HEADER PROTEIN TRANSPORT 23-MAR-11 3R7W
TITLE CRYSTAL STRUCTURE OF GTR1P-GTR2P COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GTP-BINDING PROTEIN GTR1;
COMPND 3 CHAIN: A, C;
COMPND 4 FRAGMENT: RESIDUES 8-310;
COMPND 5 SYNONYM: GTPASE1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: GTP-BINDING PROTEIN GTR2;
COMPND 9 CHAIN: B, D;
COMPND 10 FRAGMENT: RESIDUES 11-341;
COMPND 11 SYNONYM: GTPASE2;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 GENE: GTR1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PETDUET1;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 13 ORGANISM_COMMON: YEAST;
SOURCE 14 ORGANISM_TAXID: 4932;
SOURCE 15 GENE: GTR2;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PETDUET1
KEYWDS RAG GTPASES, GTR1P, GTR2P, MTOR, PROTEIN TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR R.GONG,L.LI,Y.LIU,P.WANG,H.YANG,L.WANG,J.CHENG,K.L.GUAN,Y.XU
REVDAT 2 19-JUN-13 3R7W 1 JRNL
REVDAT 1 24-AUG-11 3R7W 0
JRNL AUTH R.GONG,L.LI,Y.LIU,P.WANG,H.YANG,L.WANG,J.CHENG,K.L.GUAN,Y.XU
JRNL TITL CRYSTAL STRUCTURE OF THE GTR1P-GTR2P COMPLEX REVEALS NEW
JRNL TITL 2 INSIGHTS INTO THE AMINO ACID-INDUCED TORC1 ACTIVATION
JRNL REF GENES DEV. V. 25 1668 2011
JRNL REFN ISSN 0890-9369
JRNL PMID 21816923
JRNL DOI 10.1101/GAD.16968011
REMARK 2
REMARK 2 RESOLUTION. 2.77 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7_650)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.77
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.06
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.0
REMARK 3 NUMBER OF REFLECTIONS : 46857
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.238
REMARK 3 R VALUE (WORKING SET) : 0.236
REMARK 3 FREE R VALUE : 0.283
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.880
REMARK 3 FREE R VALUE TEST SET COUNT : 2288
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 44.0656 - 6.9787 0.99 2933 172 0.2046 0.2142
REMARK 3 2 6.9787 - 5.5427 1.00 2810 307 0.2559 0.3700
REMARK 3 3 5.5427 - 4.8430 1.00 3085 0 0.2410 0.0000
REMARK 3 4 4.8430 - 4.4007 1.00 2692 391 0.1894 0.2447
REMARK 3 5 4.4007 - 4.0855 1.00 3070 0 0.1999 0.0000
REMARK 3 6 4.0855 - 3.8448 1.00 3092 0 0.2206 0.0000
REMARK 3 7 3.8448 - 3.6523 1.00 2668 411 0.2349 0.2864
REMARK 3 8 3.6523 - 3.4934 1.00 3054 0 0.2456 0.0000
REMARK 3 9 3.4934 - 3.3590 1.00 3095 0 0.2615 0.0000
REMARK 3 10 3.3590 - 3.2431 1.00 2590 479 0.2743 0.3240
REMARK 3 11 3.2431 - 3.1417 1.00 3038 0 0.2899 0.0000
REMARK 3 12 3.1417 - 3.0519 1.00 3112 0 0.2958 0.0000
REMARK 3 13 3.0519 - 2.9716 1.00 2479 526 0.3076 0.3612
REMARK 3 14 2.9716 - 2.8991 1.00 3085 0 0.3152 0.0000
REMARK 3 15 2.8991 - 2.8332 0.86 2660 0 0.3285 0.0000
REMARK 3 16 2.8332 - 2.7729 0.36 1106 2 0.3369 0.3067
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.00
REMARK 3 SHRINKAGE RADIUS : 0.72
REMARK 3 K_SOL : 0.28
REMARK 3 B_SOL : 44.49
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.370
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 36.080
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 73.31
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 97.22
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -6.24600
REMARK 3 B22 (A**2) : 3.87960
REMARK 3 B33 (A**2) : 2.36640
REMARK 3 B12 (A**2) : -0.00000
REMARK 3 B13 (A**2) : 20.27370
REMARK 3 B23 (A**2) : -0.00000
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 : 0.023 10019
REMARK 3 ANGLE : 1.521 13123
REMARK 3 CHIRALITY : 0.099 1501
REMARK 3 PLANARITY : 0.005 1628
REMARK 3 DIHEDRAL : 24.802 5948
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 3R7W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 29-MAR-11.
