HEADER PROTEIN TRANSPORT 01-OCT-09 3A7O
TITLE THE CRYSTAL STRUCTURE OF THE COILED-COIL DOMAIN OF SACCHAROMYCES
TITLE 2 CEREVISIAE ATG16
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: AUTOPHAGY PROTEIN 16;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 FRAGMENT: COILED-COIL DOMAIN;
COMPND 5 SYNONYM: ATG16, CYTOPLASM TO VACUOLE TARGETING PROTEIN 11, SAP18
COMPND 6 HOMOLOG;
COMPND 7 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: ATG16;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX6P
KEYWDS COILED-COIL, AUTOPHAGY, COILED COIL, CYTOPLASMIC VESICLE, PROTEIN
KEYWDS 2 TRANSPORT, TRANSPORT, VACUOLE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.FUJIOKA,N.N.NODA,F.INAGAKI
REVDAT 2 18-OCT-23 3A7O 1 JRNL SEQADV
REVDAT 1 03-NOV-09 3A7O 0
JRNL AUTH Y.FUJIOKA,N.N.NODA,H.NAKATOGAWA,Y.OHSUMI,F.INAGAKI
JRNL TITL DIMERIC COILED-COIL STRUCTURE OF SACCHAROMYCES CEREVISIAE
JRNL TITL 2 ATG16 AND ITS FUNCTIONAL SIGNIFICANCE IN AUTOPHAGY.
JRNL REF J.BIOL.CHEM. V. 285 1508 2010
JRNL REFN ESSN 1083-351X
JRNL PMID 19889643
JRNL DOI 10.1074/JBC.M109.053520
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.08
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.4
REMARK 3 NUMBER OF REFLECTIONS : 22516
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.272
REMARK 3 FREE R VALUE : 0.299
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1094
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.66
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.70
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3460
REMARK 3 BIN FREE R VALUE : 0.4310
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 160
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.034
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2662
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 82
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 56.50
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 5.66000
REMARK 3 B22 (A**2) : 5.66000
REMARK 3 B33 (A**2) : -11.32000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.000
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 16.20
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.660
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.530 ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3A7O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-OCT-09.
REMARK 100 THE DEPOSITION ID IS D_1000028914.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-JUL-08; 23-JUL-08
REMARK 200 TEMPERATURE (KELVIN) : 95; 110
REMARK 200 PH : 5.0
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; N
REMARK 200 RADIATION SOURCE : SPRING-8; ROTATING ANODE
REMARK 200 BEAMLINE : BL41XU; NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL; RIGAKU MICROMAX-007
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1000; 1.5418
REMARK 200 MONOCHROMATOR : NULL; NULL
REMARK 200 OPTICS : NULL; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-225; RIGAKU RAXIS VII
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22847
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 17.90
REMARK 200 R MERGE (I) : 0.06900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.28200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; 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 (%): 61.26
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.8M AMMONIUM CHLORIDE, 0.1M SODIUM
REMARK 280 ACETATE, PH 5.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
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 38.90400
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 63.94550
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 63.94550
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 58.35600
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 63.94550
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 63.94550
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 19.45200
