HEADER MEMBRANE PROTEIN 29-NOV-16 5U1U
TITLE CRYSTAL STRUCTURE OF THE ATP-GATED P2X7 ION CHANNEL BOUND TO
TITLE 2 ALLOSTERIC ANTAGONIST A740003
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: P2X PURINOCEPTOR;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 OTHER_DETAILS: BOTH THE N- AND C-TERMINI ARE DISORDERED AND THE
COMPND 6 ELECTRON DENSITY WAS NOT WELL-DEFINED.
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: AILUROPODA MELANOLEUCA;
SOURCE 3 ORGANISM_COMMON: GIANT PANDA;
SOURCE 4 ORGANISM_TAXID: 9646;
SOURCE 5 GENE: P2RX7;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS MEMBRANE PROTEIN: ATP-GATED ION CHANNEL: ALLOSTERIC ANTAGONIST BOUND:
KEYWDS 2 CLOSED STATE, MEMBRANE PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR A.KARASAWA,T.KAWATE
REVDAT 5 04-OCT-23 5U1U 1 HETSYN
REVDAT 4 29-JUL-20 5U1U 1 COMPND REMARK HETNAM LINK
REVDAT 4 2 1 SITE
REVDAT 3 18-DEC-19 5U1U 1 REMARK
REVDAT 2 20-SEP-17 5U1U 1 REMARK
REVDAT 1 11-JAN-17 5U1U 0
JRNL AUTH A.KARASAWA,T.KAWATE
JRNL TITL STRUCTURAL BASIS FOR SUBTYPE-SPECIFIC INHIBITION OF THE P2X7
JRNL TITL 2 RECEPTOR.
JRNL REF ELIFE V. 5 2016
JRNL REFN ESSN 2050-084X
JRNL PMID 27935479
JRNL DOI 10.7554/ELIFE.22153
REMARK 2
REMARK 2 RESOLUTION. 3.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.10_2155
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.32
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 9512
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.236
REMARK 3 R VALUE (WORKING SET) : 0.233
REMARK 3 FREE R VALUE : 0.261
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.800
REMARK 3 FREE R VALUE TEST SET COUNT : 1027
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 45.3220 - 6.8867 0.99 1287 129 0.2386 0.2209
REMARK 3 2 6.8867 - 5.4692 1.00 1181 175 0.2311 0.2600
REMARK 3 3 5.4692 - 4.7787 1.00 1231 141 0.2024 0.2403
REMARK 3 4 4.7787 - 4.3422 1.00 1180 161 0.1900 0.2629
REMARK 3 5 4.3422 - 4.0312 1.00 1209 147 0.2524 0.2880
REMARK 3 6 4.0312 - 3.7936 1.00 1184 150 0.2698 0.2965
REMARK 3 7 3.7936 - 3.6037 0.98 1213 124 0.2923 0.3554
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.540
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.480
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 106.6
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 97.84
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.003 2449
REMARK 3 ANGLE : 0.661 3352
REMARK 3 CHIRALITY : 0.046 377
REMARK 3 PLANARITY : 0.004 438
REMARK 3 DIHEDRAL : 12.111 1410
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5U1U COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-DEC-16.