REMARK 100 THE RCSB ID CODE IS RCSB064600.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-MAY-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97916
REMARK 200 MONOCHROMATOR : SAGITALLY FOCUSED SI(111)
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 : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 46969
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.770
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.1
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: SAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.19
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES, 10% PEG MONOMETHYL ETHER
REMARK 280 5000, 5%(V/V) TACSIMATE, PH 7.0, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
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 74.21950
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: 2490 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27550 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
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: 2650 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25740 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A 221
REMARK 465 GLU A 222
REMARK 465 ASN A 223
REMARK 465 SER A 224
REMARK 465 ASN A 225
REMARK 465 GLU A 226
REMARK 465 ASN A 227
REMARK 465 HIS A 228
REMARK 465 ASP A 229
REMARK 465 SER A 230
REMARK 465 SER A 231
REMARK 465 ASP A 232
REMARK 465 ASN A 233
REMARK 465 ASN A 234
REMARK 465 ASN A 235
REMARK 465 VAL A 236
REMARK 465 LEU A 237
REMARK 465 GLN A 310
REMARK 465 PRO B 248
REMARK 465 VAL B 249
REMARK 465 LEU B 250
REMARK 465 ARG B 251
REMARK 465 ASN B 252
REMARK 465 SER B 253
REMARK 465 GLN B 254
REMARK 465 LYS B 255
REMARK 465 SER B 256
REMARK 465 SER B 257
REMARK 465 ASP B 258
REMARK 465 LYS B 259
REMARK 465 ASP B 260
REMARK 465 ASN B 261
REMARK 465 VAL B 262
REMARK 465 ILE B 263
REMARK 465 ASN B 264
REMARK 465 PRO B 265
REMARK 465 ARG B 266
REMARK 465 ASN B 267
REMARK 465 TRP B 325
REMARK 465 ALA B 326
REMARK 465 ASN B 327
REMARK 465 ALA B 328
REMARK 465 ARG B 329
REMARK 465 ALA B 330
REMARK 465 SER B 331
REMARK 465 GLN B 332
REMARK 465 ALA B 333
REMARK 465 LYS B 334
REMARK 465 ASN B 335
REMARK 465 SER B 336
REMARK 465 ILE B 337
REMARK 465 GLU B 338
REMARK 465 ASP B 339
REMARK 465 ASP B 340
REMARK 465 VAL B 341
REMARK 465 GLY C 221
REMARK 465 GLU C 222
REMARK 465 ASN C 223
REMARK 465 SER C 224
REMARK 465 ASN C 225
REMARK 465 GLU C 226
REMARK 465 ASN C 227
REMARK 465 HIS C 228
REMARK 465 ASP C 229
REMARK 465 SER C 230
REMARK 465 SER C 231
REMARK 465 ASP C 232
REMARK 465 ASN C 233
REMARK 465 ASN C 234
REMARK 465 ASN C 235
REMARK 465 VAL C 236
REMARK 465 LEU C 237
REMARK 465 ASN D 32
REMARK 465 MSE D 33
REMARK 465 GLN D 34
REMARK 465 PRO D 35
REMARK 465 LEU D 36
REMARK 465 ASP D 37
REMARK 465 THR D 38
REMARK 465 LEU D 39
REMARK 465 TYR D 40
REMARK 465 LEU D 41
REMARK 465 GLU D 42
REMARK 465 SER D 43
REMARK 465 THR D 44
REMARK 465 SER D 45
REMARK 465 ASN D 46
REMARK 465 PRO D 47
REMARK 465 SER D 48
REMARK 465 LEU D 49
REMARK 465 GLU D 50
REMARK 465 HIS D 51
REMARK 465 PHE D 52
REMARK 465 SER D 53
REMARK 465 THR D 54
REMARK 465 LEU D 55
REMARK 465 ILE D 56
REMARK 465 ASP D 57
REMARK 465 LEU D 58
REMARK 465 ALA D 59
REMARK 465 VAL D 60
REMARK 465 MSE D 61
REMARK 465 GLU D 62
REMARK 465 LEU D 63
REMARK 465 PRO D 64
REMARK 465 GLY D 65
REMARK 465 GLN D 66
REMARK 465 LEU D 67
REMARK 465 ASN D 68
REMARK 465 TYR D 69
REMARK 465 PHE D 70
REMARK 465 GLU D 71
REMARK 465 PRO D 72
REMARK 465 SER D 73
REMARK 465 TYR D 74
REMARK 465 ASP D 75
REMARK 465 SER D 76
REMARK 465 GLU D 77
REMARK 465 ARG D 78
REMARK 465 LEU D 79
REMARK 465 PHE D 80
REMARK 465 LYS D 81
REMARK 465 SER D 82
REMARK 465 VAL D 83
REMARK 465 GLY D 84
REMARK 465 SER D 92
REMARK 465 GLN D 93
REMARK 465 ASP D 94
REMARK 465 GLU D 95
REMARK 465 TYR D 96
REMARK 465 VAL D 126
REMARK 465 ASP D 127
REMARK 465 GLY D 128
REMARK 465 LEU D 129
REMARK 465 SER D 130
REMARK 465 GLU D 131
REMARK 465 ASP D 132
REMARK 465 PRO D 248
REMARK 465 VAL D 249
REMARK 465 LEU D 250
REMARK 465 ARG D 251
