HEADER PROTEIN TRANSPORT, CHROMOSOMAL PROTEIN 23-DEC-04 1YD8
TITLE COMPLEX OF HUMAN GGA3 GAT DOMAIN AND UBIQUITIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UBIQUIN;
COMPND 3 CHAIN: U, V;
COMPND 4 MOL_ID: 2;
COMPND 5 MOLECULE: ADP-RIBOSYLATION FACTOR BINDING PROTEIN GGA3;
COMPND 6 CHAIN: G, H;
COMPND 7 SYNONYM: GOLGI-LOCALIZED, GAMMA EAR-CONTAINING, ARF-BINDING PROTEIN
COMPND 8 3;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: CATTLE;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 TISSUE: RED BLOOD CELLS;
SOURCE 6 MOL_ID: 2;
SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 8 ORGANISM_COMMON: HUMAN;
SOURCE 9 ORGANISM_TAXID: 9606;
SOURCE 10 GENE: GGA3, KIAA0154;
SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 13 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) ROSETTA;
SOURCE 14 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 15 EXPRESSION_SYSTEM_PLASMID: PET-PARALLEL.3_HIS6_GAT
KEYWDS TRAFFICKING, POST TRANSLATIONAL MODIFICATION, MONO-UBIQUITINATION,
KEYWDS 2 PROTEIN TRANSPORT;, PROTEIN TRANSPORT, CHROMOSOMAL PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR G.PRAG,S.LEE,R.MATTERA,C.N.ARIGHI,B.M.BEACH,J.S.BONIFACINO,J.H.HURLEY
REVDAT 5 03-APR-24 1YD8 1 REMARK
REVDAT 4 14-FEB-24 1YD8 1 SEQADV
REVDAT 3 11-OCT-17 1YD8 1 REMARK
REVDAT 2 24-FEB-09 1YD8 1 VERSN
REVDAT 1 22-FEB-05 1YD8 0
JRNL AUTH G.PRAG,S.LEE,R.MATTERA,C.N.ARIGHI,B.M.BEACH,J.S.BONIFACINO,
JRNL AUTH 2 J.H.HURLEY
JRNL TITL STRUCTURAL MECHANISM FOR UBIQUITINATED-CARGO RECOGNITION BY
JRNL TITL 2 THE GOLGI-LOCALIZED, {GAMMA}-EAR-CONTAINING,
JRNL TITL 3 ADP-RIBOSYLATION-FACTOR-BINDING PROTEINS
JRNL REF PROC.NATL.ACAD.SCI.USA V. 102 2334 2005
JRNL REFN ISSN 0027-8424
JRNL PMID 15701688
JRNL DOI 10.1073/PNAS.0500118102
REMARK 2
REMARK 2 RESOLUTION. 2.80 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) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 26.85
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 217089.830
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.4
REMARK 3 NUMBER OF REFLECTIONS : 5999
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) : 0.221
REMARK 3 FREE R VALUE : 0.297
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.200
REMARK 3 FREE R VALUE TEST SET COUNT : 614
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.012
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.98
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 53.90
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 607
REMARK 3 BIN R VALUE (WORKING SET) : 0.3380
REMARK 3 BIN FREE R VALUE : 0.4780
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.20
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 69
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.057
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 : 146
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 65.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 46.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.44000
REMARK 3 B22 (A**2) : 0.93000
REMARK 3 B33 (A**2) : -1.37000
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) : 0.36
REMARK 3 ESD FROM SIGMAA (A) : 0.42
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.53
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.60
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.80
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.670
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) : NULL ; 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 : FLAT MODEL
REMARK 3 KSOL : 0.27
REMARK 3 BSOL : 47.86
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 1YD8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-DEC-04.
