HEADER TRANSFERASE 13-JUL-07 2QLL
TITLE HUMAN LIVER GLYCOGEN PHOSPHORYLASE- GL COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLYCOGEN PHOSPHORYLASE, LIVER FORM;
COMPND 3 CHAIN: A;
COMPND 4 EC: 2.4.1.1;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: PROTEIN TARGETING TO GLYCOGEN - GL;
COMPND 8 CHAIN: B;
COMPND 9 FRAGMENT: GL-CTERM (281-284);
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: PYGL;
SOURCE 6 EXPRESSION_SYSTEM: UNIDENTIFIED BACULOVIRUS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 10469;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: SF9;
SOURCE 9 EXPRESSION_SYSTEM_CELL: HIGH FIVE CELLS;
SOURCE 10 MOL_ID: 2;
SOURCE 11 SYNTHETIC: YES;
SOURCE 12 OTHER_DETAILS: PEPTIDE SYNTHESIS
KEYWDS DRUG DISCOVERY, GLYCOGEN METABOLISM, PROTEIN-PROTEIN INTERACTION,
KEYWDS 2 ALLOSTERIC ENZYME, CARBOHYDRATE METABOLISM, DISEASE MUTATION,
KEYWDS 3 GLYCOGEN STORAGE DISEASE, GLYCOSYLTRANSFERASE, NUCLEOTIDE-BINDING,
KEYWDS 4 PHOSPHORYLATION, PYRIDOXAL PHOSPHATE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.PAUTSCH,R.STREICHER,O.WISSDORF,N.STADLER
REVDAT 4 13-JUL-11 2QLL 1 VERSN
REVDAT 3 24-FEB-09 2QLL 1 VERSN
REVDAT 2 24-JUN-08 2QLL 1 JRNL
REVDAT 1 19-FEB-08 2QLL 0
JRNL AUTH A.PAUTSCH,N.STADLER,O.WISSDORF,E.LANGKOPF,W.MORETH,
JRNL AUTH 2 R.STREICHER
JRNL TITL MOLECULAR RECOGNITION OF THE PROTEIN PHOSPHATASE 1 GLYCOGEN
JRNL TITL 2 TARGETING SUBUNIT BY GLYCOGEN PHOSPHORYLASE.
JRNL REF J.BIOL.CHEM. V. 283 8913 2008
JRNL REFN ISSN 0021-9258
JRNL PMID 18198182
JRNL DOI 10.1074/JBC.M706612200
REMARK 2
REMARK 2 RESOLUTION. 2.56 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER-TNT 2.1.1
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SMART,VONRHEIN,WOMACK,
REMARK 3 : MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.56
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.50
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 3 NUMBER OF REFLECTIONS : 37156
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) : 0.206
REMARK 3 R VALUE (WORKING SET) : 0.203
REMARK 3 FREE R VALUE : 0.276
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1769
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 9
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.56
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.71
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.36
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : NULL
REMARK 3 BIN R VALUE (WORKING + TEST SET) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 5021
REMARK 3 BIN R VALUE (WORKING SET) : 0.4000
REMARK 3 BIN FREE R VALUE : 0.4620
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 264
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6565
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 15
REMARK 3 SOLVENT ATOMS : 154
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 57.54
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 65.26
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.80800
REMARK 3 B22 (A**2) : -1.80800
REMARK 3 B33 (A**2) : 3.61600
REMARK 3 B12 (A**2) : 0.00000
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) : NULL
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : NULL
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : NULL
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : NULL ; NULL ; NULL
REMARK 3 BOND ANGLES : NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES : NULL ; NULL ; NULL
REMARK 3 TRIGONAL CARBON PLANES : NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES : NULL ; NULL ; NULL
REMARK 3 ISOTROPIC THERMAL FACTORS : NULL ; NULL ; NULL
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : NULL ; NULL ; NULL
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : NULL ; NULL ; NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : NULL
REMARK 3 OTHER TORSION ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2QLL COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-JUL-07.
