HEADER EXOCYTOSIS 31-AUG-12 4B93
TITLE COMPLEX OF VAMP7 CYTOPLASMIC DOMAIN WITH 2ND ANKYRIN REPEAT DOMAIN OF
TITLE 2 VARP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: VESICLE-ASSOCIATED MEMBRANE PROTEIN 7;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CYTOPLASMIC DOMAIN, RESIDUES 1-188;
COMPND 5 SYNONYM: VAMP-7, SYNAPTOBREVIN-LIKE PROTEIN 1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: ANKYRIN REPEAT DOMAIN-CONTAINING PROTEIN 27;
COMPND 9 CHAIN: B;
COMPND 10 FRAGMENT: 2ND ANKYRIN REPEAT DOMAIN, RESIDUES 659-921;
COMPND 11 SYNONYM: VARP, VPS9 DOMAIN-CONTAINING PROTEIN;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: ROSETTA2 PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: VAMP7;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 17 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 18 EXPRESSION_SYSTEM_VARIANT: ROSETTA2 PLYSS;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: VARP658-921
KEYWDS ENDOCYTOSIS, EXOCYTOSIS, SNARE
EXPDTA X-RAY DIFFRACTION
AUTHOR I.B.SCHAEFER,D.J.OWEN,J.P.LUZIO,P.R.EVANS
REVDAT 5 08-MAY-19 4B93 1 REMARK
REVDAT 4 03-APR-19 4B93 1 REMARK
REVDAT 3 25-JAN-17 4B93 1 REMARK
REVDAT 2 19-DEC-12 4B93 1 JRNL
REVDAT 1 31-OCT-12 4B93 0
JRNL AUTH I.B.SCHAFER,G.G.HESKETH,N.A.BRIGHT,S.R.GRAY,P.R.PRYOR,
JRNL AUTH 2 P.R.EVANS,J.P.LUZIO,D.J.OWEN
JRNL TITL THE BINDING OF VARP TO VAMP7 TRAPS VAMP7 IN A CLOSED,
JRNL TITL 2 FUSOGENICALLY INACTIVE CONFORMATION.
JRNL REF NAT.STRUCT.MOL.BIOL. V. 19 1300 2012
JRNL REFN ISSN 1545-9993
JRNL PMID 23104059
JRNL DOI 10.1038/NSMB.2414
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0018
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.85
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 43692
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) : 0.215
REMARK 3 R VALUE (WORKING SET) : 0.213
REMARK 3 FREE R VALUE : 0.251
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2332
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3184
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.00
REMARK 3 BIN R VALUE (WORKING SET) : 0.3910
REMARK 3 BIN FREE R VALUE SET COUNT : 172
REMARK 3 BIN FREE R VALUE : 0.4210
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2707
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 209
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 49.15
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.83000
REMARK 3 B22 (A**2) : 1.07000
REMARK 3 B33 (A**2) : -3.90000
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): 0.131
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.132
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.125
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.895
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.962
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.946
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2758 ; 0.018 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2695 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3728 ; 1.837 ; 1.951
REMARK 3 BOND ANGLES OTHERS (DEGREES): 6169 ; 0.876 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 346 ; 6.884 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 131 ;33.262 ;24.580
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 488 ;15.701 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 17 ;17.785 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 431 ; 0.107 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3151 ; 0.009 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 646 ; 0.001 ; 0.020
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): 2758 ; 4.283 ; 4.877
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2695 ; 1.236 ; 4.980
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3727 ; 6.189 ; 7.223
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : 1.20
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 4B93 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 31-AUG-12.