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 63.94550
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 63.94550
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 58.35600
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 63.94550
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 63.94550
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 19.45200
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 38.90400
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2560 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 8350 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 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: 2470 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 8130 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 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 350
REMARK 350 BIOMOLECULE: 3
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: 2590 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 8700 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH F 130 LIES ON A SPECIAL POSITION.
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 49
REMARK 465 SER A 50
REMARK 465 GLY A 51
REMARK 465 ALA A 52
REMARK 465 ILE A 53
REMARK 465 GLY A 54
REMARK 465 GLY A 55
REMARK 465 ASN A 56
REMARK 465 ILE A 57
REMARK 465 VAL A 58
REMARK 465 SER A 59
REMARK 465 ASP A 119
REMARK 465 LEU A 120
REMARK 465 LYS A 121
REMARK 465 LYS A 122
REMARK 465 GLU A 123
REMARK 465 GLY B 49
REMARK 465 SER B 50
REMARK 465 GLY B 51
REMARK 465 ALA B 52
REMARK 465 ILE B 53
REMARK 465 GLY B 54
REMARK 465 GLY B 55
REMARK 465 ASN B 56
REMARK 465 ILE B 57
REMARK 465 VAL B 58
REMARK 465 SER B 59
REMARK 465 HIS B 60
REMARK 465 GLN B 115
REMARK 465 LYS B 116
REMARK 465 LEU B 117
REMARK 465 SER B 118
REMARK 465 ASP B 119
REMARK 465 LEU B 120
REMARK 465 LYS B 121
REMARK 465 LYS B 122
REMARK 465 GLU B 123
REMARK 465 GLY C 49
REMARK 465 SER C 50
REMARK 465 GLY C 51
REMARK 465 ALA C 52
REMARK 465 ILE C 53
REMARK 465 GLY C 54
REMARK 465 GLY C 55
REMARK 465 ASN C 56
REMARK 465 ILE C 57
REMARK 465 VAL C 58
REMARK 465 SER C 59
REMARK 465 LEU C 113
REMARK 465 GLN C 114
REMARK 465 GLN C 115
REMARK 465 LYS C 116
REMARK 465 LEU C 117
REMARK 465 SER C 118
REMARK 465 ASP C 119
REMARK 465 LEU C 120
REMARK 465 LYS C 121
REMARK 465 LYS C 122
REMARK 465 GLU C 123
REMARK 465 GLY D 49
REMARK 465 SER D 50
REMARK 465 GLY D 51
REMARK 465 ALA D 52
REMARK 465 ILE D 53
REMARK 465 GLY D 54
REMARK 465 GLY D 55
REMARK 465 ASN D 56
REMARK 465 ILE D 57
REMARK 465 VAL D 58
REMARK 465 LEU D 117
REMARK 465 SER D 118
REMARK 465 ASP D 119
REMARK 465 LEU D 120
REMARK 465 LYS D 121
REMARK 465 LYS D 122
REMARK 465 GLU D 123
REMARK 465 GLY E 49
REMARK 465 SER E 50
REMARK 465 GLY E 51
REMARK 465 ALA E 52
REMARK 465 ILE E 53
REMARK 465 GLY E 54
REMARK 465 GLY E 55
REMARK 465 ASN E 56
REMARK 465 ILE E 57
REMARK 465 VAL E 58
REMARK 465 SER E 59
REMARK 465 LEU E 120
REMARK 465 LYS E 121
REMARK 465 LYS E 122
REMARK 465 GLU E 123
REMARK 465 GLY F 49
REMARK 465 SER F 50
REMARK 465 GLY F 51
REMARK 465 ALA F 52
REMARK 465 ILE F 53
REMARK 465 GLY F 54
REMARK 465 GLY F 55
REMARK 465 ASN F 56
REMARK 465 ILE F 57
REMARK 465 VAL F 58
REMARK 465 SER F 59
REMARK 465 HIS F 60
REMARK 465 ASP F 119
REMARK 465 LEU F 120
REMARK 465 LYS F 121
REMARK 465 LYS F 122
REMARK 465 GLU F 123
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 60 CG ND1 CD2 CE1 NE2
REMARK 470 LYS A 94 CG CD CE NZ
REMARK 470 GLN A 114 CG CD OE1 NE2
REMARK 470 GLN A 115 CG CD OE1 NE2
REMARK 470 LYS A 116 CG CD CE NZ
REMARK 470 SER A 118 OG
REMARK 470 LYS B 73 CG CD CE NZ
REMARK 470 LYS B 94 CG CD CE NZ
REMARK 470 GLN C 80 CG CD OE1 NE2
REMARK 470 ARG C 83 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 94 CG CD CE NZ
REMARK 470 SER D 59 OG
REMARK 470 HIS D 60 CG ND1 CD2 CE1 NE2
REMARK 470 LYS D 76 CG CD CE NZ
REMARK 470 GLN D 115 CG CD OE1 NE2
REMARK 470 LYS D 116 CG CD CE NZ
REMARK 470 HIS E 60 CG ND1 CD2 CE1 NE2
