HEADER TRANSFERASE 16-JAN-02 1KTI
TITLE BINDING OF 100 MM N-ACETYL-N'-BETA-D-GLUCOPYRANOSYL UREA TO GLYCOGEN
TITLE 2 PHOSPHORYLASE B: KINETIC AND CRYSTALLOGRAPHIC STUDIES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLYCOGEN PHOSPHORYLASE, MUSCLE FORM;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: MYOPHOSPHORYLASE;
COMPND 5 EC: 2.4.1.1
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ORYCTOLAGUS CUNICULUS;
SOURCE 3 ORGANISM_COMMON: RABBIT;
SOURCE 4 ORGANISM_TAXID: 9986;
SOURCE 5 OTHER_DETAILS: MUSCLE
KEYWDS GLYCOGENOLYSIS, TYPE 2 DIABETES, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.G.OIKONOMAKOS,M.KOSMOPOULOU,S.E.ZOGRAPHOS,D.D.LEONIDAS,
AUTHOR 2 E.D.CHRYSINA,L.SOMSAK,V.NAGY,J.P.PRALY,T.DOCSA,B.TOTH,P.GERGELY
REVDAT 6 29-JUL-20 1KTI 1 COMPND REMARK HETNAM LINK
REVDAT 6 2 1 SITE
REVDAT 5 13-JUL-11 1KTI 1 VERSN
REVDAT 4 24-FEB-09 1KTI 1 VERSN
REVDAT 3 03-FEB-04 1KTI 1 REMARK
REVDAT 2 19-JUN-02 1KTI 1 JRNL
REVDAT 1 30-JAN-02 1KTI 0
SPRSDE 30-JAN-02 1KTI 1K0Q
JRNL AUTH N.G.OIKONOMAKOS,M.KOSMOPOULOU,S.E.ZOGRAPHOS,D.D.LEONIDAS,
JRNL AUTH 2 E.D.CHRYSINA,L.SOMSAK,V.NAGY,J.P.PRALY,T.DOCSA,B.TOTH,
JRNL AUTH 3 P.GERGELY
JRNL TITL BINDING OF N-ACETYL-N'-BETA-D-GLUCOPYRANOSYL UREA AND
JRNL TITL 2 N-BENZOYL-N'-BETA-D-GLUCOPYRANOSYL UREA TO GLYCOGEN
JRNL TITL 3 PHOSPHORYLASE B: KINETIC AND CRYSTALLOGRAPHIC STUDIES.
JRNL REF EUR.J.BIOCHEM. V. 269 1684 2002
JRNL REFN ISSN 0014-2956
JRNL PMID 11895439
JRNL DOI 10.1046/J.1432-1327.2002.02813.X
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH N.G.OIKONOMAKOS,V.T.SKAMNAKI,E.OSZ,L.SZILAGYI,L.SOMSAK,
REMARK 1 AUTH 2 T.DOCSA,B.TOTH,P.GERGELY
REMARK 1 TITL KINETIC AND CRYSTALLOGRAPHIC STUDIES OF GLUCOPYRANOSYLIDENE
REMARK 1 TITL 2 SPIROTHIOHYDANTOIN BINDING TO GLYCOGEN PHOSPHORYLASE B
REMARK 1 REF BIOORG.MED.CHEM. V. 10 261 2002
REMARK 1 REFN ISSN 0968-0896
REMARK 1 DOI 10.1016/S0968-0896(01)00277-2
REMARK 1 REFERENCE 2
REMARK 1 AUTH N.G.OIKONOMAKOS,V.T.SKAMNAKI,K.E.TSITSANOU,N.G.GAVALAS,
REMARK 1 AUTH 2 L.N.JOHNSON
REMARK 1 TITL A NEW ALLOSTERIC SITE IN GLYCOGEN PHOSPHORYLASE B AS A
REMARK 1 TITL 2 TARGET FOR DRUG INTERACTIONS
REMARK 1 REF STRUCTURE V. 8 575 2000
REMARK 1 REFN ISSN 0969-2126
REMARK 1 DOI 10.1016/S0969-2126(00)00144-1
REMARK 2
REMARK 2 RESOLUTION. 1.97 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.97
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.71
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 3470156.720
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.6
REMARK 3 NUMBER OF REFLECTIONS : 65858
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.191
REMARK 3 FREE R VALUE : 0.219
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3341
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.97
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.09
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.90
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 10508
REMARK 3 BIN R VALUE (WORKING SET) : 0.2260
REMARK 3 BIN FREE R VALUE : 0.2620
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.10
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 567
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.011
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6546
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 33
REMARK 3 SOLVENT ATOMS : 286
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 17.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.08000
REMARK 3 B22 (A**2) : 2.08000
REMARK 3 B33 (A**2) : -4.16000
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) : 0.21
REMARK 3 ESD FROM SIGMAA (A) : 0.16
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.25
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.20
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.10
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.780
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.390 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.180 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.330 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.570 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.36
REMARK 3 BSOL : 60.47
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1KTI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-JAN-02.