REMARK 100 THE RCSB ID CODE IS RCSB043751.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-APR-03
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
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) : 0.9
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 37156
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.560
REMARK 200 RESOLUTION RANGE LOW (A) : 19.500
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.07500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.4700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.56
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.71
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.47100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
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 (%): 56.84
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.85
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 8 MG/ML PROTEIN, 0.1 M TRIS, 8% PEG
REMARK 280 8000, PH 8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
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 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 41.89833
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 83.79667
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 83.79667
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 41.89833
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 SECOND PART OF THE BIOLOGICAL ASSEMBLY IS GENERATED BY:
REMARK 300 Y,X,-Z+1
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2215 ANGSTROM**2
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 350 BIOMT1 2 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 125.69500
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 MET A 0
REMARK 465 ALA A 1
REMARK 465 LYS A 2
REMARK 465 PRO A 3
REMARK 465 GLU A 162
REMARK 465 TYR A 163
REMARK 465 GLY A 164
REMARK 465 ILE A 165
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 ASP A 261
REMARK 465 TYR A 262
REMARK 465 ILE A 263
REMARK 465 GLN A 264
REMARK 465 ALA A 265
REMARK 465 ASN A 282
REMARK 465 ASP A 283
REMARK 465 ASN A 284
REMARK 465 PHE A 285
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 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 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 SER A 837 OG
REMARK 470 ASN A 838 CG OD1
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO A 199 C - N - CA ANGL. DEV. = 9.4 DEGREES
REMARK 500 PRO A 342 C - N - CA ANGL. DEV. = -11.3 DEGREES
REMARK 500 PRO A 381 C - N - CA ANGL. DEV. = 16.1 DEGREES
REMARK 500 PRO A 381 C - N - CD ANGL. DEV. = -35.6 DEGREES
REMARK 500 PRO A 419 C - N - CA ANGL. DEV. = 11.5 DEGREES
REMARK 500 PRO A 419 C - N - CD ANGL. DEV. = -16.1 DEGREES
REMARK 500 PRO A 476 C - N - CA ANGL. DEV. = 10.8 DEGREES
