HEADER PROTEIN TRANSPORT 09-JUL-13 4BX9
TITLE HUMAN VPS33A IN COMPLEX WITH A FRAGMENT OF HUMAN VPS16
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 33A;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: HVPS33A, VPS33A;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 16 HOMOLOG;
COMPND 8 CHAIN: C;
COMPND 9 FRAGMENT: RESIDUES 642-736;
COMPND 10 SYNONYM: HVPS16, VPS16;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: POPT;
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: PLYSS;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: POPT3G
KEYWDS PROTEIN TRANSPORT, HOPS, MEMBRANE TRAFFICKING, SEC1/MUNC18 PROTEINS,
KEYWDS 2 TETHERING
EXPDTA X-RAY DIFFRACTION
AUTHOR S.C.GRAHAM,L.WARTOSCH,S.R.GRAY,E.J.SCOURFIELD,J.E.DEANE,J.P.LUZIO,
AUTHOR 2 D.J.OWEN
REVDAT 6 20-DEC-23 4BX9 1 REMARK
REVDAT 5 13-MAR-19 4BX9 1 JRNL REMARK
REVDAT 4 22-APR-15 4BX9 1 HETSYN
REVDAT 3 25-SEP-13 4BX9 1 JRNL
REVDAT 2 14-AUG-13 4BX9 1 JRNL
REVDAT 1 24-JUL-13 4BX9 0
JRNL AUTH S.C.GRAHAM,L.WARTOSCH,S.R.GRAY,E.J.SCOURFIELD,J.E.DEANE,
JRNL AUTH 2 J.P.LUZIO,D.J.OWEN
JRNL TITL STRUCTURAL BASIS OF VPS33A RECRUITMENT TO THE HUMAN HOPS
JRNL TITL 2 COMPLEX BY VPS16.
JRNL REF PROC. NATL. ACAD. SCI. V. 110 13345 2013
JRNL REF 2 U.S.A.
JRNL REFN ESSN 1091-6490
JRNL PMID 23901104
JRNL DOI 10.1073/PNAS.1307074110
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0029
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) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 85.84
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 65003
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) : 0.178
REMARK 3 R VALUE (WORKING SET) : 0.176
REMARK 3 FREE R VALUE : 0.210
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3465
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) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.67
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4749
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.3770
REMARK 3 BIN FREE R VALUE SET COUNT : 248
REMARK 3 BIN FREE R VALUE : 0.3920
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9973
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 25
REMARK 3 SOLVENT ATOMS : 195
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 76.14
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 70.51
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.75000
REMARK 3 B22 (A**2) : -0.75000
REMARK 3 B33 (A**2) : 1.49000
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): 0.302
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.220
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.158
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 15.437
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.963
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 10178 ; 0.017 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 9905 ; 0.005 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 13743 ; 1.756 ; 1.976
REMARK 3 BOND ANGLES OTHERS (DEGREES): 22744 ; 1.092 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1243 ; 6.239 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 480 ;34.529 ;23.958
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1841 ;16.432 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 77 ;19.910 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1549 ; 0.094 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 11434 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 2339 ; 0.005 ; 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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : 5
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 146
REMARK 3 ORIGIN FOR THE GROUP (A): 55.2990 84.7650 302.8700
REMARK 3 T TENSOR
REMARK 3 T11: 0.0329 T22: 0.4551
REMARK 3 T33: 0.1178 T12: 0.0316
REMARK 3 T13: 0.0253 T23: 0.2185
REMARK 3 L TENSOR
REMARK 3 L11: 1.6153 L22: 4.3494
REMARK 3 L33: 1.4261 L12: 0.8319
REMARK 3 L13: 0.1152 L23: -1.3083
REMARK 3 S TENSOR
REMARK 3 S11: -0.0821 S12: 0.1606 S13: -0.0001
REMARK 3 S21: 0.0190 S22: -0.0417 S23: -0.1529
REMARK 3 S31: 0.0365 S32: 0.2943 S33: 0.1237