REMARK 465 ASN D 252
REMARK 465 SER D 253
REMARK 465 GLN D 254
REMARK 465 LYS D 255
REMARK 465 SER D 256
REMARK 465 SER D 257
REMARK 465 ASP D 258
REMARK 465 LYS D 259
REMARK 465 ASP D 260
REMARK 465 ASN D 261
REMARK 465 VAL D 262
REMARK 465 ILE D 263
REMARK 465 ASN D 264
REMARK 465 PRO D 265
REMARK 465 ARG D 266
REMARK 465 ASN D 267
REMARK 465 TRP D 325
REMARK 465 ALA D 326
REMARK 465 ASN D 327
REMARK 465 ALA D 328
REMARK 465 ARG D 329
REMARK 465 ALA D 330
REMARK 465 SER D 331
REMARK 465 GLN D 332
REMARK 465 ALA D 333
REMARK 465 LYS D 334
REMARK 465 ASN D 335
REMARK 465 SER D 336
REMARK 465 ILE D 337
REMARK 465 GLU D 338
REMARK 465 ASP D 339
REMARK 465 ASP D 340
REMARK 465 VAL D 341
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 LEU B 283 CA - CB - CG ANGL. DEV. = 15.5 DEGREES
REMARK 500 LEU D 283 CA - CB - CG ANGL. DEV. = 15.8 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 ASN A 29 27.57 44.75
REMARK 500 ASP A 34 -31.14 -32.51
REMARK 500 ASP A 43 -151.46 49.69
REMARK 500 THR A 74 -89.77 -103.25
REMARK 500 GLU A 97 68.91 -117.74
REMARK 500 PHE A 156 -111.30 -98.36
REMARK 500 PRO A 157 161.26 -15.97
REMARK 500 MSE A 186 -67.69 -29.83
REMARK 500 GLU A 204 148.77 -175.04
REMARK 500 ASP A 239 107.67 -49.79
REMARK 500 LYS A 265 -52.36 -128.82
REMARK 500 ASN A 270 -140.95 59.23
REMARK 500 LEU A 278 -101.40 -104.84
REMARK 500 SER A 279 -178.40 -63.10
REMARK 500 GLU A 296 -61.65 -29.12
REMARK 500 LYS A 304 106.53 -169.56
REMARK 500 ALA A 305 -138.33 40.47
REMARK 500 LYS A 306 -173.83 42.01
REMARK 500 PHE A 308 -104.32 -47.23
REMARK 500 ARG B 18 136.46 -15.17
REMARK 500 ASP B 37 17.71 -67.09
REMARK 500 GLU B 42 -113.22 -82.55
REMARK 500 SER B 43 96.54 -167.53
REMARK 500 PRO B 47 97.77 -58.74
REMARK 500 LEU B 55 103.21 51.85
REMARK 500 GLN B 66 -136.65 -161.82
REMARK 500 LEU B 67 73.05 57.30
REMARK 500 ASN B 68 79.29 -2.40
REMARK 500 TYR B 69 69.39 69.76
REMARK 500 PHE B 70 96.84 -37.03
REMARK 500 GLU B 71 76.51 112.10
REMARK 500 ASP B 91 178.28 -50.56
REMARK 500 SER B 92 34.13 -165.62
REMARK 500 ASP B 94 -160.75 -174.76
REMARK 500 VAL B 126 36.63 -89.04
REMARK 500 ASP B 127 -142.37 -54.39
REMARK 500 LEU B 129 54.94 -151.46
REMARK 500 SER B 130 178.41 55.69
REMARK 500 ASP B 136 -71.04 -48.57
REMARK 500 GLN B 138 -76.38 -65.50
REMARK 500 ARG B 139 -3.86 -54.50
REMARK 500 GLU B 151 -158.43 -83.48
REMARK 500 LEU B 152 88.17 -40.66
REMARK 500 LEU B 163 53.63 -116.96
REMARK 500 SER B 165 9.05 -157.02
REMARK 500 ILE B 166 -11.78 43.60
REMARK 500 ASP B 168 -163.46 -66.37
REMARK 500 VAL B 179 -7.59 -56.20
REMARK 500 PRO B 184 98.23 -56.23
REMARK 500 GLU B 185 63.09 76.81
REMARK 500
REMARK 500 THIS ENTRY HAS 118 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLU B 268 LEU B 269 129.43
REMARK 500 GLY C 53 ASN C 54 149.81
REMARK 500 PHE D 208 ASP D 209 -149.31
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 ASN C 54 24.7 L L OUTSIDE RANGE
REMARK 500 PHE D 208 24.1 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 600 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GNP C 500 O1G
REMARK 620 2 GNP C 500 O2B 87.2
REMARK 620 3 THR C 41 OG1 96.4 175.7
REMARK 620 4 SER C 20 OG 177.7 92.9 83.4
REMARK 620 5 HOH C 702 O 90.9 83.0 94.5 86.7
REMARK 620 6 HOH C 701 O 88.3 89.0 93.5 94.0 172.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 600 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 20 OG
REMARK 620 2 GNP A 500 O2B 97.4
REMARK 620 3 GNP A 500 O1G 176.1 85.5
REMARK 620 4 THR A 41 OG1 85.3 174.6 92.1
REMARK 620 5 HOH A 702 O 92.3 80.8 90.8 94.4
REMARK 620 6 HOH A 701 O 86.0 97.7 91.0 87.1 177.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D 600 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER D 23 OG
REMARK 620 2 GNP D 500 O1G 147.2
REMARK 620 3 GNP D 500 O2B 128.7 80.6
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 600 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GNP B 500 O2B
REMARK 620 2 GNP B 500 O1G 62.7
REMARK 620 3 THR B 44 OG1 157.4 124.9
REMARK 620 4 GLU B 62 OE1 99.3 83.0 102.8
REMARK 620 5 SER B 23 OG 104.1 157.6 74.5 81.5