REMARK 100 THE DEPOSITION ID IS D_1000225167.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-APR-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0-7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-E
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XSCALE
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.5.1, XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 9537
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.600
REMARK 200 RESOLUTION RANGE LOW (A) : 45.320
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 11.00
REMARK 200 R MERGE (I) : 0.22800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 11.10
REMARK 200 R MERGE FOR SHELL (I) : 1.24300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 4DW0
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 76.52
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.24
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM HEPES OR TRIS (PH 6.0-7.5), 100
REMARK 280 MM NACL, 4% ETHYLENE GLYCOL, 15% GLYCEROL, 27-32% PEG-400 OR 31-
REMARK 280 36% PEG-300, 0.1 MG/ML LIPID MIXTURE (60% POPE, 20% POPG, AND 20%
REMARK 280 CHOLESTEROL), AND 1 MM A740003, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 21 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290 5555 Z,X,Y
REMARK 290 6555 Z+1/2,-X+1/2,-Y
REMARK 290 7555 -Z+1/2,-X,Y+1/2
REMARK 290 8555 -Z,X+1/2,-Y+1/2
REMARK 290 9555 Y,Z,X
REMARK 290 10555 -Y,Z+1/2,-X+1/2
REMARK 290 11555 Y+1/2,-Z+1/2,-X
REMARK 290 12555 -Y+1/2,-Z,X+1/2
REMARK 290 13555 X+1/2,Y+1/2,Z+1/2
REMARK 290 14555 -X,-Y+1/2,Z
REMARK 290 15555 -X+1/2,Y,-Z
REMARK 290 16555 X,-Y,-Z+1/2
REMARK 290 17555 Z+1/2,X+1/2,Y+1/2
REMARK 290 18555 Z,-X,-Y+1/2
REMARK 290 19555 -Z,-X+1/2,Y
REMARK 290 20555 -Z+1/2,X,-Y
REMARK 290 21555 Y+1/2,Z+1/2,X+1/2
REMARK 290 22555 -Y+1/2,Z,-X
REMARK 290 23555 Y,-Z,-X+1/2
REMARK 290 24555 -Y,-Z+1/2,X
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 84.78300
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 84.78300
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 84.78300
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 84.78300
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 84.78300
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 84.78300
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 84.78300
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 84.78300
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 84.78300
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 84.78300
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 84.78300
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 84.78300
REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 84.78300
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 84.78300
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 84.78300
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 84.78300
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 84.78300
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 84.78300
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 84.78300
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 84.78300
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 84.78300
REMARK 290 SMTRY1 14 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 84.78300