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 147 A 600
REMARK 3 ORIGIN FOR THE GROUP (A): 32.2770 62.7260 305.8010
REMARK 3 T TENSOR
REMARK 3 T11: 0.1475 T22: 0.2334
REMARK 3 T33: 0.1607 T12: 0.0131
REMARK 3 T13: 0.0235 T23: 0.1446
REMARK 3 L TENSOR
REMARK 3 L11: 1.2554 L22: 1.1622
REMARK 3 L33: 1.5595 L12: -0.2311
REMARK 3 L13: 0.3329 L23: -0.3883
REMARK 3 S TENSOR
REMARK 3 S11: 0.0434 S12: 0.2058 S13: -0.1265
REMARK 3 S21: -0.0723 S22: 0.0538 S23: 0.0705
REMARK 3 S31: 0.3515 S32: -0.0091 S33: -0.0972
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1 B 146
REMARK 3 ORIGIN FOR THE GROUP (A): 37.3910 117.5050 290.2890
REMARK 3 T TENSOR
REMARK 3 T11: 0.3373 T22: 0.6994
REMARK 3 T33: 0.0676 T12: -0.0782
REMARK 3 T13: -0.0260 T23: 0.0714
REMARK 3 L TENSOR
REMARK 3 L11: 5.4573 L22: 2.7613
REMARK 3 L33: 3.9873 L12: 2.3899
REMARK 3 L13: 1.5231 L23: 1.3571
REMARK 3 S TENSOR
REMARK 3 S11: 0.1449 S12: -1.0032 S13: 0.2476
REMARK 3 S21: 0.4421 S22: -0.2973 S23: 0.2694
REMARK 3 S31: -0.2108 S32: 0.2345 S33: 0.1524
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 147 B 600
REMARK 3 ORIGIN FOR THE GROUP (A): 38.1690 103.3330 262.8750
REMARK 3 T TENSOR
REMARK 3 T11: 0.2103 T22: 0.5053
REMARK 3 T33: 0.0740 T12: -0.0929
REMARK 3 T13: -0.0485 T23: 0.1528
REMARK 3 L TENSOR
REMARK 3 L11: 2.2922 L22: 1.4672
REMARK 3 L33: 1.3855 L12: 0.2993
REMARK 3 L13: 0.3631 L23: -0.4272
REMARK 3 S TENSOR
REMARK 3 S11: -0.1415 S12: 0.2203 S13: -0.0933
REMARK 3 S21: -0.3643 S22: -0.0152 S23: 0.0710
REMARK 3 S31: 0.0152 S32: 0.3515 S33: 0.1567
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 640 C 736
REMARK 3 ORIGIN FOR THE GROUP (A): 6.6960 92.0180 304.7880
REMARK 3 T TENSOR
REMARK 3 T11: 0.3297 T22: 0.7863
REMARK 3 T33: 0.6416 T12: 0.0664
REMARK 3 T13: -0.0032 T23: 0.3053
REMARK 3 L TENSOR
REMARK 3 L11: 3.2542 L22: 1.5673
REMARK 3 L33: 6.8702 L12: -0.7265
REMARK 3 L13: -2.5335 L23: -0.3189
REMARK 3 S TENSOR
REMARK 3 S11: 0.0625 S12: -0.0539 S13: 0.6113
REMARK 3 S21: 0.1196 S22: 0.1245 S23: -0.0092
REMARK 3 S31: -0.5097 S32: -0.1516 S33: -0.1869
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 WITH TLS ADDED
REMARK 4
REMARK 4 4BX9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 09-JUL-13.
REMARK 100 THE DEPOSITION ID IS D_1290057619.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-MAY-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.916
REMARK 200 MONOCHROMATOR : SINGLE BOUNCE SI(111) CRYSTAL
REMARK 200 OPTICS : TOROIDAL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 68560
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 87.800
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 15.20
REMARK 200 R MERGE (I) : 0.11000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.72
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 14.00
REMARK 200 R MERGE FOR SHELL (I) : 1.31000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 4BX8
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 66.19
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.64
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALS WERE GROWN IN SITTING DROPS
REMARK 280 AT 20C. VPS33A:VPS16 COMPLEX (200 NL; A280 = 7.13, APPROX. 8.7
REMARK 280 MG/ML) WAS MIXED 1:1 WITH RESERVOIR SOLUTION AND EQUILIBRATED
REMARK 280 AGAINST 80 UL RESERVOIRS CONTAINING 4% TACSIMATE PH 6.0, 12% PEG
REMARK 280 3350 (HAMPTON RESEARCH). CRYSTALS WERE CRYOPROTECTED BY BRIEF
REMARK 280 IMMERSION IN RESERVOIR SOLUTION SUPPLEMENTED WITH 30% ETHYLENE
REMARK 280 GLYCOL AND CRYO-COOLED BY PLUNGING INTO LIQUID NITROGEN., VAPOR
REMARK 280 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 131.68000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 64.20500
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 64.20500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 197.52000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 64.20500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 64.20500
