HEADER PROTEIN TRANSPORT 29-AUG-10 3ONL
TITLE YEAST ENT3_ENTH-VTI1P_HABC COMPLEX STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EPSIN-3;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: ENTH DOMAIN, RESIDUES 28-170;
COMPND 5 SYNONYM: ENT3;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: T-SNARE VTI1;
COMPND 9 CHAIN: C;
COMPND 10 FRAGMENT: HABC DOMAIN, RESIDUES 3-99;
COMPND 11 SYNONYM: VESICLE TRANSPORT V-SNARE PROTEIN VTI1, QB-SNARE VTI1,
COMPND 12 VPS10-INTERACTING PROTEIN 1;
COMPND 13 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET22B(+);
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 12 ORGANISM_COMMON: YEAST;
SOURCE 13 ORGANISM_TAXID: 4932;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 16 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PET22B(+)
KEYWDS HELIX, ENTH, HABC, RECOGNITION BETWEEN SNARE AND ADAPTOR, PROTEIN
KEYWDS 2 TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR J.WANG,P.FANG,L.NIU,M.TENG
REVDAT 4 01-NOV-23 3ONL 1 SEQADV
REVDAT 3 02-APR-14 3ONL 1 REMARK
REVDAT 2 21-DEC-11 3ONL 1 JRNL
REVDAT 1 20-JUL-11 3ONL 0
JRNL AUTH J.WANG,M.GOSSING,P.FANG,J.ZIMMERMANN,X.LI,G.F.VON MOLLARD,
JRNL AUTH 2 L.NIU,M.TENG
JRNL TITL EPSIN N-TERMINAL HOMOLOGY DOMAINS BIND ON OPPOSITE SIDES OF
JRNL TITL 2 TWO SNARES
JRNL REF PROC.NATL.ACAD.SCI.USA V. 108 12277 2011
JRNL REFN ISSN 0027-8424
JRNL PMID 21746902
JRNL DOI 10.1073/PNAS.1013101108
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.71
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 3 NUMBER OF REFLECTIONS : 23725
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.226
REMARK 3 R VALUE (WORKING SET) : 0.223
REMARK 3 FREE R VALUE : 0.269
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1213
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.26
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1528
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.25
REMARK 3 BIN R VALUE (WORKING SET) : 0.2800
REMARK 3 BIN FREE R VALUE SET COUNT : 88
REMARK 3 BIN FREE R VALUE : 0.2920
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2977
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 180
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.57
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.33000
REMARK 3 B22 (A**2) : 0.49000
REMARK 3 B33 (A**2) : -0.83000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.228
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.931
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.903
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3020 ; 0.008 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4068 ; 1.051 ; 1.952
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 368 ; 4.234 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 159 ;33.487 ;24.088
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 561 ;16.304 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 30 ;19.121 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 453 ; 0.076 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2279 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1843 ; 2.040 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2961 ; 3.919 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1177 ; 4.422 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1107 ; 7.478 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES: REFINED INDIVIDUALLY
REMARK 4
REMARK 4 3ONL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-SEP-10.
REMARK 100 THE DEPOSITION ID IS D_1000061341.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JAN-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
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) : 1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23733
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
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 (%) : 98.4
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) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.6
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRIES 3ONJ AND 3ONK
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.94
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.51
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M TRI-LITHIUM CITRATE TETRAHYDRATE,
REMARK 280 20% PEG 3350, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 288.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
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
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 29.34150
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 47.97650
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.17550
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 47.97650
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 29.34150
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 41.17550
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 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 300 REMARK: THERE IS AN 1:1 COMPLEX FORMING BY TWO MONOMERIC PROTEIN.