REMARK 100 THE DEPOSITION ID IS D_1000015327.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-APR-01
REMARK 200 TEMPERATURE (KELVIN) : 298.0
REMARK 200 PH : 6.7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : X31
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.05
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 66108
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.970
REMARK 200 RESOLUTION RANGE LOW (A) : 28.800
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.6
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.97
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.04800
REMARK 200 <I/SIGMA(I)> FOR SHELL : 16.70
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: BES, EDTA, 100 MM N-ACETYL-N'-BETA-D
REMARK 280 -GLUCOPYRANOSYL UREA, PH 6.7, SMALL TUBES, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 58.08000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 64.19000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 64.19000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 87.12000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 64.19000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 64.19000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 29.04000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 64.19000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 64.19000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 87.12000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 64.19000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 64.19000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 29.04000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 58.08000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 APPLY THE FOLLOWING TO CHAINS: A
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 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 116.16000
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 SER A 1
REMARK 465 ARG A 2
REMARK 465 PRO A 3
REMARK 465 LEU A 4
REMARK 465 SER 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 LYS A 11
REMARK 465 GLN A 12
REMARK 465 PHE A 252
REMARK 465 ASN A 253
REMARK 465 LEU A 254
REMARK 465 LYS 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 LYS A 315
REMARK 465 PHE A 316
REMARK 465 GLY A 317
REMARK 465 CYS A 318
REMARK 465 ARG A 319
REMARK 465 ASP A 320
REMARK 465 PRO A 321
REMARK 465 VAL A 322
REMARK 465 ARG A 323
REMARK 465 THR A 324
REMARK 465 PRO A 837
REMARK 465 ASP A 838
REMARK 465 GLU A 839
REMARK 465 LYS A 840
REMARK 465 ILE A 841
REMARK 465 PRO A 842
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 SER A 14 172.75 163.38
REMARK 500 ALA A 19 65.98 -111.98
REMARK 500 LEU A 131 40.67 -87.13
REMARK 500 TYR A 203 -135.38 61.62
REMARK 500 SER A 210 -80.15 7.00
REMARK 500 ASN A 270 36.44 -77.03
REMARK 500 ASN A 284 60.04 62.85
REMARK 500 PHE A 285 143.80 -174.04
REMARK 500 ASP A 339 -168.32 73.62
REMARK 500 THR A 466 -96.65 -124.60
REMARK 500 LEU A 492 -70.13 -148.40
REMARK 500 ASP A 514 68.06 -161.34
REMARK 500 LYS A 554 100.67 57.76
REMARK 500 VAL A 555 -5.43 -179.88
REMARK 500 HIS A 556 151.00 55.49
REMARK 500 LYS A 568 166.24 175.76
REMARK 500 SER A 674 -62.66 -144.27
REMARK 500 SER A 751 69.61 -153.89
REMARK 500 LYS A 772 64.61 34.88
REMARK 500 ASN A 793 79.46 -117.15
REMARK 500 ILE A 824 -50.22 -124.71
REMARK 500 PRO A 835 75.17 -49.46
REMARK 500
REMARK 500 REMARK: NULL
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE AUTHORS STATE THAT ACCORDING TO THE
REMARK 999 ELECTRON DENSITY MAP AT 1.97 A RESOLUTION
REMARK 999 RESIDUE 380 IS AN ILE.