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 15 -1.000000 0.000000 0.000000 84.78300
REMARK 290 SMTRY2 15 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 16 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 16 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 84.78300
REMARK 290 SMTRY1 17 0.000000 0.000000 1.000000 84.78300
REMARK 290 SMTRY2 17 1.000000 0.000000 0.000000 84.78300
REMARK 290 SMTRY3 17 0.000000 1.000000 0.000000 84.78300
REMARK 290 SMTRY1 18 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 18 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 18 0.000000 -1.000000 0.000000 84.78300
REMARK 290 SMTRY1 19 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 19 -1.000000 0.000000 0.000000 84.78300
REMARK 290 SMTRY3 19 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 20 0.000000 0.000000 -1.000000 84.78300
REMARK 290 SMTRY2 20 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 20 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 21 0.000000 1.000000 0.000000 84.78300
REMARK 290 SMTRY2 21 0.000000 0.000000 1.000000 84.78300
REMARK 290 SMTRY3 21 1.000000 0.000000 0.000000 84.78300
REMARK 290 SMTRY1 22 0.000000 -1.000000 0.000000 84.78300
REMARK 290 SMTRY2 22 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 22 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 23 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 23 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 23 -1.000000 0.000000 0.000000 84.78300
REMARK 290 SMTRY1 24 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 24 0.000000 0.000000 -1.000000 84.78300
REMARK 290 SMTRY3 24 1.000000 0.000000 0.000000 0.00000
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 13220 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 42960 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 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 0.000000 1.000000 0.00000
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT1 3 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT3 3 1.000000 0.000000 0.000000 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 21
REMARK 465 SER A 22
REMARK 465 SER A 23
REMARK 465 THR A 24
REMARK 465 ASN A 25
REMARK 465 TYR A 26
REMARK 465 GLY A 27
REMARK 465 THR A 28
REMARK 465 ILE A 29
REMARK 465 LYS A 30
REMARK 465 TRP A 31
REMARK 465 ILE A 32
REMARK 465 PHE A 33
REMARK 465 THR A 348
REMARK 465 VAL A 349
REMARK 465 PHE A 350
REMARK 465 ILE A 351
REMARK 465 ASP A 352
REMARK 465 ILE A 353
REMARK 465 LEU A 354
REMARK 465 ILE A 355
REMARK 465 ASN A 356
REMARK 465 THR A 357
REMARK 465 TYR A 358
REMARK 465 SER A 359
REMARK 465 ALA A 360
REMARK 465 SER A 361
REMARK 465 SER A 362
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 HIS A 34 CG ND1 CD2 CE1 NE2
REMARK 470 LEU A 36 CG CD1 CD2
REMARK 470 VAL A 37 CG1 CG2
REMARK 470 TYR A 40 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 SER A 47 OG
REMARK 470 LYS A 49 CG CD CE NZ
REMARK 470 LYS A 53 CG CD CE NZ
REMARK 470 LYS A 54 CG CD CE NZ
REMARK 470 GLU A 55 CG CD OE1 OE2
REMARK 470 LYS A 64 CG CD CE NZ
REMARK 470 LYS A 66 CG CD CE NZ
REMARK 470 LYS A 72 CG CD CE NZ
REMARK 470 GLU A 74 CG CD OE1 OE2
REMARK 470 LEU A 76 CG CD1 CD2
REMARK 470 MET A 80 CG SD CE
REMARK 470 LYS A 81 CG CD CE NZ
REMARK 470 LYS A 82 CG CD CE NZ