REMARK 100 THE DEPOSITION ID IS D_1290053930.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JAN-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : SI111
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 43692
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 56.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 100.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.05
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.5
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : 0.96000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIRAS
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NONE
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.91
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.32
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 5 TO 7.5 % (V/V) ISOPROPANOL AND 0.1 M
REMARK 280 IMIDAZOLE PH 6.5-7.8 IN HANGING AND SITTING DROPS AT 4 DEGREES,
REMARK 280 PH 7, VAPOR DIFFUSION, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
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 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 79.30000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 79.30000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 34.78500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 61.33000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 34.78500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 61.33000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 79.30000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 34.78500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 61.33000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 79.30000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 34.78500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 61.33000
REMARK 290 SMTRY3 8 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 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 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 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 LYS A 121
REMARK 465 SER A 122
REMARK 465 LEU A 123
REMARK 465 ASP A 124
REMARK 465 LYS A 125
REMARK 465 VAL A 126
REMARK 465 MET A 127
REMARK 465 LEU A 164
REMARK 465 VAL A 165
REMARK 465 ASP A 166
REMARK 465 SER A 167
REMARK 465 SER A 168
REMARK 465 VAL A 169
REMARK 465 THR A 170
REMARK 465 PHE A 171
REMARK 465 LYS A 172
REMARK 465 THR A 173
REMARK 465 THR A 174
REMARK 465 SER A 175
REMARK 465 ARG A 176
REMARK 465 ASN A 177
REMARK 465 LEU A 178
REMARK 465 ALA A 179
REMARK 465 ARG A 180
REMARK 465 ALA A 181
REMARK 465 MET A 182
REMARK 465 CYS A 183
REMARK 465 MET A 184
REMARK 465 LYS A 185
REMARK 465 ASN A 186
REMARK 465 ILE A 187
REMARK 465 LYS A 188
REMARK 465 ARG B 659
REMARK 465 GLN B 660
REMARK 465 GLU B 661
REMARK 465 GLU B 662
REMARK 465 THR B 663
REMARK 465 LYS B 664
REMARK 465 GLU B 693
REMARK 465 GLU B 694
REMARK 465 ASP B 695
REMARK 465 LEU B 696
REMARK 465 GLU B 697
REMARK 465 ASP B 698
REMARK 465 ALA B 699
REMARK 465 GLU B 700
REMARK 465 ASP B 701
REMARK 465 THR B 702