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 65.84000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 64.20500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 64.20500
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 197.52000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 64.20500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 64.20500
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 65.84000
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 131.68000
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 APPLY THE FOLLOWING TO CHAINS: A, 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 MET A 1
REMARK 465 LYS A 272
REMARK 465 GLN A 273
REMARK 465 GLY A 274
REMARK 465 ASP A 275
REMARK 465 GLY A 276
REMARK 465 GLY A 277
REMARK 465 LYS A 278
REMARK 465 ASP A 279
REMARK 465 LEU A 280
REMARK 465 PRO A 281
REMARK 465 GLY A 532
REMARK 465 LEU A 533
REMARK 465 GLN A 534
REMARK 465 LYS A 535
REMARK 465 LYS A 536
REMARK 465 ARG A 537
REMARK 465 GLN A 538
REMARK 465 PRO A 539
REMARK 465 GLY A 540
REMARK 465 GLU A 541
REMARK 465 PHE A 596
REMARK 465 HIS A 597
REMARK 465 HIS A 598
REMARK 465 HIS A 599
REMARK 465 HIS A 600
REMARK 465 HIS A 601
REMARK 465 HIS A 602
REMARK 465 HIS A 603
REMARK 465 HIS A 604
REMARK 465 HIS A 605
REMARK 465 HIS A 606
REMARK 465 MET B 1
REMARK 465 PRO B 270
REMARK 465 LYS B 271
REMARK 465 LYS B 272
REMARK 465 GLN B 273
REMARK 465 GLY B 274
REMARK 465 ASP B 275
REMARK 465 GLY B 276
REMARK 465 GLY B 277
REMARK 465 LYS B 278
REMARK 465 ASP B 279
REMARK 465 LEU B 280
REMARK 465 PRO B 281
REMARK 465 PRO B 539
REMARK 465 GLY B 540
REMARK 465 GLU B 541
REMARK 465 HIS B 598
REMARK 465 HIS B 599
REMARK 465 HIS B 600
REMARK 465 HIS B 601
REMARK 465 HIS B 602
REMARK 465 HIS B 603
REMARK 465 HIS B 604
REMARK 465 HIS B 605
REMARK 465 HIS B 606
REMARK 465 GLY C 638
REMARK 465 PRO C 639
REMARK 465 HIS C 640
REMARK 465 MET C 641
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 LYS A 271 CG CD CE NZ
REMARK 470 LYS A 329 CG CD CE NZ
REMARK 470 LYS A 335 CG CD CE NZ
REMARK 470 ARG A 460 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 594 CG CD CE NZ
REMARK 470 LYS B 329 CG CD CE NZ
REMARK 470 ARG B 460 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 594 CG CD CE NZ
REMARK 470 HIS B 597 CG ND1 CD2 CE1 NE2
REMARK 470 GLU C 642 CG CD OE1 OE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OH TYR B 41 OE1 GLU B 157 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 439 CG GLU A 439 CD 0.094
REMARK 500 GLU A 439 CD GLU A 439 OE1 0.067
REMARK 500 SER B 319 CB SER B 319 OG -0.082
REMARK 500
REMARK 500 REMARK: NULL
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 A 124 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG A 348 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG A 471 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG B 348 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ASP C 656 CB - CG - OD1 ANGL. DEV. = 9.1 DEGREES
REMARK 500 ASP C 656 CB - CG - OD2 ANGL. DEV. = -7.8 DEGREES
REMARK 500 ASP C 718 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ARG C 725 NE - CZ - NH1 ANGL. DEV. = 3.5 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 69 -148.86 62.72
REMARK 500 ASP A 143 -70.58 -106.46
REMARK 500 THR A 214 21.30 -140.55
REMARK 500 GLU A 568 55.64 -96.00
REMARK 500 ASN B 69 -148.21 63.82
REMARK 500 PRO B 85 84.68 -68.13
REMARK 500 ASP B 143 -73.14 -93.76
REMARK 500 GLU B 568 56.20 -95.63
REMARK 500 ASP C 693 -7.05 89.28
REMARK 500 HIS C 708 66.12 -103.43
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 LYS B 535 LYS B 536 140.94
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 1598
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MLA C 1737
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 1599
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 1596
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMR A 1597
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4BX8 RELATED DB: PDB
REMARK 900 HUMAN VPS33A
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 ADDITIONAL C-TERMINAL RESIDUES ARE DERIVED FROM THE
REMARK 999 EXPRESSION VECTOR.