DBREF 1KTI A 1 842 UNP P00489 PHS2_RABIT 1 842
SEQADV 1KTI ILE A 380 UNP P00489 LEU 380 SEE REMARK 999
SEQRES 1 A 842 SER ARG PRO LEU SER ASP GLN GLU LYS ARG LYS GLN ILE
SEQRES 2 A 842 SER VAL ARG GLY LEU ALA GLY VAL GLU ASN VAL THR GLU
SEQRES 3 A 842 LEU LYS LYS ASN PHE ASN ARG HIS LEU HIS PHE THR LEU
SEQRES 4 A 842 VAL LYS ASP ARG ASN VAL ALA THR PRO ARG ASP TYR TYR
SEQRES 5 A 842 PHE ALA LEU ALA HIS THR VAL ARG ASP HIS LEU VAL GLY
SEQRES 6 A 842 ARG TRP ILE ARG THR GLN GLN HIS TYR TYR GLU LYS ASP
SEQRES 7 A 842 PRO LYS ARG ILE TYR TYR LEU SER LEU GLU PHE TYR MET
SEQRES 8 A 842 GLY ARG THR LEU GLN ASN THR MET VAL ASN LEU ALA LEU
SEQRES 9 A 842 GLU ASN ALA CYS ASP GLU ALA THR TYR GLN LEU GLY LEU
SEQRES 10 A 842 ASP MET GLU GLU LEU GLU GLU ILE GLU GLU ASP ALA GLY
SEQRES 11 A 842 LEU GLY ASN GLY GLY LEU GLY ARG LEU ALA ALA CYS PHE
SEQRES 12 A 842 LEU ASP SER MET ALA THR LEU GLY LEU ALA ALA TYR GLY
SEQRES 13 A 842 TYR GLY ILE ARG TYR GLU PHE GLY ILE PHE ASN GLN LYS
SEQRES 14 A 842 ILE CYS GLY GLY TRP GLN MET GLU GLU ALA ASP ASP TRP
SEQRES 15 A 842 LEU ARG TYR GLY ASN PRO TRP GLU LYS ALA ARG PRO GLU
SEQRES 16 A 842 PHE THR LEU PRO VAL HIS PHE TYR GLY ARG VAL GLU HIS
SEQRES 17 A 842 THR SER GLN GLY ALA LYS TRP VAL ASP THR GLN VAL VAL
SEQRES 18 A 842 LEU ALA MET PRO TYR ASP THR PRO VAL PRO GLY TYR ARG
SEQRES 19 A 842 ASN ASN VAL VAL ASN THR MET ARG LEU TRP SER ALA LYS
SEQRES 20 A 842 ALA PRO ASN ASP PHE ASN LEU LYS ASP PHE ASN VAL GLY
SEQRES 21 A 842 GLY TYR ILE GLN ALA VAL LEU ASP ARG ASN LEU ALA GLU
SEQRES 22 A 842 ASN ILE SER ARG VAL LEU TYR PRO ASN ASP ASN PHE PHE
SEQRES 23 A 842 GLU GLY LYS GLU LEU ARG LEU LYS GLN GLU TYR PHE VAL
SEQRES 24 A 842 VAL ALA ALA THR LEU GLN ASP ILE ILE ARG ARG PHE LYS
SEQRES 25 A 842 SER SER LYS PHE GLY CYS ARG ASP PRO VAL ARG THR ASN
SEQRES 26 A 842 PHE ASP ALA PHE PRO ASP LYS VAL ALA ILE GLN LEU ASN
SEQRES 27 A 842 ASP THR HIS PRO SER LEU ALA ILE PRO GLU LEU MET ARG
SEQRES 28 A 842 VAL LEU VAL ASP LEU GLU ARG LEU ASP TRP ASP LYS ALA
SEQRES 29 A 842 TRP GLU VAL THR VAL LYS THR CYS ALA TYR THR ASN HIS