REMARK 470 ARG A 126 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 133 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 136 CG CD CE NZ
REMARK 470 LYS A 137 CG CD CE NZ
REMARK 470 ARG A 139 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 143 CG CD OE1 NE2
REMARK 470 LYS A 156 CG CD CE NZ
REMARK 470 ARG A 158 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 174 CG CD CE NZ
REMARK 470 ARG A 178 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 209 CG CD1 CD2
REMARK 470 ILE A 214 CG1 CG2 CD1
REMARK 470 LYS A 220 CG CD CE NZ
REMARK 470 THR A 221 OG1 CG2
REMARK 470 GLN A 222 CG CD OE1 NE2
REMARK 470 GLN A 236 CG CD OE1 NE2
REMARK 470 LEU A 262 CG CD1 CD2
REMARK 470 PHE A 266 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 HIS A 268 CG ND1 CD2 CE1 NE2
REMARK 470 LYS A 272 CG CD CE NZ
REMARK 470 LYS A 281 CG CD CE NZ
REMARK 470 THR A 282 OG1 CG2
REMARK 470 THR A 283 OG1 CG2
REMARK 470 GLU A 285 CG CD OE1 OE2
REMARK 470 LEU A 287 CG CD1 CD2
REMARK 470 LYS A 297 CG CD CE NZ
REMARK 470 LYS A 300 CG CD CE NZ
REMARK 470 LYS A 327 CG CD CE NZ
REMARK 470 PHE A 328 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASN A 329 CG OD1 ND2
REMARK 470 VAL A 330 CG1 CG2
REMARK 470 PHE A 344 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU A 346 CG CD1 CD2
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 A 207 OH TYR A 273 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O GLY A 338 OG SER A 342 5555 2.01
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 CYS A 119 138.61 -174.62
REMARK 500 ALA A 166 -167.46 -169.94
REMARK 500 LEU A 182 57.91 -97.49
REMARK 500 SER A 184 5.00 -68.34
REMARK 500 TYR A 288 73.57 52.41
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5U1L RELATED DB: PDB
REMARK 900 RELATED ID: 5U1V RELATED DB: PDB
REMARK 900 RELATED ID: 5U1W RELATED DB: PDB
REMARK 900 RELATED ID: 5U1X RELATED DB: PDB
REMARK 900 RELATED ID: 5U1Y RELATED DB: PDB
REMARK 900 RELATED ID: 5U2H RELATED DB: PDB
DBREF 5U1U A 23 358 UNP G1M6C4 G1M6C4_AILME 24 359
SEQADV 5U1U GLY A 21 UNP G1M6C4 EXPRESSION TAG
SEQADV 5U1U SER A 22 UNP G1M6C4 EXPRESSION TAG
SEQADV 5U1U ALA A 35 UNP G1M6C4 VAL 36 ENGINEERED MUTATION
SEQADV 5U1U ALA A 125 UNP G1M6C4 ARG 126 ENGINEERED MUTATION
SEQADV 5U1U LYS A 174 UNP G1M6C4 GLU 175 ENGINEERED MUTATION
SEQADV 5U1U SER A 241 UNP G1M6C4 ASN 242 ENGINEERED MUTATION
SEQADV 5U1U SER A 284 UNP G1M6C4 ASN 285 ENGINEERED MUTATION
SEQADV 5U1U SER A 359 UNP G1M6C4 EXPRESSION TAG
SEQADV 5U1U ALA A 360 UNP G1M6C4 EXPRESSION TAG
SEQADV 5U1U SER A 361 UNP G1M6C4 EXPRESSION TAG
SEQADV 5U1U SER A 362 UNP G1M6C4 EXPRESSION TAG
SEQRES 1 A 342 GLY SER SER THR ASN TYR GLY THR ILE LYS TRP ILE PHE
SEQRES 2 A 342 HIS ALA LEU VAL PHE SER TYR ILE SER PHE ALA LEU ILE
SEQRES 3 A 342 SER ASP LYS ARG TYR GLN LYS LYS GLU PRO LEU ILE SER
SEQRES 4 A 342 SER VAL HIS THR LYS VAL LYS GLY ILE ALA GLU VAL LYS
SEQRES 5 A 342 ALA GLU ILE LEU GLU ASN GLY MET LYS LYS MET VAL SER
SEQRES 6 A 342 GLY VAL PHE ASP THR ALA ASP TYR THR PHE PRO LEU GLN
SEQRES 7 A 342 GLY ASN SER PHE PHE VAL MET THR ASN PHE ILE LYS THR
SEQRES 8 A 342 GLU GLY GLN GLN GLN GLY LEU CYS PRO ASP PHE PRO THR
SEQRES 9 A 342 ALA ARG THR ILE CYS SER SER ASP ARG GLY CYS LYS LYS
SEQRES 10 A 342 GLY ARG MET ASP PRO GLN SER LYS GLY ILE GLN THR GLY
SEQRES 11 A 342 ARG CYS VAL VAL TYR LYS GLU ARG LEU LYS THR CYS GLU