REMARK 999 ADDITIONAL N-TERMINAL RESIDUES ARE RESIDUAL FROM CLEAVAGE
REMARK 999 OF GST PURIFICATION TAG
DBREF 4BX9 A 1 596 UNP Q96AX1 VP33A_HUMAN 1 596
DBREF 4BX9 B 1 596 UNP Q96AX1 VP33A_HUMAN 1 596
DBREF 4BX9 C 642 736 UNP Q9H269 VPS16_HUMAN 642 736
SEQADV 4BX9 HIS A 597 UNP Q96AX1 EXPRESSION TAG
SEQADV 4BX9 HIS A 598 UNP Q96AX1 EXPRESSION TAG
SEQADV 4BX9 HIS A 599 UNP Q96AX1 EXPRESSION TAG
SEQADV 4BX9 HIS A 600 UNP Q96AX1 EXPRESSION TAG
SEQADV 4BX9 HIS A 601 UNP Q96AX1 EXPRESSION TAG
SEQADV 4BX9 HIS A 602 UNP Q96AX1 EXPRESSION TAG
SEQADV 4BX9 HIS A 603 UNP Q96AX1 EXPRESSION TAG
SEQADV 4BX9 HIS A 604 UNP Q96AX1 EXPRESSION TAG
SEQADV 4BX9 HIS A 605 UNP Q96AX1 EXPRESSION TAG
SEQADV 4BX9 HIS A 606 UNP Q96AX1 EXPRESSION TAG
SEQADV 4BX9 HIS B 597 UNP Q96AX1 EXPRESSION TAG
SEQADV 4BX9 HIS B 598 UNP Q96AX1 EXPRESSION TAG
SEQADV 4BX9 HIS B 599 UNP Q96AX1 EXPRESSION TAG
SEQADV 4BX9 HIS B 600 UNP Q96AX1 EXPRESSION TAG
SEQADV 4BX9 HIS B 601 UNP Q96AX1 EXPRESSION TAG
SEQADV 4BX9 HIS B 602 UNP Q96AX1 EXPRESSION TAG
SEQADV 4BX9 HIS B 603 UNP Q96AX1 EXPRESSION TAG
SEQADV 4BX9 HIS B 604 UNP Q96AX1 EXPRESSION TAG
SEQADV 4BX9 HIS B 605 UNP Q96AX1 EXPRESSION TAG
SEQADV 4BX9 HIS B 606 UNP Q96AX1 EXPRESSION TAG
SEQADV 4BX9 GLY C 638 UNP Q9H269 EXPRESSION TAG
SEQADV 4BX9 PRO C 639 UNP Q9H269 EXPRESSION TAG
SEQADV 4BX9 HIS C 640 UNP Q9H269 EXPRESSION TAG
SEQADV 4BX9 MET C 641 UNP Q9H269 EXPRESSION TAG
SEQRES 1 A 606 MET ALA ALA HIS LEU SER TYR GLY ARG VAL ASN LEU ASN
SEQRES 2 A 606 VAL LEU ARG GLU ALA VAL ARG ARG GLU LEU ARG GLU PHE
SEQRES 3 A 606 LEU ASP LYS CYS ALA GLY SER LYS ALA ILE VAL TRP ASP
SEQRES 4 A 606 GLU TYR LEU THR GLY PRO PHE GLY LEU ILE ALA GLN TYR
SEQRES 5 A 606 SER LEU LEU LYS GLU HIS GLU VAL GLU LYS MET PHE THR
SEQRES 6 A 606 LEU LYS GLY ASN ARG LEU PRO ALA ALA ASP VAL LYS ASN
SEQRES 7 A 606 ILE ILE PHE PHE VAL ARG PRO ARG LEU GLU LEU MET ASP
SEQRES 8 A 606 ILE ILE ALA GLU ASN VAL LEU SER GLU ASP ARG ARG GLY
SEQRES 9 A 606 PRO THR ARG ASP PHE HIS ILE LEU PHE VAL PRO ARG ARG
SEQRES 10 A 606 SER LEU LEU CYS GLU GLN ARG LEU LYS ASP LEU GLY VAL
SEQRES 11 A 606 LEU GLY SER PHE ILE HIS ARG GLU GLU TYR SER LEU ASP
SEQRES 12 A 606 LEU ILE PRO PHE ASP GLY ASP LEU LEU SER MET GLU SER
SEQRES 13 A 606 GLU GLY ALA PHE LYS GLU CYS TYR LEU GLU GLY ASP GLN
SEQRES 14 A 606 THR SER LEU TYR HIS ALA ALA LYS GLY LEU MET THR LEU
SEQRES 15 A 606 GLN ALA LEU TYR GLY THR ILE PRO GLN ILE PHE GLY LYS
SEQRES 16 A 606 GLY GLU CYS ALA ARG GLN VAL ALA ASN MET MET ILE ARG
SEQRES 17 A 606 MET LYS ARG GLU PHE THR GLY SER GLN ASN SER ILE PHE
SEQRES 18 A 606 PRO VAL PHE ASP ASN LEU LEU LEU LEU ASP ARG ASN VAL