REMARK 500 PRO A 476 C - N - CD ANGL. DEV. = -24.8 DEGREES
REMARK 500 PRO A 488 C - N - CA ANGL. DEV. = 12.3 DEGREES
REMARK 500 PRO A 488 C - N - CD ANGL. DEV. = -14.5 DEGREES
REMARK 500 PRO A 559 C - N - CD ANGL. DEV. = -16.4 DEGREES
REMARK 500 PRO A 594 C - N - CA ANGL. DEV. = 11.8 DEGREES
REMARK 500 PRO A 634 C - N - CA ANGL. DEV. = 14.3 DEGREES
REMARK 500 PRO A 634 C - N - CD ANGL. DEV. = -18.4 DEGREES
REMARK 500 PRO A 736 C - N - CD ANGL. DEV. = -13.4 DEGREES
REMARK 500 PRO A 829 C - N - CD ANGL. DEV. = -14.0 DEGREES
REMARK 500 PRO B 282 C - N - CD ANGL. DEV. = -14.8 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 THR A 5 114.97 72.70
REMARK 500 ASP A 6 -138.59 -112.84
REMARK 500 GLN A 7 42.94 -76.58
REMARK 500 GLU A 22 46.66 -107.08
REMARK 500 LEU A 95 -79.45 -42.90
REMARK 500 ASN A 133 -3.78 -148.05
REMARK 500 ARG A 171 112.10 -160.23
REMARK 500 ASP A 172 37.59 72.33
REMARK 500 GLU A 177 154.01 -49.43
REMARK 500 ARG A 193 60.21 -113.92
REMARK 500 MET A 197 156.21 -44.56
REMARK 500 TYR A 203 -138.17 58.09
REMARK 500 THR A 211 64.47 -107.42
REMARK 500 PRO A 249 -72.34 -50.85
REMARK 500 LEU A 267 4.91 54.76
REMARK 500 ARG A 269 20.49 -62.33
REMARK 500 ASN A 270 -17.49 -142.74
REMARK 500 ARG A 277 -20.50 -149.19
REMARK 500 ASP A 339 -179.66 69.72
REMARK 500 PRO A 342 44.61 -108.73
REMARK 500 THR A 368 -71.87 -57.62
REMARK 500 LEU A 380 156.81 -37.97
REMARK 500 GLU A 382 63.66 -112.68
REMARK 500 ALA A 383 5.17 -173.85
REMARK 500 ASP A 421 81.29 -35.16
REMARK 500 LEU A 425 -96.30 -49.19
REMARK 500 ARG A 426 -19.76 -38.82
REMARK 500 ARG A 427 -72.14 -71.32
REMARK 500 MET A 428 1.58 -61.26
REMARK 500 GLU A 434 -131.36 -154.41
REMARK 500 LYS A 437 135.68 -21.78
REMARK 500 LYS A 466 -77.15 -114.57
REMARK 500 LEU A 474 -79.25 -66.34
REMARK 500 GLU A 475 69.38 -105.97
REMARK 500 ARG A 489 -70.46 -86.58
REMARK 500 LEU A 492 -64.32 -162.70
REMARK 500 ASN A 496 57.35 -113.18
REMARK 500 GLU A 509 43.61 -105.49
REMARK 500 ASP A 514 83.02 -153.32
REMARK 500 LYS A 520 -15.13 -43.77
REMARK 500 SER A 523 3.81 -59.77
REMARK 500 ASP A 527 81.32 -42.95
REMARK 500 LYS A 554 76.93 44.87
REMARK 500 VAL A 567 78.68 -119.93
REMARK 500 ARG A 575 -100.98 71.91
REMARK 500 GLN A 576 -48.63 58.13
REMARK 500 ASP A 593 67.00 166.79
REMARK 500 PRO A 594 66.62 -64.48
REMARK 500 LYS A 595 5.75 176.96
REMARK 500 LEU A 597 104.97 -42.70
REMARK 500
REMARK 500 THIS ENTRY HAS 80 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 MET A 91 22.4 L L OUTSIDE RANGE
REMARK 500 ILE A 657 24.9 L L OUTSIDE RANGE
REMARK 500 THR A 660 24.2 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A1050 DISTANCE = 8.41 ANGSTROMS
REMARK 525 HOH A1054 DISTANCE = 5.08 ANGSTROMS
REMARK 525 HOH A1082 DISTANCE = 6.00 ANGSTROMS