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GNP A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GNP B 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GNP C 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GNP D 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 600
DBREF 3R7W A 8 310 UNP Q00582 GTR1_YEAST 8 310
DBREF 3R7W B 11 341 UNP P53290 GTR2_YEAST 11 341
DBREF 3R7W C 8 310 UNP Q00582 GTR1_YEAST 8 310
DBREF 3R7W D 11 341 UNP P53290 GTR2_YEAST 11 341
SEQADV 3R7W PRO A 4 UNP Q00582 EXPRESSION TAG
SEQADV 3R7W LEU A 5 UNP Q00582 EXPRESSION TAG
SEQADV 3R7W GLY A 6 UNP Q00582 EXPRESSION TAG
SEQADV 3R7W SER A 7 UNP Q00582 EXPRESSION TAG
SEQADV 3R7W PRO C 4 UNP Q00582 EXPRESSION TAG
SEQADV 3R7W LEU C 5 UNP Q00582 EXPRESSION TAG
SEQADV 3R7W GLY C 6 UNP Q00582 EXPRESSION TAG
SEQADV 3R7W SER C 7 UNP Q00582 EXPRESSION TAG
SEQRES 1 A 307 PRO LEU GLY SER LYS LEU LEU LEU MSE GLY ARG SER GLY
SEQRES 2 A 307 SER GLY LYS SER SER MSE ARG SER ILE ILE PHE SER ASN
SEQRES 3 A 307 TYR SER ALA PHE ASP THR ARG ARG LEU GLY ALA THR ILE
SEQRES 4 A 307 ASP VAL GLU HIS SER HIS LEU ARG PHE LEU GLY ASN MSE
SEQRES 5 A 307 THR LEU ASN LEU TRP ASP CYS GLY GLY GLN ASP VAL PHE
SEQRES 6 A 307 MSE GLU ASN TYR PHE THR LYS GLN LYS ASP HIS ILE PHE
SEQRES 7 A 307 GLN MSE VAL GLN VAL LEU ILE HIS VAL PHE ASP VAL GLU
SEQRES 8 A 307 SER THR GLU VAL LEU LYS ASP ILE GLU ILE PHE ALA LYS
SEQRES 9 A 307 ALA LEU LYS GLN LEU ARG LYS TYR SER PRO ASP ALA LYS
SEQRES 10 A 307 ILE PHE VAL LEU LEU HIS LYS MSE ASP LEU VAL GLN LEU
SEQRES 11 A 307 ASP LYS ARG GLU GLU LEU PHE GLN ILE MSE MSE LYS ASN
SEQRES 12 A 307 LEU SER GLU THR SER SER GLU PHE GLY PHE PRO ASN LEU
SEQRES 13 A 307 ILE GLY PHE PRO THR SER ILE TRP ASP GLU SER LEU TYR
SEQRES 14 A 307 LYS ALA TRP SER GLN ILE VAL CYS SER LEU ILE PRO ASN
SEQRES 15 A 307 MSE SER ASN HIS GLN SER ASN LEU LYS LYS PHE LYS GLU
SEQRES 16 A 307 ILE MSE ASN ALA LEU GLU ILE ILE LEU PHE GLU ARG THR
SEQRES 17 A 307 THR PHE LEU VAL ILE CYS SER SER ASN GLY GLU ASN SER
SEQRES 18 A 307 ASN GLU ASN HIS ASP SER SER ASP ASN ASN ASN VAL LEU
SEQRES 19 A 307 LEU ASP PRO LYS ARG PHE GLU LYS ILE SER ASN ILE MSE
SEQRES 20 A 307 LYS ASN PHE LYS GLN SER CYS THR LYS LEU LYS SER GLY
SEQRES 21 A 307 PHE LYS THR LEU ILE LEU ASN ASN ASN ILE TYR VAL SER
SEQRES 22 A 307 GLU LEU SER SER ASN MSE VAL CYS PHE ILE VAL LEU LYS
SEQRES 23 A 307 ASP MSE ASN ILE PRO GLN GLU LEU VAL LEU GLU ASN ILE
SEQRES 24 A 307 LYS LYS ALA LYS GLU PHE PHE GLN
SEQRES 1 B 331 MSE VAL LEU LEU MSE GLY VAL ARG ARG CYS GLY LYS SER
SEQRES 2 B 331 SER ILE CYS LYS VAL VAL PHE HIS ASN MSE GLN PRO LEU
SEQRES 3 B 331 ASP THR LEU TYR LEU GLU SER THR SER ASN PRO SER LEU
SEQRES 4 B 331 GLU HIS PHE SER THR LEU ILE ASP LEU ALA VAL MSE GLU
SEQRES 5 B 331 LEU PRO GLY GLN LEU ASN TYR PHE GLU PRO SER TYR ASP
SEQRES 6 B 331 SER GLU ARG LEU PHE LYS SER VAL GLY ALA LEU VAL TYR
SEQRES 7 B 331 VAL ILE ASP SER GLN ASP GLU TYR ILE ASN ALA ILE THR
SEQRES 8 B 331 ASN LEU ALA MSE ILE ILE GLU TYR ALA TYR LYS VAL ASN
SEQRES 9 B 331 PRO SER ILE ASN ILE GLU VAL LEU ILE HIS LYS VAL ASP
SEQRES 10 B 331 GLY LEU SER GLU ASP PHE LYS VAL ASP ALA GLN ARG ASP
SEQRES 11 B 331 ILE MSE GLN ARG THR GLY GLU GLU LEU LEU GLU LEU GLY
SEQRES 12 B 331 LEU ASP GLY VAL GLN VAL SER PHE TYR LEU THR SER ILE
SEQRES 13 B 331 PHE ASP HIS SER ILE TYR GLU ALA PHE SER ARG ILE VAL
SEQRES 14 B 331 GLN LYS LEU ILE PRO GLU LEU SER PHE LEU GLU ASN MSE
SEQRES 15 B 331 LEU ASP ASN LEU ILE GLN HIS SER LYS ILE GLU LYS ALA
SEQRES 16 B 331 PHE LEU PHE ASP VAL ASN SER LYS ILE TYR VAL SER THR
SEQRES 17 B 331 ASP SER ASN PRO VAL ASP ILE GLN MSE TYR GLU VAL CYS
SEQRES 18 B 331 SER GLU PHE ILE ASP VAL THR ILE ASP LEU PHE ASP LEU
SEQRES 19 B 331 TYR LYS ALA PRO VAL LEU ARG ASN SER GLN LYS SER SER
SEQRES 20 B 331 ASP LYS ASP ASN VAL ILE ASN PRO ARG ASN GLU LEU GLN
SEQRES 21 B 331 ASN VAL SER GLN LEU ALA ASN GLY VAL ILE ILE TYR LEU
SEQRES 22 B 331 ARG GLN MSE ILE ARG GLY LEU ALA LEU VAL ALA ILE ILE
SEQRES 23 B 331 ARG PRO ASN GLY THR ASP MSE GLU SER CYS LEU THR VAL