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 APPLY THE FOLLOWING TO CHAINS: A, B, C
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 SER A 21
REMARK 465 LEU A 22
REMARK 465 MET A 23
REMARK 465 ALA A 164
REMARK 465 LYS A 165
REMARK 465 LYS A 166
REMARK 465 TYR A 167
REMARK 465 LYS A 168
REMARK 465 GLY A 169
REMARK 465 VAL A 170
REMARK 465 SER B 21
REMARK 465 LEU B 22
REMARK 465 MET B 23
REMARK 465 SER B 24
REMARK 465 VAL B 25
REMARK 465 ASP B 26
REMARK 465 PRO B 27
REMARK 465 ALA B 164
REMARK 465 LYS B 165
REMARK 465 LYS B 166
REMARK 465 TYR B 167
REMARK 465 LYS B 168
REMARK 465 GLY B 169
REMARK 465 VAL B 170
REMARK 465 GLY C 98
REMARK 465 ASP C 99
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 SER A 24 OG
REMARK 470 VAL A 25 CG1 CG2
REMARK 470 PHE A 62 CD2 CE1 CE2 CZ
REMARK 470 LEU A 69 CD2
REMARK 470 ARG A 75 CZ NH1 NH2
REMARK 470 SER A 127 OG
REMARK 470 GLN A 128 CG CD OE1 NE2
REMARK 470 LYS A 141 CG CD CE NZ
REMARK 470 GLU A 145 CG CD OE1 OE2
REMARK 470 LYS A 152 CG CD CE NZ
REMARK 470 LYS A 159 CD CE NZ
REMARK 470 GLU A 162 CG CD OE1 OE2
REMARK 470 THR B 77 OG1 CG2
REMARK 470 GLU B 78 CG CD OE1 OE2
REMARK 470 ARG B 104 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 158 CD CE NZ
REMARK 470 LYS B 159 CE NZ
REMARK 470 ARG B 161 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 162 CG CD OE1 OE2
REMARK 470 LYS C 13 CE NZ
REMARK 470 GLU C 17 CG CD OE1 OE2
REMARK 470 ARG C 69 CG CD NE CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG B 157 NE - CZ - NH2 ANGL. DEV. = -3.9 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 SER A 127 33.31 -81.99
REMARK 500 GLN A 128 3.82 -150.18
REMARK 500 TYR B 124 118.13 -166.52
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3ONJ RELATED DB: PDB
REMARK 900 YEAST VTI1P_HABC DOMAIN
REMARK 900 RELATED ID: 3ONK RELATED DB: PDB
REMARK 900 YEAST ENT3_ENTH DOMAIN
DBREF 3ONL A 28 170 UNP P47160 ENT3_YEAST 28 170
DBREF 3ONL B 28 170 UNP P47160 ENT3_YEAST 28 170
DBREF 3ONL C 3 99 UNP Q04338 VTI1_YEAST 3 99
SEQADV 3ONL SER A 21 UNP P47160 EXPRESSION TAG
SEQADV 3ONL LEU A 22 UNP P47160 EXPRESSION TAG
SEQADV 3ONL MET A 23 UNP P47160 EXPRESSION TAG
SEQADV 3ONL SER A 24 UNP P47160 EXPRESSION TAG
SEQADV 3ONL VAL A 25 UNP P47160 EXPRESSION TAG
SEQADV 3ONL ASP A 26 UNP P47160 EXPRESSION TAG
SEQADV 3ONL PRO A 27 UNP P47160 EXPRESSION TAG
SEQADV 3ONL SER B 21 UNP P47160 EXPRESSION TAG
SEQADV 3ONL LEU B 22 UNP P47160 EXPRESSION TAG
SEQADV 3ONL MET B 23 UNP P47160 EXPRESSION TAG
SEQADV 3ONL SER B 24 UNP P47160 EXPRESSION TAG
SEQADV 3ONL VAL B 25 UNP P47160 EXPRESSION TAG
SEQADV 3ONL ASP B 26 UNP P47160 EXPRESSION TAG
SEQADV 3ONL PRO B 27 UNP P47160 EXPRESSION TAG
SEQRES 1 A 150 SER LEU MET SER VAL ASP PRO ASN TYR THR GLU MET GLU
SEQRES 2 A 150 GLY LYS VAL ARG GLU ALA THR ASN ASN GLU PRO TRP GLY
SEQRES 3 A 150 ALA SER SER THR LEU MET ASP GLN ILE SER GLN GLY THR
SEQRES 4 A 150 TYR ASN PHE ARG GLU ARG GLU GLU ILE LEU SER MET ILE
SEQRES 5 A 150 PHE ARG ARG PHE THR GLU LYS ALA GLY SER GLU TRP ARG
