HEADER TRANSFERASE/TRANSFERASE INHIBITOR 29-APR-10 3MRX
TITLE GLYCOGEN PHOSPHORYLASE COMPLEXED WITH 4-METHOXYBENZALDEHYDE-4-(2,3,4,
TITLE 2 6-TETRA-O-ACETYL-BETA-D-GLUCOPYRANOSYL)-THIOSEMICARBAZONE
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: EUROPEAN RABBIT,JAPANESE WHITE RABBIT,DOMESTIC
SOURCE 4 RABBIT,RABBITS;
SOURCE 5 ORGANISM_TAXID: 9986;
SOURCE 6 OTHER_DETAILS: MUSCLE
KEYWDS GLYCOGENOLYSIS, TYPE 2 DIABETES, TRANSFERASE-TRANSFERASE INHIBITOR
KEYWDS 2 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR K.-M.ALEXACOU
REVDAT 4 22-NOV-23 3MRX 1 REMARK
REVDAT 3 06-SEP-23 3MRX 1 REMARK
REVDAT 2 17-JUL-19 3MRX 1 REMARK LINK
REVDAT 1 05-JAN-11 3MRX 0
JRNL AUTH K.M.ALEXACOU,A.C.TENCHIU DELEANU,E.D.CHRYSINA,M.D.CHARAVGI,
JRNL AUTH 2 I.D.KOSTAS,S.E.ZOGRAPHOS,N.G.OIKONOMAKOS,D.D.LEONIDAS
JRNL TITL THE BINDING OF BETA-D-GLUCOPYRANOSYL-THIOSEMICARBAZONE
JRNL TITL 2 DERIVATIVES TO GLYCOGEN PHOSPHORYLASE: A NEW CLASS OF
JRNL TITL 3 INHIBITORS
JRNL REF BIOORG.MED.CHEM. V. 18 7911 2010
JRNL REFN ISSN 0968-0896
JRNL PMID 20947361
JRNL DOI 10.1016/J.BMC.2010.09.039
REMARK 2
REMARK 2 RESOLUTION. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 31.11
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 3 NUMBER OF REFLECTIONS : 65522
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) : 0.184
REMARK 3 R VALUE (WORKING SET) : 0.182
REMARK 3 FREE R VALUE : 0.216
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3490
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) : 1.95
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.00
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4753
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.53
REMARK 3 BIN R VALUE (WORKING SET) : 0.2280
REMARK 3 BIN FREE R VALUE SET COUNT : 222
REMARK 3 BIN FREE R VALUE : 0.2840
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6608
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 50
REMARK 3 SOLVENT ATOMS : 324
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.84
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.05000
REMARK 3 B22 (A**2) : 0.05000
REMARK 3 B33 (A**2) : -0.11000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.157
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.141
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.094
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.268
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.962
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.948
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6830 ; 0.009 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9249 ; 1.150 ; 1.959
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 812 ; 5.472 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 350 ;34.093 ;23.543
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1180 ;15.636 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 59 ;19.727 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1000 ; 0.086 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5241 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 3050 ; 0.181 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4647 ; 0.304 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 387 ; 0.098 ; 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): 41 ; 0.144 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 8 ; 0.104 ; 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): 4044 ; 0.632 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6531 ; 1.231 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2786 ; 1.826 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2716 ; 3.113 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 : 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 3MRX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-MAY-10.
REMARK 100 THE DEPOSITION ID IS D_1000058923.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-NOV-07
REMARK 200 TEMPERATURE (KELVIN) : 293
REMARK 200 PH : 6.7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SRS
REMARK 200 BEAMLINE : PX10.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.04498
REMARK 200 MONOCHROMATOR : CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 69032
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
REMARK 200 RESOLUTION RANGE LOW (A) : 35.580
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 200 DATA REDUNDANCY : 5.000
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.06
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.2
REMARK 200 DATA REDUNDANCY IN SHELL : 4.90
REMARK 200 R MERGE FOR SHELL (I) : 0.36600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.000
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: PDB ENTRY 2PRJ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.77
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.45
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20 MG/ML OF PROTEIN IN A BUFFER
REMARK 280 SOLUTION CONTAINING 10 MM BES PH 6.7, 1 MM EDTA AND 3 MM DTT.