SEQRES 24 B 331 ALA ASP TYR ASN ILE ASP ILE PHE LYS LYS GLY LEU GLU
SEQRES 25 B 331 ASP ILE TRP ALA ASN ALA ARG ALA SER GLN ALA LYS ASN
SEQRES 26 B 331 SER ILE GLU ASP ASP VAL
SEQRES 1 C 307 PRO LEU GLY SER LYS LEU LEU LEU MSE GLY ARG SER GLY
SEQRES 2 C 307 SER GLY LYS SER SER MSE ARG SER ILE ILE PHE SER ASN
SEQRES 3 C 307 TYR SER ALA PHE ASP THR ARG ARG LEU GLY ALA THR ILE
SEQRES 4 C 307 ASP VAL GLU HIS SER HIS LEU ARG PHE LEU GLY ASN MSE
SEQRES 5 C 307 THR LEU ASN LEU TRP ASP CYS GLY GLY GLN ASP VAL PHE
SEQRES 6 C 307 MSE GLU ASN TYR PHE THR LYS GLN LYS ASP HIS ILE PHE
SEQRES 7 C 307 GLN MSE VAL GLN VAL LEU ILE HIS VAL PHE ASP VAL GLU
SEQRES 8 C 307 SER THR GLU VAL LEU LYS ASP ILE GLU ILE PHE ALA LYS
SEQRES 9 C 307 ALA LEU LYS GLN LEU ARG LYS TYR SER PRO ASP ALA LYS
SEQRES 10 C 307 ILE PHE VAL LEU LEU HIS LYS MSE ASP LEU VAL GLN LEU
SEQRES 11 C 307 ASP LYS ARG GLU GLU LEU PHE GLN ILE MSE MSE LYS ASN
SEQRES 12 C 307 LEU SER GLU THR SER SER GLU PHE GLY PHE PRO ASN LEU
SEQRES 13 C 307 ILE GLY PHE PRO THR SER ILE TRP ASP GLU SER LEU TYR
SEQRES 14 C 307 LYS ALA TRP SER GLN ILE VAL CYS SER LEU ILE PRO ASN
SEQRES 15 C 307 MSE SER ASN HIS GLN SER ASN LEU LYS LYS PHE LYS GLU
SEQRES 16 C 307 ILE MSE ASN ALA LEU GLU ILE ILE LEU PHE GLU ARG THR
SEQRES 17 C 307 THR PHE LEU VAL ILE CYS SER SER ASN GLY GLU ASN SER
SEQRES 18 C 307 ASN GLU ASN HIS ASP SER SER ASP ASN ASN ASN VAL LEU
SEQRES 19 C 307 LEU ASP PRO LYS ARG PHE GLU LYS ILE SER ASN ILE MSE
SEQRES 20 C 307 LYS ASN PHE LYS GLN SER CYS THR LYS LEU LYS SER GLY
SEQRES 21 C 307 PHE LYS THR LEU ILE LEU ASN ASN ASN ILE TYR VAL SER
SEQRES 22 C 307 GLU LEU SER SER ASN MSE VAL CYS PHE ILE VAL LEU LYS
SEQRES 23 C 307 ASP MSE ASN ILE PRO GLN GLU LEU VAL LEU GLU ASN ILE
SEQRES 24 C 307 LYS LYS ALA LYS GLU PHE PHE GLN
SEQRES 1 D 331 MSE VAL LEU LEU MSE GLY VAL ARG ARG CYS GLY LYS SER
SEQRES 2 D 331 SER ILE CYS LYS VAL VAL PHE HIS ASN MSE GLN PRO LEU
SEQRES 3 D 331 ASP THR LEU TYR LEU GLU SER THR SER ASN PRO SER LEU
SEQRES 4 D 331 GLU HIS PHE SER THR LEU ILE ASP LEU ALA VAL MSE GLU
SEQRES 5 D 331 LEU PRO GLY GLN LEU ASN TYR PHE GLU PRO SER TYR ASP
SEQRES 6 D 331 SER GLU ARG LEU PHE LYS SER VAL GLY ALA LEU VAL TYR
SEQRES 7 D 331 VAL ILE ASP SER GLN ASP GLU TYR ILE ASN ALA ILE THR
SEQRES 8 D 331 ASN LEU ALA MSE ILE ILE GLU TYR ALA TYR LYS VAL ASN
SEQRES 9 D 331 PRO SER ILE ASN ILE GLU VAL LEU ILE HIS LYS VAL ASP
SEQRES 10 D 331 GLY LEU SER GLU ASP PHE LYS VAL ASP ALA GLN ARG ASP
SEQRES 11 D 331 ILE MSE GLN ARG THR GLY GLU GLU LEU LEU GLU LEU GLY
SEQRES 12 D 331 LEU ASP GLY VAL GLN VAL SER PHE TYR LEU THR SER ILE
SEQRES 13 D 331 PHE ASP HIS SER ILE TYR GLU ALA PHE SER ARG ILE VAL
SEQRES 14 D 331 GLN LYS LEU ILE PRO GLU LEU SER PHE LEU GLU ASN MSE
SEQRES 15 D 331 LEU ASP ASN LEU ILE GLN HIS SER LYS ILE GLU LYS ALA
SEQRES 16 D 331 PHE LEU PHE ASP VAL ASN SER LYS ILE TYR VAL SER THR
SEQRES 17 D 331 ASP SER ASN PRO VAL ASP ILE GLN MSE TYR GLU VAL CYS
SEQRES 18 D 331 SER GLU PHE ILE ASP VAL THR ILE ASP LEU PHE ASP LEU
SEQRES 19 D 331 TYR LYS ALA PRO VAL LEU ARG ASN SER GLN LYS SER SER
SEQRES 20 D 331 ASP LYS ASP ASN VAL ILE ASN PRO ARG ASN GLU LEU GLN
SEQRES 21 D 331 ASN VAL SER GLN LEU ALA ASN GLY VAL ILE ILE TYR LEU
SEQRES 22 D 331 ARG GLN MSE ILE ARG GLY LEU ALA LEU VAL ALA ILE ILE
SEQRES 23 D 331 ARG PRO ASN GLY THR ASP MSE GLU SER CYS LEU THR VAL
SEQRES 24 D 331 ALA ASP TYR ASN ILE ASP ILE PHE LYS LYS GLY LEU GLU
SEQRES 25 D 331 ASP ILE TRP ALA ASN ALA ARG ALA SER GLN ALA LYS ASN
SEQRES 26 D 331 SER ILE GLU ASP ASP VAL
MODRES 3R7W MSE A 12 MET SELENOMETHIONINE
MODRES 3R7W MSE A 22 MET SELENOMETHIONINE
MODRES 3R7W MSE A 55 MET SELENOMETHIONINE
MODRES 3R7W MSE A 69 MET SELENOMETHIONINE
MODRES 3R7W MSE A 83 MET SELENOMETHIONINE
MODRES 3R7W MSE A 128 MET SELENOMETHIONINE
MODRES 3R7W MSE A 143 MET SELENOMETHIONINE
MODRES 3R7W MSE A 144 MET SELENOMETHIONINE
MODRES 3R7W MSE A 186 MET SELENOMETHIONINE
MODRES 3R7W MSE A 200 MET SELENOMETHIONINE
MODRES 3R7W MSE A 250 MET SELENOMETHIONINE
MODRES 3R7W MSE A 282 MET SELENOMETHIONINE
