HEADER MEMBRANE PROTEIN 27-JUL-01 1JOC
TITLE EEA1 HOMODIMER OF C-TERMINAL FYVE DOMAIN BOUND TO INOSITOL 1,3-
TITLE 2 DIPHOSPHATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EARLY ENDOSOMAL AUTOANTIGEN 1;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: C-TERMINAL DOMAIN, FYVE DOMAIN;
COMPND 5 SYNONYM: EEA1;
COMPND 6 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 BL21(DE3);
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: PET15B
KEYWDS FYVE DOMAIN, INOSITOL 3-PHOSPHATE BINDING, MEMBRANE PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR J.J.DUMAS,E.MERITHEW,D.RAJAMANI,S.HAYES,D.LAWE,S.CORVERA,
AUTHOR 2 D.G.LAMBRIGHT
REVDAT 3 07-FEB-24 1JOC 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1JOC 1 VERSN
REVDAT 1 28-DEC-01 1JOC 0
JRNL AUTH J.J.DUMAS,E.MERITHEW,E.SUDHARSHAN,D.RAJAMANI,S.HAYES,D.LAWE,
JRNL AUTH 2 S.CORVERA,D.G.LAMBRIGHT
JRNL TITL MULTIVALENT ENDOSOME TARGETING BY HOMODIMERIC EEA1.
JRNL REF MOL.CELL V. 8 947 2001
JRNL REFN ISSN 1097-2765
JRNL PMID 11741531
JRNL DOI 10.1016/S1097-2765(01)00385-9
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : NULL
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.221
REMARK 3 FREE R VALUE : 0.281
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1925
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 44
REMARK 3 SOLVENT ATOMS : 56
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.100
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
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 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: RESIDUES 1287 AND 1288 WERE MISSING
REMARK 3 FROM THE ELECTRON DENSITY.
REMARK 4
REMARK 4 1JOC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-AUG-01.
REMARK 100 THE DEPOSITION ID IS D_1000014001.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-MAR-01
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X12C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.28322, 1.28356, 1.23985
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : BRANDEIS - B1
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
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) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.15
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 11% PEG 4000, 50 MM HEPES, 60 MM
REMARK 280 AMMONIUM ACETATE, 10% GLYCEROL, AND 1.5 MM INS(1,3)P2, PH 7.0,
REMARK 280 VAPOR DIFFUSION, HANGING DROP
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 18.26400
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 44.01800
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 42.54800
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 44.01800
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 18.26400
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 42.54800
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 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4960 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15820 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 ASN A 1287
REMARK 465 ASN A 1288
REMARK 465 ASN B 1287
REMARK 465 ASN B 1288
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 GLU A1307 CG CD OE1 OE2
REMARK 470 LEU A1314 CG CD1 CD2
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 OE2 GLU B 1297 CE LYS B 1301 1.97
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 A1293 NE - CZ - NH2 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG B1292 NE - CZ - NH2 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG B1293 NE - CZ - NH2 ANGL. DEV. = 3.6 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 A1347 127.33 -28.54
REMARK 500 MET A1359 0.32 -63.69
REMARK 500 SER A1366 -156.67 -164.07
REMARK 500 SER A1386 46.19 -155.66
REMARK 500 LEU A1409 0.48 -60.27
REMARK 500 GLN A1410 -0.73 73.06
REMARK 500 LEU B1345 22.59 -79.58
REMARK 500 MET B1359 0.14 -55.32
REMARK 500 SER B1386 38.75 -151.44
REMARK 500 LEU B1409 41.76 -86.66
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 300 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A1374 SG
REMARK 620 2 CYS A1377 SG 104.0
REMARK 620 3 CYS A1402 SG 114.7 120.2
REMARK 620 4 CYS A1405 SG 105.3 106.1 105.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 301 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A1358 SG
REMARK 620 2 CYS A1361 SG 109.8
REMARK 620 3 CYS A1382 SG 112.0 116.7
REMARK 620 4 CYS A1385 SG 102.2 108.9 106.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 302 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B1374 SG