SEQRES 30 A 842 THR VAL ILE PRO GLU ALA LEU GLU ARG TRP PRO VAL HIS
SEQRES 31 A 842 LEU LEU GLU THR LEU LEU PRO ARG HIS LEU GLN ILE ILE
SEQRES 32 A 842 TYR GLU ILE ASN GLN ARG PHE LEU ASN ARG VAL ALA ALA
SEQRES 33 A 842 ALA PHE PRO GLY ASP VAL ASP ARG LEU ARG ARG MET SER
SEQRES 34 A 842 LEU VAL GLU GLU GLY ALA VAL LYS ARG ILE ASN MET ALA
SEQRES 35 A 842 HIS LEU CYS ILE ALA GLY SER HIS ALA VAL ASN GLY VAL
SEQRES 36 A 842 ALA ARG ILE HIS SER GLU ILE LEU LYS LYS THR ILE PHE
SEQRES 37 A 842 LYS ASP PHE TYR GLU LEU GLU PRO HIS LYS PHE GLN ASN
SEQRES 38 A 842 LYS THR ASN GLY ILE THR PRO ARG ARG TRP LEU VAL LEU
SEQRES 39 A 842 CYS ASN PRO GLY LEU ALA GLU ILE ILE ALA GLU ARG ILE
SEQRES 40 A 842 GLY GLU GLU TYR ILE SER ASP LEU ASP GLN LEU ARG LYS
SEQRES 41 A 842 LEU LEU SER TYR VAL ASP ASP GLU ALA PHE ILE ARG ASP
SEQRES 42 A 842 VAL ALA LYS VAL LYS GLN GLU ASN LYS LEU LYS PHE ALA
SEQRES 43 A 842 ALA TYR LEU GLU ARG GLU TYR LYS VAL HIS ILE ASN PRO
SEQRES 44 A 842 ASN SER LEU PHE ASP VAL GLN VAL LYS ARG ILE HIS GLU
SEQRES 45 A 842 TYR LYS ARG GLN LEU LEU ASN CYS LEU HIS VAL ILE THR
SEQRES 46 A 842 LEU TYR ASN ARG ILE LYS LYS GLU PRO ASN LYS PHE VAL
SEQRES 47 A 842 VAL PRO ARG THR VAL MET ILE GLY GLY LYS ALA ALA PRO
SEQRES 48 A 842 GLY TYR HIS MET ALA LYS MET ILE ILE LYS LEU ILE THR
SEQRES 49 A 842 ALA ILE GLY ASP VAL VAL ASN HIS ASP PRO VAL VAL GLY
SEQRES 50 A 842 ASP ARG LEU ARG VAL ILE PHE LEU GLU ASN TYR ARG VAL
SEQRES 51 A 842 SER LEU ALA GLU LYS VAL ILE PRO ALA ALA ASP LEU SER
SEQRES 52 A 842 GLU GLN ILE SER THR ALA GLY THR GLU ALA SER GLY THR
SEQRES 53 A 842 GLY ASN MET LYS PHE MET LEU ASN GLY ALA LEU THR ILE
SEQRES 54 A 842 GLY THR MET ASP GLY ALA ASN VAL GLU MET ALA GLU GLU
SEQRES 55 A 842 ALA GLY GLU GLU ASN PHE PHE ILE PHE GLY MET ARG VAL
SEQRES 56 A 842 GLU ASP VAL ASP ARG LEU ASP GLN ARG GLY TYR ASN ALA
SEQRES 57 A 842 GLN GLU TYR TYR ASP ARG ILE PRO GLU LEU ARG GLN ILE
SEQRES 58 A 842 ILE GLU GLN LEU SER SER GLY PHE PHE SER PRO LYS GLN
SEQRES 59 A 842 PRO ASP LEU PHE LYS ASP ILE VAL ASN MET LEU MET HIS