MODRES 3R7W MSE A 291 MET SELENOMETHIONINE
MODRES 3R7W MSE B 11 MET SELENOMETHIONINE
MODRES 3R7W MSE B 15 MET SELENOMETHIONINE
MODRES 3R7W MSE B 33 MET SELENOMETHIONINE
MODRES 3R7W MSE B 61 MET SELENOMETHIONINE
MODRES 3R7W MSE B 105 MET SELENOMETHIONINE
MODRES 3R7W MSE B 142 MET SELENOMETHIONINE
MODRES 3R7W MSE B 192 MET SELENOMETHIONINE
MODRES 3R7W MSE B 227 MET SELENOMETHIONINE
MODRES 3R7W MSE B 286 MET SELENOMETHIONINE
MODRES 3R7W MSE B 303 MET SELENOMETHIONINE
MODRES 3R7W MSE C 12 MET SELENOMETHIONINE
MODRES 3R7W MSE C 22 MET SELENOMETHIONINE
MODRES 3R7W MSE C 55 MET SELENOMETHIONINE
MODRES 3R7W MSE C 69 MET SELENOMETHIONINE
MODRES 3R7W MSE C 83 MET SELENOMETHIONINE
MODRES 3R7W MSE C 128 MET SELENOMETHIONINE
MODRES 3R7W MSE C 143 MET SELENOMETHIONINE
MODRES 3R7W MSE C 144 MET SELENOMETHIONINE
MODRES 3R7W MSE C 186 MET SELENOMETHIONINE
MODRES 3R7W MSE C 200 MET SELENOMETHIONINE
MODRES 3R7W MSE C 250 MET SELENOMETHIONINE
MODRES 3R7W MSE C 282 MET SELENOMETHIONINE
MODRES 3R7W MSE C 291 MET SELENOMETHIONINE
MODRES 3R7W MSE D 11 MET SELENOMETHIONINE
MODRES 3R7W MSE D 15 MET SELENOMETHIONINE
MODRES 3R7W MSE D 105 MET SELENOMETHIONINE
MODRES 3R7W MSE D 142 MET SELENOMETHIONINE
MODRES 3R7W MSE D 192 MET SELENOMETHIONINE
MODRES 3R7W MSE D 227 MET SELENOMETHIONINE
MODRES 3R7W MSE D 286 MET SELENOMETHIONINE
MODRES 3R7W MSE D 303 MET SELENOMETHIONINE
HET MSE A 12 8
HET MSE A 22 8
HET MSE A 55 8
HET MSE A 69 8
HET MSE A 83 8
HET MSE A 128 8
HET MSE A 143 8
HET MSE A 144 8
HET MSE A 186 8
HET MSE A 200 8
HET MSE A 250 8
HET MSE A 282 8
HET MSE A 291 8
HET MSE B 11 8
HET MSE B 15 8
HET MSE B 33 8
HET MSE B 61 8
HET MSE B 105 8
HET MSE B 142 8
HET MSE B 192 8
HET MSE B 227 8
HET MSE B 286 8
HET MSE B 303 8
HET MSE C 12 8
HET MSE C 22 8
HET MSE C 55 8
HET MSE C 69 8
HET MSE C 83 8
HET MSE C 128 8
HET MSE C 143 8
HET MSE C 144 8
HET MSE C 186 8
HET MSE C 200 8
HET MSE C 250 8
HET MSE C 282 8
HET MSE C 291 8
HET MSE D 11 8
HET MSE D 15 8
HET MSE D 105 8
HET MSE D 142 8
HET MSE D 192 8
HET MSE D 227 8
HET MSE D 286 8
HET MSE D 303 8
HET GNP A 500 32
HET MG A 600 1
HET GNP B 500 32
HET MG B 600 1
HET GNP C 500 32
HET MG C 600 1
HET GNP D 500 32
HET MG D 600 1
HETNAM MSE SELENOMETHIONINE
HETNAM GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER
HETNAM MG MAGNESIUM ION
FORMUL 1 MSE 44(C5 H11 N O2 SE)
FORMUL 5 GNP 4(C10 H17 N6 O13 P3)
FORMUL 6 MG 4(MG 2+)
FORMUL 13 HOH *4(H2 O)
HELIX 1 1 GLY A 18 SER A 28 1 11
HELIX 2 2 ALA A 32 LEU A 38 5 7
HELIX 3 3 GLN A 65 THR A 74 1 10
HELIX 4 4 GLN A 76 GLN A 82 1 7
HELIX 5 5 GLU A 97 SER A 116 1 20
HELIX 6 6 LYS A 127 VAL A 131 5 5
HELIX 7 7 GLN A 132 GLU A 153 1 22
HELIX 8 8 GLU A 169 SER A 181 1 13
HELIX 9 9 ASN A 185 ASN A 201 1 17
HELIX 10 10 LYS A 241 THR A 258 1 18
HELIX 11 11 LYS A 259 LYS A 261 5 3
HELIX 12 12 PRO A 294 ILE A 302 1 9
HELIX 13 13 SER B 23 HIS B 31 1 9
HELIX 14 14 PRO B 35 LEU B 39 5 5
HELIX 15 15 SER B 73 LYS B 81 1 9
HELIX 16 16 ILE B 97 ASN B 114 1 18
HELIX 17 17 GLU B 131 GLU B 148 1 18
HELIX 18 18 HIS B 169 GLN B 180 1 12
HELIX 19 19 GLU B 185 ASP B 194 1 10
HELIX 20 20 ASN B 195 GLN B 198 5 4
HELIX 21 21 ASP B 224 ASP B 243 1 20
HELIX 22 22 ASP B 302 ASP B 323 1 22
HELIX 23 23 GLY C 18 SER C 28 1 11
HELIX 24 24 PHE C 33 LEU C 38 5 6
HELIX 25 25 GLN C 65 THR C 74 1 10
HELIX 26 26 GLN C 76 GLN C 82 1 7
HELIX 27 27 GLU C 97 SER C 116 1 20
HELIX 28 28 GLN C 132 GLU C 153 1 22
HELIX 29 29 GLU C 169 SER C 181 1 13
HELIX 30 30 ASN C 185 ASN C 201 1 17
HELIX 31 31 LYS C 241 THR C 258 1 18
HELIX 32 32 PRO C 294 LYS C 306 1 13
HELIX 33 33 GLY D 21 VAL D 28 1 8
HELIX 34 34 ILE D 97 LYS D 112 1 16
HELIX 35 35 PHE D 133 LEU D 149 1 17
HELIX 36 36 HIS D 169 LYS D 181 1 13
HELIX 37 37 ASP D 194 GLN D 198 5 5
HELIX 38 38 ASP D 224 TYR D 245 1 22
HELIX 39 39 ASP D 302 ASP D 323 1 22
SHEET 1 A 6 VAL A 44 PHE A 51 0
SHEET 2 A 6 MSE A 55 CYS A 62 -1 O MSE A 55 N PHE A 51
SHEET 3 A 6 GLY A 6 MSE A 12 1 N LEU A 9 O TRP A 60
SHEET 4 A 6 VAL A 86 ASP A 92 1 O VAL A 86 N LEU A 10
SHEET 5 A 6 LYS A 120 HIS A 126 1 O LYS A 120 N LEU A 87