REMARK 620 2 CYS B1377 SG 101.5
REMARK 620 3 CYS B1402 SG 108.1 125.9
REMARK 620 4 CYS B1405 SG 111.8 109.0 100.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 303 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B1358 SG
REMARK 620 2 CYS B1361 SG 111.4
REMARK 620 3 CYS B1382 SG 112.8 114.2
REMARK 620 4 CYS B1385 SG 109.4 102.2 106.1
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 300
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ITP A 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ITP B 102
DBREF 1JOC A 1287 1411 UNP Q15075 EEA1_HUMAN 1287 1410
DBREF 1JOC B 1287 1411 UNP Q15075 EEA1_HUMAN 1287 1410
SEQADV 1JOC ALA A 1325 UNP Q15075 INSERTION
SEQADV 1JOC ALA B 1325 UNP Q15075 INSERTION
SEQRES 1 A 125 ASN ASN GLN ASP GLU ARG ARG ALA LEU LEU GLU ARG CYS
SEQRES 2 A 125 LEU LYS GLY GLU GLY GLU ILE GLU LYS LEU GLN THR LYS
SEQRES 3 A 125 VAL LEU GLU LEU GLN ARG LYS LEU ASP ASN THR THR ALA
SEQRES 4 A 125 ALA VAL GLN GLU LEU GLY ARG GLU ASN GLN SER LEU GLN
SEQRES 5 A 125 ILE LYS HIS THR GLN ALA LEU ASN ARG LYS TRP ALA GLU
SEQRES 6 A 125 ASP ASN GLU VAL GLN ASN CYS MET ALA CYS GLY LYS GLY
SEQRES 7 A 125 PHE SER VAL THR VAL ARG ARG HIS HIS CYS ARG GLN CYS
SEQRES 8 A 125 GLY ASN ILE PHE CYS ALA GLU CYS SER ALA LYS ASN ALA
SEQRES 9 A 125 LEU THR PRO SER SER LYS LYS PRO VAL ARG VAL CYS ASP
SEQRES 10 A 125 ALA CYS PHE ASN ASP LEU GLN GLY
SEQRES 1 B 125 ASN ASN GLN ASP GLU ARG ARG ALA LEU LEU GLU ARG CYS
SEQRES 2 B 125 LEU LYS GLY GLU GLY GLU ILE GLU LYS LEU GLN THR LYS
SEQRES 3 B 125 VAL LEU GLU LEU GLN ARG LYS LEU ASP ASN THR THR ALA
SEQRES 4 B 125 ALA VAL GLN GLU LEU GLY ARG GLU ASN GLN SER LEU GLN
SEQRES 5 B 125 ILE LYS HIS THR GLN ALA LEU ASN ARG LYS TRP ALA GLU
SEQRES 6 B 125 ASP ASN GLU VAL GLN ASN CYS MET ALA CYS GLY LYS GLY
SEQRES 7 B 125 PHE SER VAL THR VAL ARG ARG HIS HIS CYS ARG GLN CYS
SEQRES 8 B 125 GLY ASN ILE PHE CYS ALA GLU CYS SER ALA LYS ASN ALA
SEQRES 9 B 125 LEU THR PRO SER SER LYS LYS PRO VAL ARG VAL CYS ASP
SEQRES 10 B 125 ALA CYS PHE ASN ASP LEU GLN GLY
HET ZN A 300 1
HET ZN A 301 1
HET ITP A 101 20
HET ZN B 302 1
HET ZN B 303 1
HET ITP B 102 20
HETNAM ZN ZINC ION
HETNAM ITP PHOSPHORIC ACID MONO-(2,3,4,6-TETRAHYDROXY-5-
HETNAM 2 ITP PHOSPHONOOXY-CYCLOHEXYL) ESTER
HETSYN ITP INOSITOL 1,3-BISPHOSPHATE
FORMUL 3 ZN 4(ZN 2+)
FORMUL 5 ITP 2(C6 H14 O12 P2)
FORMUL 9 HOH *56(H2 O)
HELIX 1 1 GLN A 1289 ARG A 1347 1 59
HELIX 2 2 GLU A 1351 VAL A 1355 5 5
HELIX 3 3 CYS A 1382 SER A 1386 5 5
HELIX 4 4 CYS A 1402 LEU A 1409 1 8
HELIX 5 6 GLU B 1351 VAL B 1355 5 5
HELIX 6 7 CYS B 1382 SER B 1386 5 5
HELIX 7 8 CYS B 1402 LEU B 1409 1 8
SHEET 1 A 2 HIS A1372 HIS A1373 0
SHEET 2 A 2 ILE A1380 PHE A1381 -1 N PHE A1381 O HIS A1372
SHEET 1 B 2 LYS A1388 ALA A1390 0
SHEET 2 B 2 VAL A1399 VAL A1401 -1 O VAL A1399 N ALA A1390
SHEET 1 C 2 HIS B1372 HIS B1373 0
SHEET 2 C 2 ILE B1380 PHE B1381 -1 N PHE B1381 O HIS B1372
SHEET 1 D 2 LYS B1388 ALA B1390 0
SHEET 2 D 2 VAL B1399 VAL B1401 -1 N VAL B1399 O ALA B1390
LINK ZN ZN A 300 SG CYS A1374 1555 1555 2.41
LINK ZN ZN A 300 SG CYS A1377 1555 1555 2.24
LINK ZN ZN A 300 SG CYS A1402 1555 1555 2.25
LINK ZN ZN A 300 SG CYS A1405 1555 1555 2.25
LINK ZN ZN A 301 SG CYS A1358 1555 1555 2.34
LINK ZN ZN A 301 SG CYS A1361 1555 1555 2.42
LINK ZN ZN A 301 SG CYS A1382 1555 1555 2.29
LINK ZN ZN A 301 SG CYS A1385 1555 1555 2.35
LINK ZN ZN B 302 SG CYS B1374 1555 1555 2.33
LINK ZN ZN B 302 SG CYS B1377 1555 1555 2.14
LINK ZN ZN B 302 SG CYS B1402 1555 1555 2.28
LINK ZN ZN B 302 SG CYS B1405 1555 1555 2.36
LINK ZN ZN B 303 SG CYS B1358 1555 1555 2.26
LINK ZN ZN B 303 SG CYS B1361 1555 1555 2.22
LINK ZN ZN B 303 SG CYS B1382 1555 1555 2.38
LINK ZN ZN B 303 SG CYS B1385 1555 1555 2.41
SITE 1 AC1 4 CYS A1374 CYS A1377 CYS A1402 CYS A1405
SITE 1 AC2 4 CYS A1358 CYS A1361 CYS A1382 CYS A1385
SITE 1 AC3 4 CYS B1374 CYS B1377 CYS B1402 CYS B1405
SITE 1 AC4 4 CYS B1358 CYS B1361 CYS B1382 CYS B1385
SITE 1 AC5 10 HOH A 427 HOH A 450 HOH A 451 HOH A 452
SITE 2 AC5 10 ASP A1352 ARG A1370 ARG A1371 HIS A1372
SITE 3 AC5 10 HIS A1373 ARG A1375
SITE 1 AC6 7 HOH B 423 ASP B1352 ARG B1370 ARG B1371
SITE 2 AC6 7 HIS B1372 HIS B1373 ARG B1375
CRYST1 36.528 85.096 88.036 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 0.027376 -0.000001 -0.000001 0.00000
SCALE2 0.000000 0.011751 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011359 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