SEQRES 19 A 606 ASP LEU LEU THR PRO LEU ALA THR GLN LEU THR TYR GLU
SEQRES 20 A 606 GLY LEU ILE ASP GLU ILE TYR GLY ILE GLN ASN SER TYR
SEQRES 21 A 606 VAL LYS LEU PRO PRO GLU LYS PHE ALA PRO LYS LYS GLN
SEQRES 22 A 606 GLY ASP GLY GLY LYS ASP LEU PRO THR GLU ALA LYS LYS
SEQRES 23 A 606 LEU GLN LEU ASN SER ALA GLU GLU LEU TYR ALA GLU ILE
SEQRES 24 A 606 ARG ASP LYS ASN PHE ASN ALA VAL GLY SER VAL LEU SER
SEQRES 25 A 606 LYS LYS ALA LYS ILE ILE SER ALA ALA PHE GLU GLU ARG
SEQRES 26 A 606 HIS ASN ALA LYS THR VAL GLY GLU ILE LYS GLN PHE VAL
SEQRES 27 A 606 SER GLN LEU PRO HIS MET GLN ALA ALA ARG GLY SER LEU
SEQRES 28 A 606 ALA ASN HIS THR SER ILE ALA GLU LEU ILE LYS ASP VAL
SEQRES 29 A 606 THR THR SER GLU ASP PHE PHE ASP LYS LEU THR VAL GLU
SEQRES 30 A 606 GLN GLU PHE MET SER GLY ILE ASP THR ASP LYS VAL ASN
SEQRES 31 A 606 ASN TYR ILE GLU ASP CYS ILE ALA GLN LYS HIS SER LEU
SEQRES 32 A 606 ILE LYS VAL LEU ARG LEU VAL CYS LEU GLN SER VAL CYS
SEQRES 33 A 606 ASN SER GLY LEU LYS GLN LYS VAL LEU ASP TYR TYR LYS
SEQRES 34 A 606 ARG GLU ILE LEU GLN THR TYR GLY TYR GLU HIS ILE LEU
SEQRES 35 A 606 THR LEU HIS ASN LEU GLU LYS ALA GLY LEU LEU LYS PRO
SEQRES 36 A 606 GLN THR GLY GLY ARG ASN ASN TYR PRO THR ILE ARG LYS
SEQRES 37 A 606 THR LEU ARG LEU TRP MET ASP ASP VAL ASN GLU GLN ASN
SEQRES 38 A 606 PRO THR ASP ILE SER TYR VAL TYR SER GLY TYR ALA PRO
SEQRES 39 A 606 LEU SER VAL ARG LEU ALA GLN LEU LEU SER ARG PRO GLY
SEQRES 40 A 606 TRP ARG SER ILE GLU GLU VAL LEU ARG ILE LEU PRO GLY
SEQRES 41 A 606 PRO HIS PHE GLU GLU ARG GLN PRO LEU PRO THR GLY LEU
SEQRES 42 A 606 GLN LYS LYS ARG GLN PRO GLY GLU ASN ARG VAL THR LEU
SEQRES 43 A 606 ILE PHE PHE LEU GLY GLY VAL THR PHE ALA GLU ILE ALA
SEQRES 44 A 606 ALA LEU ARG PHE LEU SER GLN LEU GLU ASP GLY GLY THR
SEQRES 45 A 606 GLU TYR VAL ILE ALA THR THR LYS LEU MET ASN GLY THR
SEQRES 46 A 606 SER TRP ILE GLU ALA LEU MET GLU LYS PRO PHE HIS HIS
SEQRES 47 A 606 HIS HIS HIS HIS HIS HIS HIS HIS
SEQRES 1 B 606 MET ALA ALA HIS LEU SER TYR GLY ARG VAL ASN LEU ASN
SEQRES 2 B 606 VAL LEU ARG GLU ALA VAL ARG ARG GLU LEU ARG GLU PHE
SEQRES 3 B 606 LEU ASP LYS CYS ALA GLY SER LYS ALA ILE VAL TRP ASP
SEQRES 4 B 606 GLU TYR LEU THR GLY PRO PHE GLY LEU ILE ALA GLN TYR
SEQRES 5 B 606 SER LEU LEU LYS GLU HIS GLU VAL GLU LYS MET PHE THR
SEQRES 6 B 606 LEU LYS GLY ASN ARG LEU PRO ALA ALA ASP VAL LYS ASN
SEQRES 7 B 606 ILE ILE PHE PHE VAL ARG PRO ARG LEU GLU LEU MET ASP
SEQRES 8 B 606 ILE ILE ALA GLU ASN VAL LEU SER GLU ASP ARG ARG GLY
SEQRES 9 B 606 PRO THR ARG ASP PHE HIS ILE LEU PHE VAL PRO ARG ARG
SEQRES 10 B 606 SER LEU LEU CYS GLU GLN ARG LEU LYS ASP LEU GLY VAL