SHEET 6 A 6 ILE A 160 PRO A 163 1 O PHE A 162 N LEU A 125
SHEET 1 B10 VAL A 215 SER A 218 0
SHEET 2 B10 ALA A 202 GLU A 209 -1 N LEU A 207 O ILE A 216
SHEET 3 B10 MSE A 282 LEU A 288 -1 O VAL A 287 N GLU A 204
SHEET 4 B10 ILE A 273 GLU A 277 -1 N TYR A 274 O ILE A 286
SHEET 5 B10 PHE A 264 LEU A 269 -1 N LEU A 267 O VAL A 275
SHEET 6 B10 GLN B 270 LEU B 275 -1 O VAL B 272 N ILE A 268
SHEET 7 B10 ILE B 280 GLN B 285 -1 O ILE B 281 N SER B 273
SHEET 8 B10 LEU B 290 ILE B 296 -1 O LEU B 292 N ARG B 284
SHEET 9 B10 ILE B 202 ASP B 209 -1 N GLU B 203 O ILE B 295
SHEET 10 B10 SER B 217 THR B 218 -1 O SER B 217 N LEU B 207
SHEET 1 C 6 GLU B 50 PHE B 52 0
SHEET 2 C 6 LEU B 58 GLU B 62 -1 O VAL B 60 N GLU B 50
SHEET 3 C 6 VAL B 12 MSE B 15 1 N LEU B 14 O MSE B 61
SHEET 4 C 6 ALA B 85 VAL B 89 1 O VAL B 89 N MSE B 15
SHEET 5 C 6 ASN B 118 LEU B 122 1 O GLU B 120 N LEU B 86
SHEET 6 C 6 VAL B 159 TYR B 162 1 O SER B 160 N VAL B 121
SHEET 1 D 6 VAL C 44 PHE C 51 0
SHEET 2 D 6 MSE C 55 CYS C 62 -1 O MSE C 55 N PHE C 51
SHEET 3 D 6 SER C 7 MSE C 12 1 N LEU C 9 O TRP C 60
SHEET 4 D 6 VAL C 84 ASP C 92 1 O ILE C 88 N LEU C 10
SHEET 5 D 6 LYS C 120 HIS C 126 1 O LEU C 124 N PHE C 91
SHEET 6 D 6 ILE C 160 THR C 164 1 O PHE C 162 N LEU C 125
SHEET 1 E 9 VAL C 215 SER C 218 0
SHEET 2 E 9 ALA C 202 GLU C 209 -1 N LEU C 207 O ILE C 216
SHEET 3 E 9 MSE C 282 LEU C 288 -1 O VAL C 287 N GLU C 204
SHEET 4 E 9 ILE C 273 GLU C 277 -1 N TYR C 274 O ILE C 286
SHEET 5 E 9 THR C 266 LEU C 269 -1 N LEU C 267 O VAL C 275
SHEET 6 E 9 GLN D 270 GLN D 274 -1 O VAL D 272 N ILE C 268
SHEET 7 E 9 ILE D 280 GLN D 285 -1 O ILE D 281 N SER D 273
SHEET 8 E 9 ALA D 291 ILE D 296 -1 O LEU D 292 N ARG D 284
SHEET 9 E 9 ILE D 202 PHE D 206 -1 N PHE D 206 O VAL D 293
SHEET 1 F 4 LEU D 13 GLY D 16 0
SHEET 2 F 4 LEU D 86 VAL D 89 1 O VAL D 89 N MSE D 15
SHEET 3 F 4 ILE D 119 ILE D 123 1 O GLU D 120 N TYR D 88
SHEET 4 F 4 SER D 160 LEU D 163 1 O SER D 160 N ILE D 119
LINK C LEU A 11 N MSE A 12 1555 1555 1.32
LINK C MSE A 12 N GLY A 13 1555 1555 1.33
LINK C SER A 21 N MSE A 22 1555 1555 1.33
LINK C MSE A 22 N ARG A 23 1555 1555 1.34
LINK C ASN A 54 N MSE A 55 1555 1555 1.33
LINK C MSE A 55 N THR A 56 1555 1555 1.32
LINK C PHE A 68 N MSE A 69 1555 1555 1.31
LINK C MSE A 69 N GLU A 70 1555 1555 1.33
LINK C GLN A 82 N MSE A 83 1555 1555 1.33
LINK C MSE A 83 N VAL A 84 1555 1555 1.33
LINK C LYS A 127 N MSE A 128 1555 1555 1.32
LINK C MSE A 128 N ASP A 129 1555 1555 1.33
LINK C ILE A 142 N MSE A 143 1555 1555 1.34
LINK C MSE A 143 N MSE A 144 1555 1555 1.33
LINK C MSE A 144 N LYS A 145 1555 1555 1.33
LINK C ASN A 185 N MSE A 186 1555 1555 1.33
LINK C MSE A 186 N SER A 187 1555 1555 1.33
LINK C ILE A 199 N MSE A 200 1555 1555 1.33
LINK C MSE A 200 N ASN A 201 1555 1555 1.33
LINK C ILE A 249 N MSE A 250 1555 1555 1.33
LINK C MSE A 250 N LYS A 251 1555 1555 1.33
LINK C ASN A 281 N MSE A 282 1555 1555 1.33
LINK C MSE A 282 N VAL A 283 1555 1555 1.33
LINK C ASP A 290 N MSE A 291 1555 1555 1.33
LINK C MSE A 291 N ASN A 292 1555 1555 1.33
LINK C MSE B 11 N VAL B 12 1555 1555 1.33
LINK C LEU B 14 N MSE B 15 1555 1555 1.33
LINK C MSE B 15 N GLY B 16 1555 1555 1.33
LINK C ASN B 32 N MSE B 33 1555 1555 1.33
LINK C MSE B 33 N GLN B 34 1555 1555 1.33
LINK C VAL B 60 N MSE B 61 1555 1555 1.33
LINK C MSE B 61 N GLU B 62 1555 1555 1.32
LINK C ALA B 104 N MSE B 105 1555 1555 1.33
LINK C MSE B 105 N ILE B 106 1555 1555 1.33
LINK C ILE B 141 N MSE B 142 1555 1555 1.33
LINK C MSE B 142 N GLN B 143 1555 1555 1.33
LINK C ASN B 191 N MSE B 192 1555 1555 1.33
LINK C MSE B 192 N LEU B 193 1555 1555 1.32
LINK C GLN B 226 N MSE B 227 1555 1555 1.33
LINK C MSE B 227 N TYR B 228 1555 1555 1.33
LINK C GLN B 285 N MSE B 286 1555 1555 1.33
LINK C MSE B 286 N ILE B 287 1555 1555 1.33
LINK C ASP B 302 N MSE B 303 1555 1555 1.33
LINK C MSE B 303 N GLU B 304 1555 1555 1.33
LINK C LEU C 11 N MSE C 12 1555 1555 1.33
LINK C MSE C 12 N GLY C 13 1555 1555 1.33
LINK C SER C 21 N MSE C 22 1555 1555 1.33
LINK C MSE C 22 N ARG C 23 1555 1555 1.33