REMARK 525 HOH A1126 DISTANCE = 6.53 ANGSTROMS
REMARK 525 HOH A1148 DISTANCE = 6.58 ANGSTROMS
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 PLP A 999
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP A 999
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1FA9 RELATED DB: PDB
REMARK 900 RELATED ID: 1FC0 RELATED DB: PDB
DBREF 2QLL A 0 846 UNP P06737 PYGL_HUMAN 1 847
DBREF 2QLL B 281 284 PDB 2QLL 2QLL 281 284
SEQADV 2QLL SEP A 14 UNP P06737 SER 15 MODIFIED RESIDUE
SEQRES 1 A 847 MET ALA LYS PRO LEU THR ASP GLN GLU LYS ARG ARG GLN
SEQRES 2 A 847 ILE SEP ILE ARG GLY ILE VAL GLY VAL GLU ASN VAL ALA
SEQRES 3 A 847 GLU LEU LYS LYS SER PHE ASN ARG HIS LEU HIS PHE THR
SEQRES 4 A 847 LEU VAL LYS ASP ARG ASN VAL ALA THR THR ARG ASP TYR
SEQRES 5 A 847 TYR PHE ALA LEU ALA HIS THR VAL ARG ASP HIS LEU VAL
SEQRES 6 A 847 GLY ARG TRP ILE ARG THR GLN GLN HIS TYR TYR ASP LYS
SEQRES 7 A 847 CYS PRO LYS ARG VAL TYR TYR LEU SER LEU GLU PHE TYR
SEQRES 8 A 847 MET GLY ARG THR LEU GLN ASN THR MET ILE ASN LEU GLY
SEQRES 9 A 847 LEU GLN ASN ALA CYS ASP GLU ALA ILE TYR GLN LEU GLY
SEQRES 10 A 847 LEU ASP ILE GLU GLU LEU GLU GLU ILE GLU GLU ASP ALA
SEQRES 11 A 847 GLY LEU GLY ASN GLY GLY LEU GLY ARG LEU ALA ALA CYS
SEQRES 12 A 847 PHE LEU ASP SER MET ALA THR LEU GLY LEU ALA ALA TYR
SEQRES 13 A 847 GLY TYR GLY ILE ARG TYR GLU TYR GLY ILE PHE ASN GLN
SEQRES 14 A 847 LYS ILE ARG ASP GLY TRP GLN VAL GLU GLU ALA ASP ASP
SEQRES 15 A 847 TRP LEU ARG TYR GLY ASN PRO TRP GLU LYS SER ARG PRO
SEQRES 16 A 847 GLU PHE MET LEU PRO VAL HIS PHE TYR GLY LYS VAL GLU
SEQRES 17 A 847 HIS THR ASN THR GLY THR LYS TRP ILE ASP THR GLN VAL
SEQRES 18 A 847 VAL LEU ALA LEU PRO TYR ASP THR PRO VAL PRO GLY TYR
SEQRES 19 A 847 MET ASN ASN THR VAL ASN THR MET ARG LEU TRP SER ALA
SEQRES 20 A 847 ARG ALA PRO ASN ASP PHE ASN LEU ARG ASP PHE ASN VAL
SEQRES 21 A 847 GLY ASP TYR ILE GLN ALA VAL LEU ASP ARG ASN LEU ALA
SEQRES 22 A 847 GLU ASN ILE SER ARG VAL LEU TYR PRO ASN ASP ASN PHE
SEQRES 23 A 847 PHE GLU GLY LYS GLU LEU ARG LEU LYS GLN GLU TYR PHE
SEQRES 24 A 847 VAL VAL ALA ALA THR LEU GLN ASP ILE ILE ARG ARG PHE
SEQRES 25 A 847 LYS ALA SER LYS PHE GLY SER THR ARG GLY ALA GLY THR
SEQRES 26 A 847 VAL PHE ASP ALA PHE PRO ASP GLN VAL ALA ILE GLN LEU
SEQRES 27 A 847 ASN ASP THR HIS PRO ALA LEU ALA ILE PRO GLU LEU MET
SEQRES 28 A 847 ARG ILE PHE VAL ASP ILE GLU LYS LEU PRO TRP SER LYS
SEQRES 29 A 847 ALA TRP GLU LEU THR GLN LYS THR PHE ALA TYR THR ASN
SEQRES 30 A 847 HIS THR VAL LEU PRO GLU ALA LEU GLU ARG TRP PRO VAL
SEQRES 31 A 847 ASP LEU VAL GLU LYS LEU LEU PRO ARG HIS LEU GLU ILE
SEQRES 32 A 847 ILE TYR GLU ILE ASN GLN LYS HIS LEU ASP ARG ILE VAL
SEQRES 33 A 847 ALA LEU PHE PRO LYS ASP VAL ASP ARG LEU ARG ARG MET