SEQRES 11 B 606 LEU GLY SER PHE ILE HIS ARG GLU GLU TYR SER LEU ASP
SEQRES 12 B 606 LEU ILE PRO PHE ASP GLY ASP LEU LEU SER MET GLU SER
SEQRES 13 B 606 GLU GLY ALA PHE LYS GLU CYS TYR LEU GLU GLY ASP GLN
SEQRES 14 B 606 THR SER LEU TYR HIS ALA ALA LYS GLY LEU MET THR LEU
SEQRES 15 B 606 GLN ALA LEU TYR GLY THR ILE PRO GLN ILE PHE GLY LYS
SEQRES 16 B 606 GLY GLU CYS ALA ARG GLN VAL ALA ASN MET MET ILE ARG
SEQRES 17 B 606 MET LYS ARG GLU PHE THR GLY SER GLN ASN SER ILE PHE
SEQRES 18 B 606 PRO VAL PHE ASP ASN LEU LEU LEU LEU ASP ARG ASN VAL
SEQRES 19 B 606 ASP LEU LEU THR PRO LEU ALA THR GLN LEU THR TYR GLU
SEQRES 20 B 606 GLY LEU ILE ASP GLU ILE TYR GLY ILE GLN ASN SER TYR
SEQRES 21 B 606 VAL LYS LEU PRO PRO GLU LYS PHE ALA PRO LYS LYS GLN
SEQRES 22 B 606 GLY ASP GLY GLY LYS ASP LEU PRO THR GLU ALA LYS LYS
SEQRES 23 B 606 LEU GLN LEU ASN SER ALA GLU GLU LEU TYR ALA GLU ILE
SEQRES 24 B 606 ARG ASP LYS ASN PHE ASN ALA VAL GLY SER VAL LEU SER
SEQRES 25 B 606 LYS LYS ALA LYS ILE ILE SER ALA ALA PHE GLU GLU ARG
SEQRES 26 B 606 HIS ASN ALA LYS THR VAL GLY GLU ILE LYS GLN PHE VAL
SEQRES 27 B 606 SER GLN LEU PRO HIS MET GLN ALA ALA ARG GLY SER LEU
SEQRES 28 B 606 ALA ASN HIS THR SER ILE ALA GLU LEU ILE LYS ASP VAL
SEQRES 29 B 606 THR THR SER GLU ASP PHE PHE ASP LYS LEU THR VAL GLU
SEQRES 30 B 606 GLN GLU PHE MET SER GLY ILE ASP THR ASP LYS VAL ASN
SEQRES 31 B 606 ASN TYR ILE GLU ASP CYS ILE ALA GLN LYS HIS SER LEU
SEQRES 32 B 606 ILE LYS VAL LEU ARG LEU VAL CYS LEU GLN SER VAL CYS
SEQRES 33 B 606 ASN SER GLY LEU LYS GLN LYS VAL LEU ASP TYR TYR LYS
SEQRES 34 B 606 ARG GLU ILE LEU GLN THR TYR GLY TYR GLU HIS ILE LEU
SEQRES 35 B 606 THR LEU HIS ASN LEU GLU LYS ALA GLY LEU LEU LYS PRO
SEQRES 36 B 606 GLN THR GLY GLY ARG ASN ASN TYR PRO THR ILE ARG LYS
SEQRES 37 B 606 THR LEU ARG LEU TRP MET ASP ASP VAL ASN GLU GLN ASN
SEQRES 38 B 606 PRO THR ASP ILE SER TYR VAL TYR SER GLY TYR ALA PRO
SEQRES 39 B 606 LEU SER VAL ARG LEU ALA GLN LEU LEU SER ARG PRO GLY
SEQRES 40 B 606 TRP ARG SER ILE GLU GLU VAL LEU ARG ILE LEU PRO GLY
SEQRES 41 B 606 PRO HIS PHE GLU GLU ARG GLN PRO LEU PRO THR GLY LEU
SEQRES 42 B 606 GLN LYS LYS ARG GLN PRO GLY GLU ASN ARG VAL THR LEU
SEQRES 43 B 606 ILE PHE PHE LEU GLY GLY VAL THR PHE ALA GLU ILE ALA
SEQRES 44 B 606 ALA LEU ARG PHE LEU SER GLN LEU GLU ASP GLY GLY THR
SEQRES 45 B 606 GLU TYR VAL ILE ALA THR THR LYS LEU MET ASN GLY THR
SEQRES 46 B 606 SER TRP ILE GLU ALA LEU MET GLU LYS PRO PHE HIS HIS
SEQRES 47 B 606 HIS HIS HIS HIS HIS HIS HIS HIS
SEQRES 1 C 99 GLY PRO HIS MET GLU ARG ILE GLU GLY ARG VAL ALA ALA
SEQRES 2 C 99 LEU GLN THR ALA ALA ASP ALA PHE TYR LYS ALA LYS ASN
SEQRES 3 C 99 GLU PHE ALA ALA LYS ALA THR GLU ASP GLN MET ARG LEU