REMARK 100 THE DEPOSITION ID IS D_1000031398.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-JUL-04
REMARK 200 TEMPERATURE (KELVIN) : 95.0
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : R-AXIS
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 5999
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 26.850
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.4
REMARK 200 DATA REDUNDANCY : 2.700
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 81.1
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.36100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: COMO
REMARK 200 STARTING MODEL: MODIFIED GGA1 GAT DOMAIN MADE WITH MODELER
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 37.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.96
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 23.94300
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 48.64650
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 23.94300
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 48.64650
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: U, H
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 APPLY THE FOLLOWING TO CHAINS: G, V
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 ARG U 74
REMARK 465 GLY U 75
REMARK 465 GLY U 76
REMARK 465 GLY G -4
REMARK 465 ALA G -3
REMARK 465 MET G -2
REMARK 465 GLN G 300
REMARK 465 VAL G 301
REMARK 465 ARG V 74
REMARK 465 GLY V 75
REMARK 465 GLY V 76
REMARK 465 GLY H -4
REMARK 465 ALA H -3
REMARK 465 MET H -2
REMARK 465 GLN H 300
REMARK 465 VAL H 301
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 THR U 12 66.42 -111.96
REMARK 500 SER U 20 55.52 -108.24
REMARK 500 ASP U 39 28.21 -66.10
REMARK 500 GLN U 40 24.27 -160.00
REMARK 500 THR U 55 -154.58 -120.63
REMARK 500 ASN U 60 79.65 59.42
REMARK 500 GLN U 62 175.11 -50.49
REMARK 500 GLU U 64 37.02 71.04
REMARK 500 ILE G 208 -72.18 -102.13
REMARK 500 GLN G 237 -92.65 -40.51
REMARK 500 SER G 240 156.18 162.65
REMARK 500 SER G 267 -5.26 -54.40
REMARK 500 ASP G 271 51.37 27.83
REMARK 500 ASP G 273 -170.95 -58.19
REMARK 500 ASN G 274 -83.51 23.34
REMARK 500 SER G 275 -63.07 -11.29
REMARK 500 THR V 12 68.20 -112.36
REMARK 500 SER V 20 56.02 -108.40
REMARK 500 ASP V 39 27.90 -67.04
REMARK 500 GLN V 40 25.96 -159.17
REMARK 500 THR V 55 -155.33 -120.48
REMARK 500 ASN V 60 78.75 60.02
REMARK 500 GLN V 62 173.87 -52.29
REMARK 500 GLU V 64 37.02 70.95
REMARK 500 ILE H 208 -71.58 -102.46
REMARK 500 GLN H 237 -92.10 -41.37
REMARK 500 SER H 240 156.64 162.27
REMARK 500 SER H 267 -6.38 -52.54
REMARK 500 ASP H 271 51.32 27.40
REMARK 500 ASP H 273 -170.65 -58.09
REMARK 500 ASN H 274 -83.53 23.03
REMARK 500 SER H 275 -63.84 -11.02
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1YD8 U 1 76 UNP P62990 UBIQ_BOVIN 1 76
DBREF 1YD8 V 1 76 UNP P62990 UBIQ_BOVIN 1 76
DBREF 1YD8 G 208 301 UNP Q9NZ52 GGA3_HUMAN 208 301
DBREF 1YD8 H 208 301 UNP Q9NZ52 GGA3_HUMAN 208 301
SEQADV 1YD8 GLY G -4 UNP Q9NZ52 CLONING ARTIFACT
SEQADV 1YD8 ALA G -3 UNP Q9NZ52 CLONING ARTIFACT
SEQADV 1YD8 MET G -2 UNP Q9NZ52 CLONING ARTIFACT