SEQRES 34 A 847 SER LEU ILE GLU GLU GLU GLY SER LYS ARG ILE ASN MET
SEQRES 35 A 847 ALA HIS LEU CYS ILE VAL GLY SER HIS ALA VAL ASN GLY
SEQRES 36 A 847 VAL ALA LYS ILE HIS SER ASP ILE VAL LYS THR LYS VAL
SEQRES 37 A 847 PHE LYS ASP PHE SER GLU LEU GLU PRO ASP LYS PHE GLN
SEQRES 38 A 847 ASN LYS THR ASN GLY ILE THR PRO ARG ARG TRP LEU LEU
SEQRES 39 A 847 LEU CYS ASN PRO GLY LEU ALA GLU LEU ILE ALA GLU LYS
SEQRES 40 A 847 ILE GLY GLU ASP TYR VAL LYS ASP LEU SER GLN LEU THR
SEQRES 41 A 847 LYS LEU HIS SER PHE LEU GLY ASP ASP VAL PHE LEU ARG
SEQRES 42 A 847 GLU LEU ALA LYS VAL LYS GLN GLU ASN LYS LEU LYS PHE
SEQRES 43 A 847 SER GLN PHE LEU GLU THR GLU TYR LYS VAL LYS ILE ASN
SEQRES 44 A 847 PRO SER SER MET PHE ASP VAL GLN VAL LYS ARG ILE HIS
SEQRES 45 A 847 GLU TYR LYS ARG GLN LEU LEU ASN CYS LEU HIS VAL ILE
SEQRES 46 A 847 THR MET TYR ASN ARG ILE LYS LYS ASP PRO LYS LYS LEU
SEQRES 47 A 847 PHE VAL PRO ARG THR VAL ILE ILE GLY GLY LYS ALA ALA
SEQRES 48 A 847 PRO GLY TYR HIS MET ALA LYS MET ILE ILE LYS LEU ILE
SEQRES 49 A 847 THR SER VAL ALA ASP VAL VAL ASN ASN ASP PRO MET VAL
SEQRES 50 A 847 GLY SER LYS LEU LYS VAL ILE PHE LEU GLU ASN TYR ARG
SEQRES 51 A 847 VAL SER LEU ALA GLU LYS VAL ILE PRO ALA THR ASP LEU
SEQRES 52 A 847 SER GLU GLN ILE SER THR ALA GLY THR GLU ALA SER GLY
SEQRES 53 A 847 THR GLY ASN MET LYS PHE MET LEU ASN GLY ALA LEU THR
SEQRES 54 A 847 ILE GLY THR MET ASP GLY ALA ASN VAL GLU MET ALA GLU
SEQRES 55 A 847 GLU ALA GLY GLU GLU ASN LEU PHE ILE PHE GLY MET ARG
SEQRES 56 A 847 ILE ASP ASP VAL ALA ALA LEU ASP LYS LYS GLY TYR GLU
SEQRES 57 A 847 ALA LYS GLU TYR TYR GLU ALA LEU PRO GLU LEU LYS LEU
SEQRES 58 A 847 VAL ILE ASP GLN ILE ASP ASN GLY PHE PHE SER PRO LYS
SEQRES 59 A 847 GLN PRO ASP LEU PHE LYS ASP ILE ILE ASN MET LEU PHE
SEQRES 60 A 847 TYR HIS ASP ARG PHE LYS VAL PHE ALA ASP TYR GLU ALA
SEQRES 61 A 847 TYR VAL LYS CYS GLN ASP LYS VAL SER GLN LEU TYR MET
SEQRES 62 A 847 ASN PRO LYS ALA TRP ASN THR MET VAL LEU LYS ASN ILE
SEQRES 63 A 847 ALA ALA SER GLY LYS PHE SER SER ASP ARG THR ILE LYS
SEQRES 64 A 847 GLU TYR ALA GLN ASN ILE TRP ASN VAL GLU PRO SER ASP
SEQRES 65 A 847 LEU LYS ILE SER LEU SER ASN GLU SER ASN LYS VAL ASN
SEQRES 66 A 847 GLY ASN
SEQRES 1 B 4 GLY PRO TYR TYR
MODRES 2QLL SEP A 14 SER PHOSPHOSERINE
HET SEP A 14 10
HET PLP A 999 15
HETNAM SEP PHOSPHOSERINE
HETNAM PLP PYRIDOXAL-5'-PHOSPHATE
HETSYN SEP PHOSPHONOSERINE
HETSYN PLP VITAMIN B6 PHOSPHATE
FORMUL 1 SEP C3 H8 N O6 P
FORMUL 3 PLP C8 H10 N O6 P
FORMUL 4 HOH *154(H2 O)
HELIX 1 1 LYS A 9 ILE A 13 5 5
HELIX 2 2 ASN A 23 PHE A 37 1 15
HELIX 3 3 THR A 47 CYS A 78 1 32
HELIX 4 4 THR A 94 LEU A 102 1 9
HELIX 5 5 LEU A 104 LEU A 115 1 12
HELIX 6 6 ASP A 118 GLU A 124 1 7
HELIX 7 7 GLY A 134 LEU A 150 1 17