SEQRES 4 C 99 LEU ARG LEU GLN ARG ARG LEU GLU ASP GLU LEU GLY GLY
SEQRES 5 C 99 GLN PHE LEU ASP LEU SER LEU HIS ASP THR VAL THR THR
SEQRES 6 C 99 LEU ILE LEU GLY GLY HIS ASN LYS ARG ALA GLU GLN LEU
SEQRES 7 C 99 ALA ARG ASP PHE ARG ILE PRO ASP LYS ARG LEU TRP TRP
SEQRES 8 C 99 LEU LYS LEU THR ALA LEU ALA ASP
HET FMT A1596 3
HET LMR A1597 9
HET FMT B1598 3
HET FMT B1599 3
HET MLA C1737 7
HETNAM FMT FORMIC ACID
HETNAM LMR (2S)-2-HYDROXYBUTANEDIOIC ACID
HETNAM MLA MALONIC ACID
HETSYN LMR L-MALATE
HETSYN MLA DICARBOXYLIC ACID C3; PROPANEDIOLIC ACID;
HETSYN 2 MLA METHANEDICARBOXYLIC ACID
FORMUL 4 FMT 3(C H2 O2)
FORMUL 5 LMR C4 H6 O5
FORMUL 8 MLA C3 H4 O4
FORMUL 9 HOH *195(H2 O)
HELIX 1 1 ALA A 2 TYR A 7 5 6
HELIX 2 2 LEU A 12 CYS A 30 1 19
HELIX 3 3 LEU A 42 GLY A 47 1 6
HELIX 4 4 GLN A 51 GLU A 57 1 7
HELIX 5 5 ARG A 86 SER A 99 1 14
HELIX 6 6 SER A 118 LEU A 128 1 11
HELIX 7 7 VAL A 130 GLY A 132 5 3
HELIX 8 8 GLY A 158 GLY A 167 1 10
HELIX 9 9 GLN A 169 GLY A 187 1 19
HELIX 10 10 GLY A 196 GLU A 212 1 17
HELIX 11 11 ASN A 233 ASP A 235 5 3
HELIX 12 12 LEU A 237 ALA A 241 5 5
HELIX 13 13 THR A 245 TYR A 254 1 10
HELIX 14 14 GLU A 293 ARG A 300 1 8
HELIX 15 15 ALA A 306 GLU A 324 1 19
HELIX 16 16 VAL A 331 THR A 366 1 36
HELIX 17 17 SER A 367 SER A 382 1 16
HELIX 18 18 ASN A 390 GLN A 399 1 10
HELIX 19 19 SER A 402 SER A 418 1 17
HELIX 20 20 LYS A 421 GLY A 437 1 17
HELIX 21 21 HIS A 440 ALA A 450 1 11
HELIX 22 22 ASN A 462 ARG A 471 1 10
HELIX 23 23 ASP A 484 SER A 490 5 7
HELIX 24 24 PRO A 494 ARG A 505 1 12
HELIX 25 25 GLY A 507 SER A 510 5 4
HELIX 26 26 ILE A 511 ARG A 516 1 6
HELIX 27 27 THR A 554 LEU A 567 1 14
HELIX 28 28 ASN A 583 MET A 592 1 10
HELIX 29 29 ALA B 2 TYR B 7 5 6
HELIX 30 30 ASN B 11 CYS B 30 1 20
HELIX 31 31 ASP B 39 GLY B 47 1 9
HELIX 32 32 GLN B 51 GLU B 57 1 7
HELIX 33 33 ARG B 86 SER B 99 1 14
HELIX 34 34 SER B 118 LEU B 128 1 11
HELIX 35 35 GLY B 129 GLY B 132 5 4
HELIX 36 36 GLY B 158 LEU B 165 1 8
HELIX 37 37 GLN B 169 GLY B 187 1 19
HELIX 38 38 GLY B 196 PHE B 213 1 18
HELIX 39 39 ASN B 233 ASP B 235 5 3
HELIX 40 40 THR B 245 TYR B 254 1 10
HELIX 41 41 GLU B 293 ARG B 300 1 8
HELIX 42 42 ALA B 306 HIS B 326 1 21
HELIX 43 43 VAL B 331 GLN B 340 1 10
HELIX 44 44 GLN B 340 THR B 366 1 27
HELIX 45 45 SER B 367 SER B 382 1 16
HELIX 46 46 ASN B 390 GLN B 399 1 10
HELIX 47 47 SER B 402 SER B 418 1 17
HELIX 48 48 LYS B 421 GLY B 437 1 17
HELIX 49 49 HIS B 440 ALA B 450 1 11
HELIX 50 50 ASN B 462 ARG B 471 1 10
HELIX 51 51 ASP B 484 SER B 490 5 7
HELIX 52 52 PRO B 494 ARG B 505 1 12
HELIX 53 53 GLY B 507 SER B 510 5 4
HELIX 54 54 ILE B 511 ARG B 516 1 6
