HEADER ENDOCYTOSIS 12-DEC-00 1HG2
TITLE CALM-N N-TERMINAL DOMAIN OF CLATHRIN ASSEMBLY LYMPHOID MYELOID
TITLE 2 LEUKAEMIA PROTEIN, INOSITOL(4,5)P2 COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CLATHRIN ASSEMBLY PROTEIN SHORT FORM;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-TERMINAL DOMAIN RESIDUES 1-289;
COMPND 5 SYNONYM: CALM-N, AP180-2;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: NORWAY RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGEX4T2;
SOURCE 10 EXPRESSION_SYSTEM_GENE: CALM-N
KEYWDS ENDOCYTOSIS, ADAPTOR
EXPDTA X-RAY DIFFRACTION
AUTHOR M.G.J.FORD,P.R.EVANS,H.T.MCMAHON
REVDAT 3 09-OCT-19 1HG2 1 REMARK
REVDAT 2 24-FEB-09 1HG2 1 VERSN
REVDAT 1 12-FEB-01 1HG2 0
JRNL AUTH M.G.J.FORD,B.M.F.PEARSE,M.K.HIGGINS,Y.VALLIS,D.J.OWEN,
JRNL AUTH 2 A.GIBSON,C.R.HOPKINS,P.R.EVANS,H.T.MCMAHON
JRNL TITL SIMULTANEOUS BINDING OF PTDINS(4,5)P2 AND CLATHRIN BY AP180
JRNL TITL 2 IN THE NUCLEATION OF CLATHRIN LATTICES ON MEMBRANES
JRNL REF SCIENCE V. 291 1051 2001
JRNL REFN ISSN 0036-8075
JRNL PMID 11161218
JRNL DOI 10.1126/SCIENCE.291.5506.1051
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 65.94
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 3 NUMBER OF REFLECTIONS : 24532
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) : 0.198
REMARK 3 R VALUE (WORKING SET) : 0.197
REMARK 3 FREE R VALUE : 0.217
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1315
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2114
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 20
REMARK 3 SOLVENT ATOMS : 128
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 43.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.94
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.59000
REMARK 3 B22 (A**2) : 1.59000
REMARK 3 B33 (A**2) : -3.18000
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): 0.154
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.135
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.188
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.970
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.033 ; 0.022
REMARK 3 ANGLE DISTANCE (A) : 2.460 ; 1.950
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : 0.011 ; 0.020
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : 0.160 ; 0.200
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.600 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.900 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 4.200 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 6.600 ; 4.500
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS SCALING DETAILS BABINET"S PRINCIPLE FOR SCALING HAS
REMARK 3 BEEN USED BULK SOLVENT CORRECTION BASED ON CONSTANT VALUE HAS
REMARK 3 BEEN U PARAMETERS FOR MASK CALCULATION VDW PROB RADII = 1.40 ION
REMARK 3 PROB RADII = 0.80 SHRINKAGE RADII = 0.80
REMARK 4
REMARK 4 1HG2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-DEC-00.
REMARK 100 THE DEPOSITION ID IS D_1290005668.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-APR-00
REMARK 200 TEMPERATURE (KELVIN) : 293.0
REMARK 200 PH : 7.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SRS
REMARK 200 BEAMLINE : PX9.6
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.87
REMARK 200 MONOCHROMATOR : SI
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25871
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 37.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 6.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 7.200
REMARK 200 R MERGE (I) : 0.12600
REMARK 200 R SYM (I) : 0.12600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.1000
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) : 2.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 7.00
REMARK 200 R MERGE FOR SHELL (I) : 1.95800
REMARK 200 R SYM FOR SHELL (I) : 1.95800
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: 1HF8
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES, PH 7.5, 12% PEG 8K, 8%
REMARK 280 ETHYLENE GLYCOL CRYSTALS SOAKED IN 1MM LIGAND FOR 1 HOUR, PH
REMARK 280 7.50, VAPOR DIFFUSION, HANGING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 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+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
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 61.16650
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 38.92950
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 38.92950
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 30.58325
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 38.92950
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 38.92950