HELIX 8 8 PRO A 194 MET A 197 5 4
HELIX 9 9 ALA A 272 ARG A 277 5 6
HELIX 10 10 PHE A 286 ALA A 313 1 28
HELIX 11 11 THR A 324 ASP A 331 5 8
HELIX 12 12 LEU A 344 ILE A 356 1 13
HELIX 13 13 PRO A 360 THR A 371 1 12
HELIX 14 14 VAL A 389 LEU A 396 1 8
HELIX 15 15 LEU A 396 PHE A 418 1 23
HELIX 16 16 ASP A 421 SER A 429 1 9
HELIX 17 17 MET A 441 GLY A 448 1 8
HELIX 18 18 ALA A 456 LYS A 466 1 11
HELIX 19 19 PHE A 468 GLU A 475 1 8
HELIX 20 20 ASN A 496 GLY A 508 1 13
HELIX 21 21 ASP A 514 LEU A 525 5 12
HELIX 22 22 ASP A 527 LYS A 554 1 28
HELIX 23 23 GLN A 576 ARG A 589 1 14
HELIX 24 24 TYR A 613 ASP A 633 1 21
HELIX 25 25 ARG A 649 ILE A 657 1 9
HELIX 26 26 PRO A 658 THR A 660 5 3
HELIX 27 27 GLY A 675 ASN A 684 1 10
HELIX 28 28 ASP A 693 GLY A 704 1 12
HELIX 29 29 GLU A 705 LEU A 708 5 4
HELIX 30 30 ARG A 714 ASP A 722 1 9
HELIX 31 31 ALA A 728 LEU A 735 1 8
HELIX 32 32 LEU A 735 ASN A 747 1 13
HELIX 33 33 ILE A 762 TYR A 767 1 6
HELIX 34 34 LYS A 772 ASN A 793 1 22
HELIX 35 35 ASN A 793 ALA A 806 1 14
HELIX 36 36 ALA A 807 PHE A 811 5 5
HELIX 37 37 SER A 812 ILE A 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 VAL A 200 O VAL A 221
SHEET 1 B 9 LYS A 191 SER A 192 0
SHEET 2 B 9 GLN A 219 PRO A 231 -1 O ASP A 227 N LYS A 191
SHEET 3 B 9 VAL A 238 ARG A 247 -1 O LEU A 243 N TYR A 226
SHEET 4 B 9 ALA A 154 ILE A 159 1 N GLY A 156 O ARG A 242
SHEET 5 B 9 ARG A 81 LEU A 85 1 N TYR A 84 O TYR A 157
SHEET 6 B 9 VAL A 333 ASN A 338 1 O GLN A 336 N TYR A 83
SHEET 7 B 9 PHE A 372 THR A 375 1 O THR A 375 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 GLY A 454
SHEET 1 C 2 LYS A 169 ARG A 171 0
SHEET 2 C 2 TRP A 174 VAL A 176 -1 O VAL A 176 N LYS A 169
SHEET 1 D 2 LYS A 205 GLU A 207 0
SHEET 2 D 2 LYS A 214 ILE A 216 -1 O ILE A 216 N LYS A 205
SHEET 1 E 3 ARG A 386 PRO A 388 0
SHEET 2 E 3 ARG A 438 ASN A 440 -1 O ILE A 439 N TRP A 387
SHEET 3 E 3 ILE A 431 GLU A 432 -1 N GLU A 432 O ARG A 438
SHEET 1 F 6 LEU A 640 LEU A 645 0
SHEET 2 F 6 ARG A 601 GLY A 606 1 N VAL A 603 O LYS A 641
SHEET 3 F 6 MET A 562 VAL A 567 1 N GLN A 566 O ILE A 604
SHEET 4 F 6 LEU A 662 GLN A 665 1 O GLU A 664 N VAL A 565
SHEET 5 F 6 LEU A 687 GLY A 690 1 O LEU A 687 N SER A 663
SHEET 6 F 6 PHE A 709 ILE A 710 1 O PHE A 709 N THR A 688
LINK C ILE A 13 N SEP A 14 1555 1555 1.34
LINK C SEP A 14 N ILE A 15 1555 1555 1.34
SITE 1 AC1 9 TYR A 90 GLY A 135 LYS A 568 LYS A 574
SITE 2 AC1 9 ARG A 649 VAL A 650 THR A 676 GLY A 677
SITE 3 AC1 9 LYS A 680
CRYST1 123.986 123.986 125.695 90.00 90.00 120.00 P 31 2 1 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 0.004657 0.000000 0.00000
SCALE2 0.000000 0.009313 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007956 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