HELIX 55 55 PRO B 530 GLN B 534 5 5
HELIX 56 56 THR B 554 LEU B 567 1 14
HELIX 57 57 ASN B 583 MET B 592 1 10
HELIX 58 58 ILE C 644 ALA C 661 1 18
HELIX 59 59 ASN C 663 GLY C 688 1 26
HELIX 60 60 SER C 695 GLY C 706 1 12
HELIX 61 61 HIS C 708 PHE C 719 1 12
HELIX 62 62 PRO C 722 ALA C 735 1 14
SHEET 1 AA 5 VAL A 60 THR A 65 0
SHEET 2 AA 5 LYS A 34 TRP A 38 1 O LYS A 34 N GLU A 61
SHEET 3 AA 5 ASN A 78 VAL A 83 1 O ASN A 78 N ALA A 35
SHEET 4 AA 5 ASP A 108 PHE A 113 1 O ASP A 108 N ILE A 79
SHEET 5 AA 5 PHE A 134 GLU A 139 1 N ILE A 135 O PHE A 109
SHEET 1 AB 7 ILE A 145 ASP A 148 0
SHEET 2 AB 7 LEU A 151 SER A 153 -1 O LEU A 151 N PHE A 147
SHEET 3 AB 7 THR A 572 THR A 578 1 O ILE A 576 N LEU A 152
SHEET 4 AB 7 ARG A 543 LEU A 550 1 O ARG A 543 N GLU A 573
SHEET 5 AB 7 ASN A 226 ASP A 231 1 O ASN A 226 N LEU A 546
SHEET 6 AB 7 GLN A 191 LYS A 195 1 O GLN A 191 N LEU A 227
SHEET 7 AB 7 HIS A 522 ARG A 526 -1 O PHE A 523 N GLY A 194
SHEET 1 AC 3 ILE A 256 GLN A 257 0
SHEET 2 AC 3 TYR A 260 LEU A 263 -1 O TYR A 260 N GLN A 257
SHEET 3 AC 3 LYS A 285 GLN A 288 -1 O LYS A 285 N LEU A 263
SHEET 1 BA 5 VAL B 60 THR B 65 0
SHEET 2 BA 5 LYS B 34 TRP B 38 1 O LYS B 34 N GLU B 61
SHEET 3 BA 5 ASN B 78 VAL B 83 1 O ASN B 78 N ALA B 35
SHEET 4 BA 5 ASP B 108 PHE B 113 1 O ASP B 108 N ILE B 79
SHEET 5 BA 5 PHE B 134 GLU B 139 1 N ILE B 135 O PHE B 109
SHEET 1 BB 7 ILE B 145 ASP B 148 0
SHEET 2 BB 7 LEU B 151 SER B 153 -1 O LEU B 151 N PHE B 147
SHEET 3 BB 7 THR B 572 THR B 578 1 O ILE B 576 N LEU B 152
SHEET 4 BB 7 ARG B 543 LEU B 550 1 O ARG B 543 N GLU B 573
SHEET 5 BB 7 ASN B 226 ASP B 231 1 O ASN B 226 N LEU B 546
SHEET 6 BB 7 GLN B 191 LYS B 195 1 O GLN B 191 N LEU B 227
SHEET 7 BB 7 HIS B 522 ARG B 526 -1 O PHE B 523 N GLY B 194
SHEET 1 BC 3 ILE B 256 GLN B 257 0
SHEET 2 BC 3 TYR B 260 LEU B 263 -1 O TYR B 260 N GLN B 257
SHEET 3 BC 3 LYS B 285 GLN B 288 -1 O LYS B 285 N LEU B 263
CISPEP 1 VAL A 114 PRO A 115 0 15.83
CISPEP 2 ALA A 269 PRO A 270 0 -16.40
CISPEP 3 ARG A 505 PRO A 506 0 9.02
CISPEP 4 VAL B 114 PRO B 115 0 8.20
CISPEP 5 ARG B 505 PRO B 506 0 5.92
SITE 1 AC1 4 GLU B 252 PHE B 370 LYS B 373 HOH B2046
SITE 1 AC2 4 HIS C 708 ASN C 709 LYS C 710 ARG C 711
SITE 1 AC3 3 SER B 141 ASP B 143 LEU B 144
SITE 1 AC4 2 ASP A 143 LEU A 144
SITE 1 AC5 5 ARG A 116 SER A 118 LEU A 119 LEU A 120
SITE 2 AC5 5 ARG B 208
CRYST1 128.410 128.410 263.360 90.00 90.00 90.00 P 43 21 2 16
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 0.007788 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007788 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003797 0.00000
(ATOM LINES ARE NOT SHOWN.)
END