SEQADV 1YD8 GLY G -1 UNP Q9NZ52 CLONING ARTIFACT
SEQADV 1YD8 GLY H -4 UNP Q9NZ52 CLONING ARTIFACT
SEQADV 1YD8 ALA H -3 UNP Q9NZ52 CLONING ARTIFACT
SEQADV 1YD8 MET H -2 UNP Q9NZ52 CLONING ARTIFACT
SEQADV 1YD8 GLY H -1 UNP Q9NZ52 CLONING ARTIFACT
SEQRES 1 U 76 MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE
SEQRES 2 U 76 THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL
SEQRES 3 U 76 LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP
SEQRES 4 U 76 GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP
SEQRES 5 U 76 GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER
SEQRES 6 U 76 THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY
SEQRES 1 G 98 GLY ALA MET GLY ILE GLN LYS VAL THR LYS ARG LEU HIS
SEQRES 2 G 98 THR LEU GLU GLU VAL ASN ASN ASN VAL ARG LEU LEU SER
SEQRES 3 G 98 GLU MET LEU LEU HIS TYR SER GLN GLU ASP SER SER ASP
SEQRES 4 G 98 GLY ASP ARG GLU LEU MET LYS GLU LEU PHE ASP GLN CYS
SEQRES 5 G 98 GLU ASN LYS ARG ARG THR LEU PHE LYS LEU ALA SER GLU
SEQRES 6 G 98 THR GLU ASP ASN ASP ASN SER LEU GLY ASP ILE LEU GLN
SEQRES 7 G 98 ALA SER ASP ASN LEU SER ARG VAL ILE ASN SER TYR LYS
SEQRES 8 G 98 THR ILE ILE GLU GLY GLN VAL
SEQRES 1 V 76 MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE
SEQRES 2 V 76 THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL
SEQRES 3 V 76 LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP
SEQRES 4 V 76 GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP
SEQRES 5 V 76 GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER
SEQRES 6 V 76 THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY
SEQRES 1 H 98 GLY ALA MET GLY ILE GLN LYS VAL THR LYS ARG LEU HIS
SEQRES 2 H 98 THR LEU GLU GLU VAL ASN ASN ASN VAL ARG LEU LEU SER
SEQRES 3 H 98 GLU MET LEU LEU HIS TYR SER GLN GLU ASP SER SER ASP
SEQRES 4 H 98 GLY ASP ARG GLU LEU MET LYS GLU LEU PHE ASP GLN CYS
SEQRES 5 H 98 GLU ASN LYS ARG ARG THR LEU PHE LYS LEU ALA SER GLU
SEQRES 6 H 98 THR GLU ASP ASN ASP ASN SER LEU GLY ASP ILE LEU GLN
SEQRES 7 H 98 ALA SER ASP ASN LEU SER ARG VAL ILE ASN SER TYR LYS
SEQRES 8 H 98 THR ILE ILE GLU GLY GLN VAL
FORMUL 5 HOH *146(H2 O)
HELIX 1 1 THR U 22 GLY U 35 1 14
HELIX 2 2 PRO U 37 ASP U 39 5 3
HELIX 3 3 VAL G 211 HIS G 234 1 24
HELIX 4 4 SER G 241 SER G 267 1 27
HELIX 5 5 ASN G 274 GLY G 299 1 26
HELIX 6 6 THR V 22 GLY V 35 1 14
HELIX 7 7 PRO V 37 ASP V 39 5 3
HELIX 8 8 VAL H 211 HIS H 234 1 24
HELIX 9 9 SER H 241 SER H 267 1 27
HELIX 10 10 ASN H 274 GLY H 299 1 26
SHEET 1 A 4 THR U 12 GLU U 16 0
SHEET 2 A 4 GLN U 2 THR U 7 -1 N VAL U 5 O ILE U 13
SHEET 3 A 4 THR U 66 LEU U 71 1 O LEU U 69 N LYS U 6
SHEET 4 A 4 GLN U 41 ILE U 44 -1 N ARG U 42 O VAL U 70
SHEET 1 B 4 THR V 12 GLU V 16 0
SHEET 2 B 4 GLN V 2 THR V 7 -1 N VAL V 5 O ILE V 13
SHEET 3 B 4 THR V 66 LEU V 71 1 O LEU V 69 N LYS V 6
SHEET 4 B 4 GLN V 41 ILE V 44 -1 N ARG V 42 O VAL V 70
CRYST1 47.886 97.293 66.459 90.00 90.03 90.00 C 1 2 1 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 0.020883 0.000000 0.000011 0.00000
SCALE2 0.000000 0.010278 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015047 0.00000
(ATOM LINES ARE NOT SHOWN.)
END