LINK C ASN C 54 N MSE C 55 1555 1555 1.34
LINK C MSE C 55 N THR C 56 1555 1555 1.33
LINK C PHE C 68 N MSE C 69 1555 1555 1.33
LINK C MSE C 69 N GLU C 70 1555 1555 1.33
LINK C GLN C 82 N MSE C 83 1555 1555 1.33
LINK C MSE C 83 N VAL C 84 1555 1555 1.32
LINK C LYS C 127 N MSE C 128 1555 1555 1.32
LINK C MSE C 128 N ASP C 129 1555 1555 1.33
LINK C ILE C 142 N MSE C 143 1555 1555 1.32
LINK C MSE C 143 N MSE C 144 1555 1555 1.33
LINK C MSE C 144 N LYS C 145 1555 1555 1.34
LINK C ASN C 185 N MSE C 186 1555 1555 1.33
LINK C MSE C 186 N SER C 187 1555 1555 1.33
LINK C ILE C 199 N MSE C 200 1555 1555 1.33
LINK C MSE C 200 N ASN C 201 1555 1555 1.33
LINK C ILE C 249 N MSE C 250 1555 1555 1.33
LINK C MSE C 250 N LYS C 251 1555 1555 1.32
LINK C ASN C 281 N MSE C 282 1555 1555 1.33
LINK C MSE C 282 N VAL C 283 1555 1555 1.33
LINK C ASP C 290 N MSE C 291 1555 1555 1.33
LINK C MSE C 291 N ASN C 292 1555 1555 1.33
LINK C MSE D 11 N VAL D 12 1555 1555 1.33
LINK C LEU D 14 N MSE D 15 1555 1555 1.34
LINK C MSE D 15 N GLY D 16 1555 1555 1.33
LINK C ALA D 104 N MSE D 105 1555 1555 1.33
LINK C MSE D 105 N ILE D 106 1555 1555 1.33
LINK C ILE D 141 N MSE D 142 1555 1555 1.33
LINK C MSE D 142 N GLN D 143 1555 1555 1.33
LINK C ASN D 191 N MSE D 192 1555 1555 1.33
LINK C MSE D 192 N LEU D 193 1555 1555 1.33
LINK C GLN D 226 N MSE D 227 1555 1555 1.34
LINK C MSE D 227 N TYR D 228 1555 1555 1.33
LINK C GLN D 285 N MSE D 286 1555 1555 1.33
LINK C MSE D 286 N ILE D 287 1555 1555 1.33
LINK C ASP D 302 N MSE D 303 1555 1555 1.33
LINK C MSE D 303 N GLU D 304 1555 1555 1.33
LINK O1G GNP C 500 MG MG C 600 1555 1555 1.99
LINK OG SER A 20 MG MG A 600 1555 1555 2.05
LINK OG SER D 23 MG MG D 600 1555 1555 2.09
LINK O2B GNP A 500 MG MG A 600 1555 1555 2.12
LINK O2B GNP C 500 MG MG C 600 1555 1555 2.15
LINK O1G GNP A 500 MG MG A 600 1555 1555 2.15
LINK OG1 THR C 41 MG MG C 600 1555 1555 2.24
LINK OG SER C 20 MG MG C 600 1555 1555 2.27
LINK OG1 THR A 41 MG MG A 600 1555 1555 2.27
LINK O1G GNP D 500 MG MG D 600 1555 1555 2.31
LINK O2B GNP B 500 MG MG B 600 1555 1555 2.40
LINK O1G GNP B 500 MG MG B 600 1555 1555 2.48
LINK OG1 THR B 44 MG MG B 600 1555 1555 2.73
LINK O2B GNP D 500 MG MG D 600 1555 1555 2.82
LINK OE1 GLU B 62 MG MG B 600 1555 1555 2.83
LINK OG SER B 23 MG MG B 600 1555 1555 2.87
LINK MG MG C 600 O HOH C 702 1555 1555 1.72
LINK MG MG C 600 O HOH C 701 1555 1555 1.91
LINK MG MG A 600 O HOH A 702 1555 1555 2.02
LINK MG MG A 600 O HOH A 701 1555 1555 2.17
CISPEP 1 PRO A 157 ASN A 158 0 18.11
CISPEP 2 LYS A 304 ALA A 305 0 -11.80
CISPEP 3 LEU B 55 ILE B 56 0 3.80
CISPEP 4 PHE B 70 GLU B 71 0 15.69
CISPEP 5 SER D 212 LYS D 213 0 26.39
SITE 1 AC1 20 SER A 15 GLY A 16 SER A 17 GLY A 18
SITE 2 AC1 20 LYS A 19 SER A 20 SER A 21 THR A 35
SITE 3 AC1 20 THR A 41 GLY A 64 HIS A 126 LYS A 127
SITE 4 AC1 20 ASP A 129 LEU A 130 SER A 165 ILE A 166
SITE 5 AC1 20 TRP A 167 MG A 600 HOH A 701 HOH A 702
SITE 1 AC2 5 SER A 20 THR A 41 GNP A 500 HOH A 701
SITE 2 AC2 5 HOH A 702
SITE 1 AC3 18 ARG B 18 ARG B 19 CYS B 20 GLY B 21
SITE 2 AC3 18 LYS B 22 SER B 23 SER B 24 THR B 38
SITE 3 AC3 18 LEU B 39 SER B 43 GLU B 62 GLY B 65
SITE 4 AC3 18 HIS B 124 LYS B 125 ASP B 127 SER B 165
SITE 5 AC3 18 ILE B 166 MG B 600
SITE 1 AC4 4 SER B 23 THR B 44 GLU B 62 GNP B 500
SITE 1 AC5 19 SER C 15 GLY C 16 SER C 17 GLY C 18
SITE 2 AC5 19 LYS C 19 SER C 20 SER C 21 THR C 35
SITE 3 AC5 19 THR C 41 GLY C 64 HIS C 126 LYS C 127
SITE 4 AC5 19 ASP C 129 LEU C 130 SER C 165 ILE C 166
SITE 5 AC5 19 MG C 600 HOH C 701 HOH C 702
SITE 1 AC6 5 SER C 20 THR C 41 GNP C 500 HOH C 701
SITE 2 AC6 5 HOH C 702
SITE 1 AC7 9 CYS D 20 GLY D 21 LYS D 22 SER D 23
SITE 2 AC7 9 SER D 24 HIS D 124 LYS D 125 ILE D 166
SITE 3 AC7 9 MG D 600
SITE 1 AC8 3 LYS D 22 SER D 23 GNP D 500
CRYST1 68.908 148.439 98.508 90.00 100.61 90.00 P 1 21 1 4
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 0.014512 0.000000 0.002718 0.00000
SCALE2 0.000000 0.006737 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010328 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