REMARK 465 VAL B 703
REMARK 465 SER B 704
REMARK 465 ALA B 705
REMARK 465 ALA B 706
REMARK 465 ASP B 707
REMARK 465 PRO B 708
REMARK 465 GLU B 709
REMARK 465 PHE B 710
REMARK 465 CYS B 711
REMARK 465 HIS B 712
REMARK 465 PRO B 713
REMARK 465 LEU B 714
REMARK 465 CYS B 715
REMARK 465 GLN B 716
REMARK 465 CYS B 717
REMARK 465 PRO B 718
REMARK 465 LYS B 719
REMARK 465 CYS B 720
REMARK 465 ALA B 721
REMARK 465 PRO B 722
REMARK 465 ALA B 723
REMARK 465 GLN B 724
REMARK 465 LYS B 725
REMARK 465 ARG B 726
REMARK 465 LEU B 727
REMARK 465 ALA B 728
REMARK 465 LYS B 729
REMARK 465 VAL B 730
REMARK 465 PRO B 731
REMARK 465 ALA B 732
REMARK 465 VAL B 896
REMARK 465 PRO B 897
REMARK 465 SER B 898
REMARK 465 CYS B 899
REMARK 465 VAL B 900
REMARK 465 ALA B 901
REMARK 465 SER B 902
REMARK 465 LEU B 903
REMARK 465 ASP B 904
REMARK 465 ASP B 905
REMARK 465 VAL B 906
REMARK 465 ALA B 907
REMARK 465 GLU B 908
REMARK 465 THR B 909
REMARK 465 ASP B 910
REMARK 465 ARG B 911
REMARK 465 LYS B 912
REMARK 465 GLU B 913
REMARK 465 TYR B 914
REMARK 465 VAL B 915
REMARK 465 THR B 916
REMARK 465 VAL B 917
REMARK 465 LYS B 918
REMARK 465 ILE B 919
REMARK 465 ARG B 920
REMARK 465 LYS B 921
REMARK 465 HIS B 922
REMARK 465 HIS B 923
REMARK 465 HIS B 924
REMARK 465 HIS B 925
REMARK 465 HIS B 926
REMARK 465 HIS B 927
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 ASP B 743 CB - CA - C ANGL. DEV. = -14.3 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 ARG A 59 -5.52 72.54
REMARK 500 TYR A 100 14.16 57.13
REMARK 500 SER B 741 -167.19 -68.46
REMARK 500 ASP B 743 -31.26 -26.29
REMARK 500 ASP B 881 31.00 -78.74
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2VX8 RELATED DB: PDB
REMARK 900 VAMP7 LONGIN DOMAIN HRB PEPTIDE COMPLEX
REMARK 900 RELATED ID: 4AFI RELATED DB: PDB
REMARK 900 COMPLEX BETWEEN VAMP7 LONGIN DOMAIN AND FRAGMENT OF DELTA-ADAPTIN
REMARK 900 FROM AP3
DBREF 4B93 A 0 187 UNP P70280 VAMP7_MOUSE 1 188
DBREF 4B93 B 659 921 UNP Q96NW4 ANR27_HUMAN 659 921
SEQADV 4B93 SER A 0 UNP P70280 EXPRESSION TAG
SEQADV 4B93 HIS B 922 UNP Q96NW4 EXPRESSION TAG
SEQADV 4B93 HIS B 923 UNP Q96NW4 EXPRESSION TAG
SEQADV 4B93 HIS B 924 UNP Q96NW4 EXPRESSION TAG
SEQADV 4B93 HIS B 925 UNP Q96NW4 EXPRESSION TAG
SEQADV 4B93 HIS B 926 UNP Q96NW4 EXPRESSION TAG
SEQADV 4B93 HIS B 927 UNP Q96NW4 EXPRESSION TAG
SEQRES 1 A 189 SER MET ALA ILE LEU PHE ALA VAL VAL ALA ARG GLY THR
SEQRES 2 A 189 THR ILE LEU ALA LYS HIS ALA TRP CYS GLY GLY ASN PHE
SEQRES 3 A 189 LEU GLU VAL THR GLU GLN ILE LEU ALA LYS ILE PRO SER
SEQRES 4 A 189 GLU ASN ASN LYS LEU THR TYR SER HIS GLY ASN TYR LEU
SEQRES 5 A 189 PHE HIS TYR ILE CYS GLN ASP ARG ILE VAL TYR LEU CYS
SEQRES 6 A 189 ILE THR ASP ASP ASP PHE GLU ARG SER ARG ALA PHE SER
SEQRES 7 A 189 PHE LEU ASN GLU VAL LYS LYS ARG PHE GLN THR THR TYR
SEQRES 8 A 189 GLY SER ARG ALA GLN THR ALA LEU PRO TYR ALA MET ASN
SEQRES 9 A 189 SER GLU PHE SER SER VAL LEU ALA ALA GLN LEU LYS HIS
SEQRES 10 A 189 HIS SER GLU ASN LYS SER LEU ASP LYS VAL MET GLU THR
SEQRES 11 A 189 GLN ALA GLN VAL ASP GLU LEU LYS GLY ILE MET VAL ARG