REMARK 470 LYS E 73 CG CD CE NZ
REMARK 470 ARG E 83 CG CD NE CZ NH1 NH2
REMARK 470 GLN E 114 CG CD OE1 NE2
REMARK 470 GLN E 115 CG CD OE1 NE2
REMARK 470 LYS E 116 CG CD CE NZ
REMARK 470 LEU E 117 CG CD1 CD2
REMARK 470 ASP E 119 CG OD1 OD2
REMARK 470 LYS F 116 CG CD CE NZ
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 OE1 GLN D 114 OE1 GLN D 114 7556 2.03
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 LEU F 113 -71.81 -61.75
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3A7P RELATED DB: PDB
DBREF 3A7O A 50 123 UNP Q03818 ATG16_YEAST 50 123
DBREF 3A7O B 50 123 UNP Q03818 ATG16_YEAST 50 123
DBREF 3A7O C 50 123 UNP Q03818 ATG16_YEAST 50 123
DBREF 3A7O D 50 123 UNP Q03818 ATG16_YEAST 50 123
DBREF 3A7O E 50 123 UNP Q03818 ATG16_YEAST 50 123
DBREF 3A7O F 50 123 UNP Q03818 ATG16_YEAST 50 123
SEQADV 3A7O GLY A 49 UNP Q03818 EXPRESSION TAG
SEQADV 3A7O GLY B 49 UNP Q03818 EXPRESSION TAG
SEQADV 3A7O GLY C 49 UNP Q03818 EXPRESSION TAG
SEQADV 3A7O GLY D 49 UNP Q03818 EXPRESSION TAG
SEQADV 3A7O GLY E 49 UNP Q03818 EXPRESSION TAG
SEQADV 3A7O GLY F 49 UNP Q03818 EXPRESSION TAG
SEQRES 1 A 75 GLY SER GLY ALA ILE GLY GLY ASN ILE VAL SER HIS ASP
SEQRES 2 A 75 ASP ALA LEU LEU ASN THR LEU ALA ILE LEU GLN LYS GLU
SEQRES 3 A 75 LEU LYS SER LYS GLU GLN GLU ILE ARG ARG LEU LYS GLU
SEQRES 4 A 75 VAL ILE ALA LEU LYS ASN LYS ASN THR GLU ARG LEU ASN
SEQRES 5 A 75 ASP GLU LEU ILE SER GLY THR ILE GLU ASN ASN VAL LEU
SEQRES 6 A 75 GLN GLN LYS LEU SER ASP LEU LYS LYS GLU
SEQRES 1 B 75 GLY SER GLY ALA ILE GLY GLY ASN ILE VAL SER HIS ASP
SEQRES 2 B 75 ASP ALA LEU LEU ASN THR LEU ALA ILE LEU GLN LYS GLU
SEQRES 3 B 75 LEU LYS SER LYS GLU GLN GLU ILE ARG ARG LEU LYS GLU
SEQRES 4 B 75 VAL ILE ALA LEU LYS ASN LYS ASN THR GLU ARG LEU ASN
SEQRES 5 B 75 ASP GLU LEU ILE SER GLY THR ILE GLU ASN ASN VAL LEU
SEQRES 6 B 75 GLN GLN LYS LEU SER ASP LEU LYS LYS GLU
SEQRES 1 C 75 GLY SER GLY ALA ILE GLY GLY ASN ILE VAL SER HIS ASP
SEQRES 2 C 75 ASP ALA LEU LEU ASN THR LEU ALA ILE LEU GLN LYS GLU
SEQRES 3 C 75 LEU LYS SER LYS GLU GLN GLU ILE ARG ARG LEU LYS GLU
SEQRES 4 C 75 VAL ILE ALA LEU LYS ASN LYS ASN THR GLU ARG LEU ASN
SEQRES 5 C 75 ASP GLU LEU ILE SER GLY THR ILE GLU ASN ASN VAL LEU
SEQRES 6 C 75 GLN GLN LYS LEU SER ASP LEU LYS LYS GLU
SEQRES 1 D 75 GLY SER GLY ALA ILE GLY GLY ASN ILE VAL SER HIS ASP
SEQRES 2 D 75 ASP ALA LEU LEU ASN THR LEU ALA ILE LEU GLN LYS GLU
SEQRES 3 D 75 LEU LYS SER LYS GLU GLN GLU ILE ARG ARG LEU LYS GLU
SEQRES 4 D 75 VAL ILE ALA LEU LYS ASN LYS ASN THR GLU ARG LEU ASN
SEQRES 5 D 75 ASP GLU LEU ILE SER GLY THR ILE GLU ASN ASN VAL LEU
SEQRES 6 D 75 GLN GLN LYS LEU SER ASP LEU LYS LYS GLU
SEQRES 1 E 75 GLY SER GLY ALA ILE GLY GLY ASN ILE VAL SER HIS ASP
SEQRES 2 E 75 ASP ALA LEU LEU ASN THR LEU ALA ILE LEU GLN LYS GLU
SEQRES 3 E 75 LEU LYS SER LYS GLU GLN GLU ILE ARG ARG LEU LYS GLU
SEQRES 4 E 75 VAL ILE ALA LEU LYS ASN LYS ASN THR GLU ARG LEU ASN
SEQRES 5 E 75 ASP GLU LEU ILE SER GLY THR ILE GLU ASN ASN VAL LEU
SEQRES 6 E 75 GLN GLN LYS LEU SER ASP LEU LYS LYS GLU
SEQRES 1 F 75 GLY SER GLY ALA ILE GLY GLY ASN ILE VAL SER HIS ASP
SEQRES 2 F 75 ASP ALA LEU LEU ASN THR LEU ALA ILE LEU GLN LYS GLU
SEQRES 3 F 75 LEU LYS SER LYS GLU GLN GLU ILE ARG ARG LEU LYS GLU
SEQRES 4 F 75 VAL ILE ALA LEU LYS ASN LYS ASN THR GLU ARG LEU ASN
SEQRES 5 F 75 ASP GLU LEU ILE SER GLY THR ILE GLU ASN ASN VAL LEU
SEQRES 6 F 75 GLN GLN LYS LEU SER ASP LEU LYS LYS GLU
FORMUL 7 HOH *82(H2 O)
HELIX 1 1 HIS A 60 SER A 118 1 59
HELIX 2 2 ASP B 61 LEU B 113 1 53
HELIX 3 3 HIS C 60 GLU C 109 1 50
HELIX 4 4 SER D 59 LYS D 116 1 58
HELIX 5 5 HIS E 60 ASP E 119 1 60
HELIX 6 6 ASP F 61 LEU F 117 1 57
CRYST1 127.891 127.891 77.808 90.00 90.00 90.00 P 43 21 2 48
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 0.007819 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007819 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012852 0.00000
(ATOM LINES ARE NOT SHOWN.)
END