SEQRES 60 A 842 HIS ASP ARG PHE LYS VAL PHE ALA ASP TYR GLU GLU TYR
SEQRES 61 A 842 VAL LYS CYS GLN GLU ARG VAL SER ALA LEU TYR LYS ASN
SEQRES 62 A 842 PRO ARG GLU TRP THR ARG MET VAL ILE ARG ASN ILE ALA
SEQRES 63 A 842 THR SER GLY LYS PHE SER SER ASP ARG THR ILE ALA GLN
SEQRES 64 A 842 TYR ALA ARG GLU ILE TRP GLY VAL GLU PRO SER ARG GLN
SEQRES 65 A 842 ARG LEU PRO ALA PRO ASP GLU LYS ILE PRO
HET AZC A 998 18
HET PLP A 999 15
HETNAM AZC N-(ACETYLCARBAMOYL)-BETA-D-GLUCOPYRANOSYLAMINE
HETNAM PLP PYRIDOXAL-5'-PHOSPHATE
HETSYN PLP VITAMIN B6 PHOSPHATE
FORMUL 2 AZC C9 H16 N2 O7
FORMUL 3 PLP C8 H10 N O6 P
FORMUL 4 HOH *286(H2 O)
HELIX 1 1 GLY A 20 THR A 38 1 19
HELIX 2 2 THR A 47 ASP 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 124 1 7
HELIX 6 6 GLY A 134 LEU A 150 1 17
HELIX 7 7 PRO A 194 THR A 197 5 4
HELIX 8 8 GLY A 261 ASP A 268 1 8
HELIX 9 9 ARG A 269 ARG A 277 5 9
HELIX 10 10 LYS A 289 SER A 314 1 26
HELIX 11 11 ASN A 325 ASP A 327 5 3
HELIX 12 12 ALA A 328 LYS A 332 1 5
HELIX 13 13 LEU A 344 LEU A 356 1 13
HELIX 14 14 ASP A 360 THR A 371 1 12
HELIX 15 16 VAL A 389 LEU A 396 1 8
HELIX 16 17 LEU A 396 PHE A 418 1 23
HELIX 17 18 ASP A 421 SER A 429 1 9
HELIX 18 19 MET A 441 GLY A 448 1 8
HELIX 19 20 ALA A 456 THR A 466 1 11
HELIX 20 21 PHE A 468 GLU A 475 1 8
HELIX 21 22 ASN A 496 GLY A 508 1 13
HELIX 22 23 GLU A 509 VAL A 525 5 17
HELIX 23 24 ASP A 527 TYR A 553 1 27
HELIX 24 25 HIS A 571 LYS A 574 5 4
HELIX 25 26 ARG A 575 GLU A 593 1 19
HELIX 26 27 TYR A 613 ASN A 631 1 19
HELIX 27 28 ARG A 649 ILE A 657 1 9
HELIX 28 29 PRO A 658 ALA A 660 5 3
HELIX 29 30 THR A 676 ASN A 684 1 9
HELIX 30 31 ALA A 695 GLY A 704 1 10
HELIX 31 32 GLU A 705 PHE A 708 5 4
HELIX 32 33 ARG A 714 GLY A 725 1 12
HELIX 33 34 ASN A 727 ILE A 735 1 9
HELIX 34 35 ILE A 735 GLY A 748 1 14
HELIX 35 36 PHE A 758 HIS A 768 1 11
HELIX 36 37 LYS A 772 LYS A 792 1 21
HELIX 37 38 ASN A 793 THR A 807 1 15
HELIX 38 39 SER A 808 PHE A 811 5 4
HELIX 39 40 SER A 812 ILE A 824 1 13
SHEET 1 A 9 PHE A 479 ASN A 481 0