SEQRES 6 A 150 GLN ILE TYR LYS ALA LEU GLN LEU LEU ASP TYR LEU ILE
SEQRES 7 A 150 LYS HIS GLY SER GLU ARG PHE ILE ASP ASP THR ARG ASN
SEQRES 8 A 150 SER ILE ASN LEU ILE ARG ILE LEU GLU THR PHE HIS TYR
SEQRES 9 A 150 ILE ASP SER GLN GLY ARG ASP GLN GLY ILE ASN VAL ARG
SEQRES 10 A 150 THR ARG VAL LYS ALA LEU ILE GLU LEU LEU SER ASP ASP
SEQRES 11 A 150 ASN LYS ILE ARG ALA GLU ARG LYS LYS ALA ARG GLU THR
SEQRES 12 A 150 ALA LYS LYS TYR LYS GLY VAL
SEQRES 1 B 150 SER LEU MET SER VAL ASP PRO ASN TYR THR GLU MET GLU
SEQRES 2 B 150 GLY LYS VAL ARG GLU ALA THR ASN ASN GLU PRO TRP GLY
SEQRES 3 B 150 ALA SER SER THR LEU MET ASP GLN ILE SER GLN GLY THR
SEQRES 4 B 150 TYR ASN PHE ARG GLU ARG GLU GLU ILE LEU SER MET ILE
SEQRES 5 B 150 PHE ARG ARG PHE THR GLU LYS ALA GLY SER GLU TRP ARG
SEQRES 6 B 150 GLN ILE TYR LYS ALA LEU GLN LEU LEU ASP TYR LEU ILE
SEQRES 7 B 150 LYS HIS GLY SER GLU ARG PHE ILE ASP ASP THR ARG ASN
SEQRES 8 B 150 SER ILE ASN LEU ILE ARG ILE LEU GLU THR PHE HIS TYR
SEQRES 9 B 150 ILE ASP SER GLN GLY ARG ASP GLN GLY ILE ASN VAL ARG
SEQRES 10 B 150 THR ARG VAL LYS ALA LEU ILE GLU LEU LEU SER ASP ASP
SEQRES 11 B 150 ASN LYS ILE ARG ALA GLU ARG LYS LYS ALA ARG GLU THR
SEQRES 12 B 150 ALA LYS LYS TYR LYS GLY VAL
SEQRES 1 C 97 SER LEU LEU ILE SER TYR GLU SER ASP PHE LYS THR THR
SEQRES 2 C 97 LEU GLU GLN ALA LYS ALA SER LEU ALA GLU ALA PRO SER
SEQRES 3 C 97 GLN PRO LEU SER GLN ARG ASN THR THR LEU LYS HIS VAL
SEQRES 4 C 97 GLU GLN GLN GLN ASP GLU LEU PHE ASP LEU LEU ASP GLN
SEQRES 5 C 97 MET ASP VAL GLU VAL ASN ASN SER ILE GLY ASP ALA SER
SEQRES 6 C 97 GLU ARG ALA THR TYR LYS ALA LYS LEU ARG GLU TRP LYS
SEQRES 7 C 97 LYS THR ILE GLN SER ASP ILE LYS ARG PRO LEU GLN SER
SEQRES 8 C 97 LEU VAL ASP SER GLY ASP
FORMUL 4 HOH *180(H2 O)
HELIX 1 1 THR A 30 THR A 40 1 11
HELIX 2 2 SER A 48 THR A 59 1 12
HELIX 3 3 ASN A 61 LYS A 79 1 19
HELIX 4 4 ALA A 80 SER A 82 5 3
HELIX 5 5 GLU A 83 GLY A 101 1 19
HELIX 6 6 SER A 102 SER A 112 1 11
HELIX 7 7 SER A 112 ILE A 118 1 7
HELIX 8 8 LEU A 119 PHE A 122 5 4
HELIX 9 9 GLN A 132 SER A 148 1 17
HELIX 10 10 ASP A 149 THR A 163 1 15
HELIX 11 11 THR B 30 THR B 40 1 11
HELIX 12 12 SER B 48 THR B 59 1 12
HELIX 13 13 ASN B 61 LYS B 79 1 19
HELIX 14 14 ALA B 80 SER B 82 5 3
HELIX 15 15 GLU B 83 GLY B 101 1 19
HELIX 16 16 SER B 102 SER B 112 1 11
HELIX 17 17 SER B 112 ILE B 118 1 7
HELIX 18 18 LEU B 119 PHE B 122 5 4
HELIX 19 19 GLN B 132 SER B 148 1 17
HELIX 20 20 ASP B 149 THR B 163 1 15
HELIX 21 21 SER C 3 ALA C 26 1 24
HELIX 22 22 PRO C 27 GLN C 29 5 3
HELIX 23 23 PRO C 30 ILE C 63 1 34
HELIX 24 24 ASP C 65 ILE C 87 1 23
HELIX 25 25 ILE C 87 SER C 97 1 11
CISPEP 1 GLU B 43 PRO B 44 0 -7.61
CRYST1 58.683 82.351 95.953 90.00 90.00 90.00 P 21 21 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.017041 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012143 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010422 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
