HEADER PROTEIN TRANSPORT 15-JUN-10 2KZB
TITLE SOLUTION STRUCTURE OF ALPHA-MANNOSIDASE BINDING DOMAIN OF ATG19
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: AUTOPHAGY-RELATED PROTEIN 19;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: ALPHA-MANNOSIDASE BINDING DOMAIN;
COMPND 5 SYNONYM: ATG19, CYTOPLASM-TO-VACUOLE TARGETING PROTEIN 19;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BREWER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 GENE: ATG19, CVT19, YOL082W, YOL01, O0980;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: VECTOR;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PGEX-6P-1
KEYWDS SELECTIVE AUTOPHAGY, ATG19, ALPHA-MANNOSIDASE, PROTEIN TRANSPORT
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR Y.WATANABE,N.NODA,H.KUMETA,K.SUZUKI,Y.OHSUMI,F.INAGAKI
REVDAT 4 14-JUN-23 2KZB 1 REMARK
REVDAT 3 26-FEB-20 2KZB 1 REMARK SEQADV
REVDAT 2 12-MAR-14 2KZB 1 JRNL VERSN
REVDAT 1 21-JUL-10 2KZB 0
JRNL AUTH Y.WATANABE,N.N.NODA,H.KUMETA,K.SUZUKI,Y.OHSUMI,F.INAGAKI
JRNL TITL SELECTIVE TRANSPORT OF ALPHA-MANNOSIDASE BY AUTOPHAGIC
JRNL TITL 2 PATHWAYS: STRUCTURAL BASIS FOR CARGO RECOGNITION BY ATG19
JRNL TITL 3 AND ATG34.
JRNL REF J.BIOL.CHEM. V. 285 30026 2010
JRNL REFN ISSN 0021-9258
JRNL PMID 20659891
JRNL DOI 10.1074/JBC.M110.143545
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CYANA
REMARK 3 AUTHORS : GUNTERT, MUMENTHALER AND WUTHRICH
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2KZB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 23-JUN-10.
REMARK 100 THE DEPOSITION ID IS D_1000101761.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 25MM SODIUM PHOSPHATE-1, 100MM
REMARK 210 SODIUM CHLORIDE-2, 2MM DTT-3, 90%
REMARK 210 H2O/10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-15N HSQC; 3D HNCO; 3D
REMARK 210 HNCA; 3D HN(CO)CA; 3D CBCA(CO)NH;
REMARK 210 3D HNCACB; 3D HNHA; 3D HBHA(CO)
REMARK 210 NH; 2D 1H-13C HSQC; 2D 1H-1H
REMARK 210 TOCSY; 3D 1H-13C NOESY; 3D 1H-
REMARK 210 15N NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CYANA, NMRPIPE, SPARKY
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: NULL
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
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: MONOMERIC
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-20
REMARK 465 RES C SSSEQI
REMARK 465 GLY A 250
REMARK 465 PRO A 251
REMARK 465 HIS A 252
REMARK 465 MET A 253
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 1 GLU A 255 156.14 -49.66
REMARK 500 1 ARG A 269 -160.16 -124.24
REMARK 500 1 ASN A 279 96.73 -46.91
REMARK 500 1 SER A 283 -84.92 -118.02
REMARK 500 1 VAL A 284 156.31 167.61
REMARK 500 1 ALA A 296 -69.75 -130.22
REMARK 500 1 PRO A 300 -162.28 -74.99
REMARK 500 1 GLN A 303 109.25 -57.00
REMARK 500 1 LYS A 315 24.55 47.80
REMARK 500 1 GLU A 316 -158.62 -77.91
REMARK 500 1 TYR A 317 139.85 -175.57
REMARK 500 1 PHE A 323 162.03 168.72
REMARK 500 1 TYR A 325 91.50 -179.51
REMARK 500 1 LEU A 327 -166.76 -60.73
REMARK 500 1 SER A 333 96.72 -37.67
REMARK 500 1 ASN A 339 -174.49 -52.62
REMARK 500 1 ASN A 357 161.04 -49.55
REMARK 500 1 LEU A 358 -90.99 -116.76
REMARK 500 1 ARG A 359 153.10 80.04
REMARK 500 1 LEU A 364 -60.15 -97.81
REMARK 500 2 PRO A 257 -76.90 -75.00
REMARK 500 2 ARG A 260 -175.52 -58.50