SEQRES 12 A 189 ASN ILE ASP LEU VAL ALA GLN ARG GLY GLU ARG LEU GLU
SEQRES 13 A 189 LEU LEU ILE ASP LYS THR GLU ASN LEU VAL ASP SER SER
SEQRES 14 A 189 VAL THR PHE LYS THR THR SER ARG ASN LEU ALA ARG ALA
SEQRES 15 A 189 MET CYS MET LYS ASN ILE LYS
SEQRES 1 B 269 ARG GLN GLU GLU THR LYS LYS ASP TYR ARG GLU VAL GLU
SEQRES 2 B 269 LYS LEU LEU ARG ALA VAL ALA ASP GLY ASP LEU GLU MET
SEQRES 3 B 269 VAL ARG TYR LEU LEU GLU TRP THR GLU GLU ASP LEU GLU
SEQRES 4 B 269 ASP ALA GLU ASP THR VAL SER ALA ALA ASP PRO GLU PHE
SEQRES 5 B 269 CYS HIS PRO LEU CYS GLN CYS PRO LYS CYS ALA PRO ALA
SEQRES 6 B 269 GLN LYS ARG LEU ALA LYS VAL PRO ALA SER GLY LEU GLY
SEQRES 7 B 269 VAL ASN VAL THR SER GLN ASP GLY SER SER PRO LEU HIS
SEQRES 8 B 269 VAL ALA ALA LEU HIS GLY ARG ALA ASP LEU ILE PRO LEU
SEQRES 9 B 269 LEU LEU LYS HIS GLY ALA ASN ALA GLY ALA ARG ASN ALA
SEQRES 10 B 269 ASP GLN ALA VAL PRO LEU HIS LEU ALA CYS GLN GLN GLY
SEQRES 11 B 269 HIS PHE GLN VAL VAL LYS CYS LEU LEU ASP SER ASN ALA
SEQRES 12 B 269 LYS PRO ASN LYS LYS ASP LEU SER GLY ASN THR PRO LEU
SEQRES 13 B 269 ILE TYR ALA CYS SER GLY GLY HIS HIS GLU LEU VAL ALA
SEQRES 14 B 269 LEU LEU LEU GLN HIS GLY ALA SER ILE ASN ALA SER ASN
SEQRES 15 B 269 ASN LYS GLY ASN THR ALA LEU HIS GLU ALA VAL ILE GLU
SEQRES 16 B 269 LYS HIS VAL PHE VAL VAL GLU LEU LEU LEU LEU HIS GLY
SEQRES 17 B 269 ALA SER VAL GLN VAL LEU ASN LYS ARG GLN ARG THR ALA
SEQRES 18 B 269 VAL ASP CYS ALA GLU GLN ASN SER LYS ILE MET GLU LEU
SEQRES 19 B 269 LEU GLN VAL VAL PRO SER CYS VAL ALA SER LEU ASP ASP
SEQRES 20 B 269 VAL ALA GLU THR ASP ARG LYS GLU TYR VAL THR VAL LYS
SEQRES 21 B 269 ILE ARG LYS HIS HIS HIS HIS HIS HIS
FORMUL 3 HOH *209(H2 O)
HELIX 1 1 ASN A 24 ALA A 34 1 11
HELIX 2 2 GLU A 71 GLY A 91 1 21
HELIX 3 3 SER A 92 THR A 96 5 5
HELIX 4 4 MET A 102 GLU A 119 1 18
HELIX 5 5 THR A 129 GLU A 135 1 7
HELIX 6 6 TYR B 667 ASP B 679 1 13
HELIX 7 7 ASP B 681 GLU B 690 1 10
HELIX 8 8 SER B 746 HIS B 754 1 9
HELIX 9 9 ASP B 758 HIS B 766 1 9
HELIX 10 10 VAL B 779 GLY B 788 1 10
HELIX 11 11 HIS B 789 SER B 799 1 11
HELIX 12 12 THR B 812 GLY B 820 1 9
HELIX 13 13 HIS B 822 GLU B 824 5 3
HELIX 14 14 LEU B 825 HIS B 832 1 8
HELIX 15 15 THR B 845 GLU B 853 1 9
HELIX 16 16 HIS B 855 HIS B 865 1 11
HELIX 17 17 ALA B 879 ALA B 883 5 5
HELIX 18 18 SER B 887 LEU B 893 1 7
SHEET 1 AA 6 THR A 13 ALA A 19 0
SHEET 2 AA 6 ILE A 3 ARG A 10 -1 O ALA A 6 N HIS A 18
SHEET 3 AA 6 ILE A 60 ASP A 67 -1 O VAL A 61 N ALA A 9
SHEET 4 AA 6 TYR A 50 GLN A 57 -1 O LEU A 51 N THR A 66
SHEET 5 AA 6 ASN A 41 HIS A 47 -1 O ASN A 41 N CYS A 56
SHEET 6 AA 6 VAL A 141 ARG A 142 1 O ARG A 142 N SER A 46
SHEET 1 AB 2 GLY A 22 GLY A 23 0
SHEET 2 AB 2 ILE A 158 ASP A 159 -1 N ASP A 159 O GLY A 22
CRYST1 69.570 122.660 158.600 90.00 90.00 90.00 C 2 2 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 0.014374 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008153 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006305 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