SEQRES 12 A 342 VAL SER ALA TRP CYS PRO ILE GLU GLU VAL LYS ASP ALA
SEQRES 13 A 342 PRO ARG PRO ALA LEU LEU ASN SER ALA GLU ASN PHE THR
SEQRES 14 A 342 VAL LEU ILE LYS ASN ASN ILE ASP PHE PRO GLY HIS ASN
SEQRES 15 A 342 TYR THR THR ARG ASN ILE LEU PRO GLY VAL ASN ILE THR
SEQRES 16 A 342 CYS THR PHE HIS LYS THR GLN ASN PRO GLN CYS PRO ILE
SEQRES 17 A 342 PHE ARG LEU GLY ASP ILE PHE GLN GLU THR GLY ASP SER
SEQRES 18 A 342 PHE SER ASP VAL ALA ILE GLN GLY GLY ILE MET GLY ILE
SEQRES 19 A 342 GLU ILE TYR TRP ASP CYS ASN LEU ASP GLY TRP PHE HIS
SEQRES 20 A 342 HIS CYS ARG PRO LYS TYR SER PHE ARG ARG LEU ASP ASP
SEQRES 21 A 342 LYS THR THR SER GLU SER LEU TYR PRO GLY TYR ASN PHE
SEQRES 22 A 342 ARG TYR ALA LYS TYR TYR LYS GLU ASN ASN VAL GLU LYS
SEQRES 23 A 342 ARG THR LEU ILE LYS VAL PHE GLY ILE ARG PHE ASP ILE
SEQRES 24 A 342 LEU VAL PHE GLY THR GLY GLY LYS PHE ASN VAL ILE GLN
SEQRES 25 A 342 LEU ALA VAL TYR ILE GLY SER VAL ILE SER TYR PHE GLY
SEQRES 26 A 342 LEU ALA THR VAL PHE ILE ASP ILE LEU ILE ASN THR TYR
SEQRES 27 A 342 SER ALA SER SER
HET NAG A 401 14
HET NAG A 402 14
HET NAG A 403 14
HET 7S4 A 404 35
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM 7S4 N-{(1R)-1-[N''-CYANO-N'-(QUINOLIN-5-YL)
HETNAM 2 7S4 CARBAMIMIDAMIDO]-2,2-DIMETHYLPROPYL}-2-(3,4-
HETNAM 3 7S4 DIMETHOXYPHENYL)ACETAMIDE
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN 7S4 ANTAGONIST A740003
FORMUL 2 NAG 3(C8 H15 N O6)
FORMUL 5 7S4 C26 H30 N6 O3
HELIX 1 AA1 HIS A 34 LYS A 49 1 16
HELIX 2 AA2 ASP A 89 THR A 94 1 6
HELIX 3 AA3 SER A 131 CYS A 135 5 5
HELIX 4 AA4 LEU A 182 ASN A 187 5 6
HELIX 5 AA5 LEU A 231 THR A 238 1 8
HELIX 6 AA6 SER A 241 GLY A 249 1 9
HELIX 7 AA7 SER A 284 TYR A 288 5 5
HELIX 8 AA8 ASN A 329 ALA A 347 1 19
SHEET 1 AA1 4 GLN A 52 GLU A 55 0
SHEET 2 AA1 4 VAL A 304 PHE A 328 -1 O LYS A 327 N LYS A 53
SHEET 3 AA1 4 GLY A 250 ASN A 261 1 N ILE A 254 O LEU A 320
SHEET 4 AA1 4 HIS A 268 ARG A 277 -1 O SER A 274 N GLU A 255
SHEET 1 AA2 5 ILE A 147 VAL A 154 0
SHEET 2 AA2 5 LYS A 160 CYS A 168 -1 O GLU A 163 N THR A 149
SHEET 3 AA2 5 SER A 101 PRO A 120 -1 N CYS A 119 O VAL A 164
SHEET 4 AA2 5 VAL A 304 PHE A 328 -1 O ARG A 307 N GLN A 114
SHEET 5 AA2 5 ASN A 292 GLU A 301 -1 N PHE A 293 O VAL A 312
SHEET 1 AA3 3 ILE A 58 LYS A 66 0
SHEET 2 AA3 3 THR A 189 PHE A 198 -1 O THR A 189 N LYS A 66
SHEET 3 AA3 3 TYR A 203 ARG A 206 -1 O THR A 205 N ILE A 196
SHEET 1 AA4 3 ILE A 58 LYS A 66 0
SHEET 2 AA4 3 THR A 189 PHE A 198 -1 O THR A 189 N LYS A 66
SHEET 3 AA4 3 ILE A 228 ARG A 230 -1 O PHE A 229 N VAL A 190
SHEET 1 AA5 2 ALA A 69 GLU A 77 0
SHEET 2 AA5 2 MET A 80 PHE A 88 -1 O GLY A 86 N VAL A 71
SSBOND 1 CYS A 119 CYS A 168 1555 1555 2.01
SSBOND 2 CYS A 129 CYS A 152 1555 1555 2.03
SSBOND 3 CYS A 135 CYS A 162 1555 1555 2.03
SSBOND 4 CYS A 216 CYS A 226 1555 1555 2.03
SSBOND 5 CYS A 260 CYS A 269 1555 1555 2.03
LINK ND2 ASN A 187 C1 NAG A 401 1555 1555 1.44
LINK ND2 ASN A 202 C1 NAG A 402 1555 1555 1.44
LINK ND2 ASN A 213 C1 NAG A 403 1555 1555 1.44
CISPEP 1 CYS A 168 PRO A 169 0 4.09
CRYST1 169.566 169.566 169.566 90.00 90.00 90.00 I 21 3 24
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 0.005897 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005897 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005897 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