REMARK 500 2 ARG A 269 -166.45 -103.77
REMARK 500 2 ASN A 279 97.01 -47.50
REMARK 500 2 THR A 281 176.86 -51.88
REMARK 500 2 SER A 283 -81.53 -121.17
REMARK 500 2 VAL A 284 155.52 166.09
REMARK 500 2 THR A 294 127.08 -170.83
REMARK 500 2 ALA A 296 -76.38 -126.33
REMARK 500 2 PRO A 300 -161.27 -75.01
REMARK 500 2 THR A 302 39.47 -89.35
REMARK 500 2 LYS A 315 24.22 49.36
REMARK 500 2 GLU A 316 -169.14 -76.44
REMARK 500 2 PHE A 323 165.62 173.98
REMARK 500 2 TYR A 325 101.61 -178.04
REMARK 500 2 LEU A 327 -162.72 -69.69
REMARK 500 2 LEU A 329 154.18 -38.43
REMARK 500 2 SER A 333 98.71 -36.71
REMARK 500 2 ASN A 339 -174.41 -52.83
REMARK 500 2 SER A 353 162.65 84.34
REMARK 500 2 LEU A 358 -87.78 -121.52
REMARK 500 2 ARG A 359 158.20 71.30
REMARK 500 3 GLU A 255 70.19 40.26
REMARK 500 3 PRO A 257 -162.74 -74.95
REMARK 500 3 ASN A 258 -71.65 -120.11
REMARK 500 3 ARG A 260 -175.63 -57.23
REMARK 500 3 ARG A 269 -159.24 -129.75
REMARK 500 3 SER A 272 169.60 179.46
REMARK 500 3 ASN A 279 92.64 -52.62
REMARK 500 3 SER A 283 -79.76 -140.16
REMARK 500
REMARK 500 THIS ENTRY HAS 449 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 17006 RELATED DB: BMRB
DBREF 2KZB A 254 367 UNP P35193 ATG19_YEAST 254 367
SEQADV 2KZB GLY A 250 UNP P35193 EXPRESSION TAG
SEQADV 2KZB PRO A 251 UNP P35193 EXPRESSION TAG
SEQADV 2KZB HIS A 252 UNP P35193 EXPRESSION TAG
SEQADV 2KZB MET A 253 UNP P35193 EXPRESSION TAG
SEQRES 1 A 118 GLY PRO HIS MET VAL GLU PRO PRO ASN GLU ARG SER LEU
SEQRES 2 A 118 GLN ILE THR MET ASN GLN ARG ASP ASN SER LEU TYR PHE
SEQRES 3 A 118 GLN LEU PHE ASN ASN THR ASN SER VAL LEU ALA GLY ASN
SEQRES 4 A 118 CYS LYS LEU LYS PHE THR ASP ALA GLY ASP LYS PRO THR
SEQRES 5 A 118 THR GLN ILE ILE ASP MET GLY PRO HIS GLU ILE GLY ILE
SEQRES 6 A 118 LYS GLU TYR LYS GLU TYR ARG TYR PHE PRO TYR ALA LEU
SEQRES 7 A 118 ASP LEU GLU ALA GLY SER THR ILE GLU ILE GLU ASN GLN
SEQRES 8 A 118 TYR GLY GLU VAL ILE PHE LEU GLY LYS TYR GLY SER SER
SEQRES 9 A 118 PRO MET ILE ASN LEU ARG PRO PRO SER ARG LEU SER ALA
SEQRES 10 A 118 GLU
SHEET 1 A 4 LYS A 318 TYR A 322 0
SHEET 2 A 4 SER A 272 ASN A 279 -1 N PHE A 275 O TYR A 320
SHEET 3 A 4 LEU A 262 ARG A 269 -1 N ARG A 269 O SER A 272
SHEET 4 A 4 ILE A 356 ASN A 357 -1 O ILE A 356 N ILE A 264
SHEET 1 B 4 ILE A 305 ASP A 306 0
SHEET 2 B 4 LYS A 290 LEU A 291 -1 N LEU A 291 O ILE A 305
SHEET 3 B 4 ILE A 335 GLU A 338 -1 O GLU A 338 N LYS A 290
SHEET 4 B 4 VAL A 344 GLY A 348 -1 O ILE A 345 N ILE A 337
CISPEP 1 PHE A 323 PRO A 324 1 -0.04
CISPEP 2 PHE A 323 PRO A 324 2 -0.01
CISPEP 3 PHE A 323 PRO A 324 3 0.03
CISPEP 4 PHE A 323 PRO A 324 4 0.00
CISPEP 5 PHE A 323 PRO A 324 5 0.05
CISPEP 6 PHE A 323 PRO A 324 6 0.02
CISPEP 7 PHE A 323 PRO A 324 7 0.02
CISPEP 8 PHE A 323 PRO A 324 8 0.04
CISPEP 9 PHE A 323 PRO A 324 9 0.00
CISPEP 10 PHE A 323 PRO A 324 10 -0.08
CISPEP 11 PHE A 323 PRO A 324 11 -0.05
CISPEP 12 PHE A 323 PRO A 324 12 0.04
CISPEP 13 PHE A 323 PRO A 324 13 0.00
CISPEP 14 PHE A 323 PRO A 324 14 0.00
CISPEP 15 PHE A 323 PRO A 324 15 -0.03
CISPEP 16 PHE A 323 PRO A 324 16 0.02
CISPEP 17 PHE A 323 PRO A 324 17 -0.08
CISPEP 18 PHE A 323 PRO A 324 18 -0.13
CISPEP 19 PHE A 323 PRO A 324 19 0.01
CISPEP 20 PHE A 323 PRO A 324 20 0.01
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
(ATOM LINES ARE NOT SHOWN.)
END