REMARK 280 6.7MM INHIBITOR IN 20% DMSO SOAKED WITH NATIVE CRYSTALS FOR 3
REMARK 280 HRS, 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 58.02500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 64.15500
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 64.15500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 87.03750
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 64.15500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 64.15500
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 29.01250
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 64.15500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 64.15500
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 87.03750
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 64.15500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 64.15500
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 29.01250
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 58.02500
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: 4840 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 56250 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL
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 116.05000
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 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 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 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: 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 ARG A 138 NE - CZ - NH1 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ARG A 138 NE - CZ - NH2 ANGL. DEV. = 3.7 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 ALA A 19 73.32 -110.33
REMARK 500 LEU A 131 40.69 -89.45
REMARK 500 TYR A 203 -138.34 60.58
REMARK 500 GLN A 211 39.03 -98.62
REMARK 500 SER A 313 33.57 -82.96
REMARK 500 ASP A 339 -164.70 65.59
REMARK 500 THR A 466 -87.78 -121.52
REMARK 500 LEU A 492 -64.13 -143.51
REMARK 500 ASP A 514 73.83 -152.28
REMARK 500 LYS A 568 164.21 167.95
REMARK 500 SER A 674 -59.30 -137.38
REMARK 500 HIS A 768 52.79 -144.28
REMARK 500 HIS A 768 45.63 -140.44
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 A1146 DISTANCE = 7.46 ANGSTROMS
REMARK 525 HOH A1164 DISTANCE = 11.34 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 17S A 920
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 17S A 998
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3MQF RELATED DB: PDB
REMARK 900 RELATED ID: 3MRT RELATED DB: PDB
REMARK 900 RELATED ID: 3MRV RELATED DB: PDB
REMARK 900 RELATED ID: 3MS2 RELATED DB: PDB
REMARK 900 RELATED ID: 3MS4 RELATED DB: PDB
REMARK 900 RELATED ID: 3MS7 RELATED DB: PDB
REMARK 900 RELATED ID: 3MSC RELATED DB: PDB
REMARK 900 RELATED ID: 3MT7 RELATED DB: PDB
REMARK 900 RELATED ID: 3MT8 RELATED DB: PDB
REMARK 900 RELATED ID: 3MT9 RELATED DB: PDB
REMARK 900 RELATED ID: 3MTA RELATED DB: PDB
REMARK 900 RELATED ID: 3MTB RELATED DB: PDB
REMARK 900 RELATED ID: 3MTD RELATED DB: PDB
DBREF 3MRX A 1 842 UNP P00489 PYGM_RABIT 2 843
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 LEU 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 LLP 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
MODRES 3MRX LLP A 680 LYS
HET LLP A 680 24
HET 17S A 920 25
HET 17S A 998 25
HETNAM LLP (2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-
HETNAM 2 LLP (PHOSPHONOOXYMETHYL)PYRIDIN-4-
HETNAM 3 LLP YL]METHYLIDENEAMINO]HEXANOIC ACID
HETNAM 17S N-({(2E)-2-[(4-METHOXYPHENYL)
HETNAM 2 17S METHYLIDENE]HYDRAZINO}CARBONOTHIOYL)-BETA-D-
HETNAM 3 17S GLUCOPYRANOSYLAMINE
HETSYN LLP N'-PYRIDOXYL-LYSINE-5'-MONOPHOSPHATE
HETSYN 17S 4-METHOXYBENZALDEHYDE-4-(BETA-D-GLUCOPYRANOSYL)
HETSYN 2 17S THIOSEMICARBAZONE
FORMUL 1 LLP C14 H22 N3 O7 P
FORMUL 2 17S 2(C15 H21 N3 O6 S)
FORMUL 4 HOH *324(H2 O)
HELIX 1 1 ILE A 13 GLY A 17 5 5
HELIX 2 2 GLY A 20 THR A 38 1 19
HELIX 3 3 THR A 47 ASP 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 THR A 197 5 4
HELIX 9 9 GLY A 260 ASP A 268 1 9
HELIX 10 10 ASP A 268 ASN A 274 1 7
HELIX 11 11 ILE A 275 ARG A 277 5 3
HELIX 12 12 LYS A 289 SER A 313 1 25
HELIX 13 13 ASN A 325 ASP A 327 5 3
HELIX 14 14 ALA A 328 LYS A 332 1 5
HELIX 15 15 LEU A 344 LEU A 356 1 13
HELIX 16 16 ASP 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 THR A 466 1 11
HELIX 23 23 PHE A 468 GLU A 475 1 8
HELIX 24 24 THR A 487 LEU A 492 1 6
HELIX 25 25 ASN A 496 GLY A 508 1 13
HELIX 26 26 GLU A 509 VAL A 525 5 17
HELIX 27 27 ASP A 527 LYS A 554 1 28
HELIX 28 28 ARG A 575 GLU A 593 1 19
HELIX 29 29 TYR A 613 ASN A 631 1 19
HELIX 30 30 ARG A 649 ALA A 660 1 12
HELIX 31 31 THR A 676 ASN A 684 1 9
HELIX 32 32 ALA A 695 GLY A 704 1 10
HELIX 33 33 GLU A 705 PHE A 708 5 4
HELIX 34 34 ARG A 714 GLY A 725 1 12
HELIX 35 35 ASN A 727 ILE A 735 1 9
HELIX 36 36 ILE A 735 GLY A 748 1 14
HELIX 37 37 PHE A 758 HIS A 768 1 11
HELIX 38 38 VAL A 773 ALA A 775 5 3
HELIX 39 39 ASP A 776 LYS A 792 1 17
HELIX 40 40 ASN A 793 THR A 807 1 15
HELIX 41 41 SER A 808 PHE A 811 5 4
HELIX 42 42 SER A 812 ILE A 824 1 13
SHEET 1 A 3 LYS A 191 ALA 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 LEU A 198 O ALA A 223
SHEET 1 B 9 LYS A 191 ALA 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 LYS A 247 -1 O SER A 245 N MET 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 CYS 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 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 THR A 209 0
SHEET 2 E 2 GLY A 212 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 THR A 688
LINK C MET A 679 N LLP A 680 1555 1555 1.34
LINK C LLP A 680 N PHE A 681 1555 1555 1.34
SITE 1 AC1 15 PHE A 37 THR A 38 VAL A 40 ARG A 60
SITE 2 AC1 15 LEU A 63 VAL A 64 TRP A 67 GLU A 190
SITE 3 AC1 15 LYS A 191 ALA A 192 TYR A 226 PRO A 229
SITE 4 AC1 15 HOH A 894 HOH A 896 HOH A 897
SITE 1 AC2 17 GLU A 88 ASN A 133 GLY A 135 LEU A 136
SITE 2 AC2 17 ASN A 282 HIS A 341 HIS A 377 ASN A 484
SITE 3 AC2 17 TYR A 573 GLU A 672 ALA A 673 SER A 674
SITE 4 AC2 17 GLY A 675 HOH A 926 HOH A 927 HOH A 990
SITE 5 AC2 17 HOH A 991
CRYST1 128.310 128.310 116.050 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 0.007794 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007794 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008617 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
