14 N ILE A 15 1555 1555 1.33
LINK NZ LYS A 680 C4A PLP A 903 1555 1555 1.26
LINK NZ LYS B 680 C4A PLP B 902 1555 1555 1.28
SITE 1 AC1 11 GLY A 135 LEU A 136 ASN A 284 ASP A 339
SITE 2 AC1 11 HIS A 377 ASN A 484 TYR A 573 GLU A 672
SITE 3 AC1 11 ALA A 673 SER A 674 GLY A 675
SITE 1 AC2 10 LEU B 136 ASN B 284 ASP B 339 HIS B 377
SITE 2 AC2 10 ASN B 484 TYR B 573 GLU B 672 ALA B 673
SITE 3 AC2 10 SER B 674 GLY B 675
SITE 1 AC3 3 ILE A 15 ARG A 16 LYS B 205
SITE 1 AC4 11 TYR A 90 GLY A 134 TRP A 491 LYS A 568
SITE 2 AC4 11 LYS A 574 TYR A 648 ARG A 649 GLY A 675
SITE 3 AC4 11 THR A 676 GLY A 677 LYS A 680
SITE 1 AC5 12 TYR B 90 GLY B 134 TRP B 491 LYS B 568
SITE 2 AC5 12 LYS B 574 TYR B 648 ARG B 649 ALA B 653
SITE 3 AC5 12 GLY B 675 THR B 676 GLY B 677 LYS B 680
SITE 1 AC6 6 ASN A 282 PHE A 285 HIS A 571 ALA A 610
SITE 2 AC6 6 GLY A 612 TYR A 613
SITE 1 AC7 6 ASN B 282 PHE B 285 HIS B 571 ALA B 610
SITE 2 AC7 6 GLY B 612 TYR B 613
SITE 1 AC8 5 ILE B 170 ASP B 172 GLY B 173 GLU B 552
SITE 2 AC8 5 GLU B 646
SITE 1 AC9 10 LYS A 41 ASP A 42 GLN B 71 GLN B 72
SITE 2 AC9 10 ARG B 193 PHE B 196 ASP B 227 THR B 240
SITE 3 AC9 10 ARG B 310 ALA B 313
SITE 1 BC1 10 GLN A 71 GLN A 72 ARG A 193 PHE A 196
SITE 2 BC1 10 ASP A 227 THR A 240 ARG A 310 ALA A 313
SITE 3 BC1 10 LYS B 41 ASP B 42
SITE 1 BC2 8 ARG B 43 TYR B 51 GLY B 116 LEU B 531
SITE 2 BC2 8 ARG B 532 MET B 792 ASN B 793 PRO B 794
SITE 1 BC3 4 TRP A 215 ARG A 351 ILE A 356 GLY B 508
CRYST1 124.403 124.403 123.614 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 0.008038 0.004641 0.000000 0.00000
SCALE2 0.000000 0.009282 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008090 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