SHEET 2 A 9 ALA A 451 GLY A 454 1 N VAL A 452 O GLN A 480
SHEET 3 A 9 CYS A 372 THR A 375 1 N TYR A 374 O ALA A 451
SHEET 4 A 9 VAL A 333 ASN A 338 1 N LEU A 337 O ALA A 373
SHEET 5 A 9 ARG A 81 LEU A 85 1 N TYR A 83 O ALA A 334
SHEET 6 A 9 ALA A 154 ILE A 159 1 O TYR A 155 N ILE A 82
SHEET 7 A 9 VAL A 238 LYS A 247 1 O ARG A 242 N GLY A 156
SHEET 8 A 9 GLN A 219 PRO A 231 -1 N MET A 224 O SER A 245
SHEET 9 A 9 LYS A 191 ALA A 192 -1 N LYS A 191 O ASP A 227
SHEET 1 B 9 PHE A 479 ASN A 481 0
SHEET 2 B 9 ALA A 451 GLY A 454 1 N VAL A 452 O GLN A 480
SHEET 3 B 9 CYS A 372 THR A 375 1 N TYR A 374 O ALA A 451
SHEET 4 B 9 VAL A 333 ASN A 338 1 N LEU A 337 O ALA A 373
SHEET 5 B 9 ARG A 81 LEU A 85 1 N TYR A 83 O ALA A 334
SHEET 6 B 9 ALA A 154 ILE A 159 1 O TYR A 155 N ILE A 82
SHEET 7 B 9 VAL A 238 LYS A 247 1 O ARG A 242 N GLY A 156
SHEET 8 B 9 GLN A 219 PRO A 231 -1 N MET A 224 O SER A 245
SHEET 9 B 9 LEU A 198 PHE A 202 -1 N LEU A 198 O ALA A 223
SHEET 1 C 2 PHE A 89 GLY A 92 0
SHEET 2 C 2 ALA A 129 LEU A 131 -1 O LEU A 131 N PHE A 89
SHEET 1 D 2 ASN A 167 CYS A 171 0
SHEET 2 D 2 TRP A 174 GLU A 178 -1 O MET A 176 N LYS A 169
SHEET 1 E 2 ARG A 205 HIS A 208 0
SHEET 2 E 2 ALA A 213 VAL A 216 -1 O LYS A 214 N GLU A 207
SHEET 1 F 3 ARG A 386 PRO A 388 0
SHEET 2 F 3 ARG A 438 ASN A 440 -1 O ILE A 439 N TRP A 387
SHEET 3 F 3 VAL A 431 GLU A 432 -1 N GLU A 432 O ARG A 438
SHEET 1 G 6 LEU A 640 LEU A 645 0
SHEET 2 G 6 ARG A 601 GLY A 606 1 N VAL A 603 O ARG A 641
SHEET 3 G 6 LEU A 562 VAL A 567 1 N ASP A 564 O MET A 604
SHEET 4 G 6 LEU A 662 GLN A 665 1 O LEU A 662 N VAL A 565
SHEET 5 G 6 LEU A 687 GLY A 690 1 O LEU A 687 N SER A 663
SHEET 6 G 6 PHE A 709 ILE A 710 1 O PHE A 709 N GLY A 690
LINK NZ LYS A 680 C4A PLP A 999 1555 1555 1.35
CRYST1 128.380 128.380 116.160 90.00 90.00 90.00 P 43 21 2 8
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 0.007789 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007789 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008609 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