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 91.74975
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 38.92950
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 38.92950
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 30.58325
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 38.92950
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 38.92950
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 91.74975
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 61.16650
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: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 BIOMT1 2 0.000000 -1.000000 0.000000 77.85900
REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 77.85900
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 61.16650
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 SER A 2
REMARK 465 GLY A 3
REMARK 465 GLN A 4
REMARK 465 SER A 5
REMARK 465 LEU A 6
REMARK 465 THR A 7
REMARK 465 ASP A 8
REMARK 465 ARG A 9
REMARK 465 ILE A 10
REMARK 465 THR A 11
REMARK 465 ALA A 12
REMARK 465 ALA A 13
REMARK 465 GLN A 14
REMARK 465 HIS A 15
REMARK 465 SER A 16
REMARK 465 VAL A 17
REMARK 465 THR A 18
REMARK 465 LEU A 282
REMARK 465 ALA A 283
REMARK 465 SER A 284
REMARK 465 LEU A 285
REMARK 465 GLU A 286
REMARK 465 GLY A 287
REMARK 465 LYS A 288
REMARK 465 LYS A 289
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 2044 O HOH A 2044 7556 2.07
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 MET A 86 SD MET A 86 CE -0.617
REMARK 500 MET A 156 SD MET A 156 CE -0.410
REMARK 500 MET A 175 SD MET A 175 CE -0.440
REMARK 500 MET A 198 SD MET A 198 CE -0.365
REMARK 500 TYR A 211 CD1 TYR A 211 CE1 0.099
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 ASP A 144 CB - CG - OD2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 MET A 175 CG - SD - CE ANGL. DEV. = -12.5 DEGREES
REMARK 500 TYR A 211 CB - CG - CD2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 TYR A 211 CB - CG - CD1 ANGL. DEV. = 4.8 DEGREES
REMARK 500 ASP A 224 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ASP A 235 CB - CG - OD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ARG A 261 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ALA A 270 N - CA - C ANGL. DEV. = 16.7 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 LEU A 103 -120.06 -124.78
REMARK 500 THR A 158 68.74 -110.62
REMARK 500 ASN A 160 158.96 -46.42
REMARK 500 LEU A 218 -77.21 -49.37
REMARK 500 LYS A 226 152.80 -45.62
REMARK 500 CYS A 230 -36.14 -38.46
REMARK 500 ALA A 270 23.49 80.41
REMARK 500 SER A 273 20.73 -58.96
REMARK 500 LEU A 274 -7.41 -56.43
REMARK 500 LEU A 275 59.40 -95.02
REMARK 500 GLU A 279 4.27 -68.03
REMARK 500 GLN A 280 61.57 -101.20
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 IP2 A1282
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1HF8 RELATED DB: PDB
REMARK 900 CALM-N N-TERMINAL DOMAIN OF CLATHRIN ASSEMBLY LYMPHOID MYELOID
REMARK 900 LEUKAEMIA PROTEIN
REMARK 900 RELATED ID: 1HFA RELATED DB: PDB
REMARK 900 CALM-N N-TERMINAL DOMAIN OF CLATHRIN ASSEMBLY LYMPHOID MYELOID
REMARK 900 LEUKAEMIA PROTEIN, PI(4,5)P2 COMPLEX
REMARK 900 RELATED ID: 1HG5 RELATED DB: PDB
REMARK 900 CALM-N N-TERMINAL DOMAIN OF CLATHRIN ASSEMBLY LYMPHOID MYELOID
REMARK 900 LEUKAEMIA PROTEIN, INOSITOL(1,2,3,4,5,6)P6 COMPLEX
DBREF 1HG2 A 1 289 UNP O55011 O55011 1 289
SEQRES 1 A 289 MET SER GLY GLN SER LEU THR ASP ARG ILE THR ALA ALA
SEQRES 2 A 289 GLN HIS SER VAL THR GLY SER ALA VAL SER LYS THR VAL
SEQRES 3 A 289 CYS LYS ALA THR THR HIS GLU ILE MET GLY PRO LYS LYS
SEQRES 4 A 289 LYS HIS LEU ASP TYR LEU ILE GLN CYS THR ASN GLU MET
SEQRES 5 A 289 ASN VAL ASN ILE PRO GLN LEU ALA ASP SER LEU PHE GLU
SEQRES 6 A 289 ARG THR THR ASN SER SER TRP VAL VAL VAL PHE LYS SER
SEQRES 7 A 289 LEU ILE THR THR HIS HIS LEU MET VAL TYR GLY ASN GLU
SEQRES 8 A 289 ARG PHE ILE GLN TYR LEU ALA SER ARG ASN THR LEU PHE
SEQRES 9 A 289 ASN LEU SER ASN PHE LEU ASP LYS SER GLY LEU GLN GLY
SEQRES 10 A 289 TYR ASP MET SER THR PHE ILE ARG ARG TYR SER ARG TYR
SEQRES 11 A 289 LEU ASN GLU LYS ALA VAL SER TYR ARG GLN VAL ALA PHE
SEQRES 12 A 289 ASP PHE THR LYS VAL LYS ARG GLY ALA ASP GLY VAL MET
SEQRES 13 A 289 ARG THR MET ASN THR GLU LYS LEU LEU LYS THR VAL PRO
SEQRES 14 A 289 ILE ILE GLN ASN GLN MET ASP ALA LEU LEU ASP PHE ASN
SEQRES 15 A 289 VAL ASN SER ASN GLU LEU THR ASN GLY VAL ILE ASN ALA
SEQRES 16 A 289 ALA PHE MET LEU LEU PHE LYS ASP ALA ILE ARG LEU PHE
SEQRES 17 A 289 ALA ALA TYR ASN GLU GLY ILE ILE ASN LEU LEU GLU LYS
SEQRES 18 A 289 TYR PHE ASP MET LYS LYS ASN GLN CYS LYS GLU GLY LEU
SEQRES 19 A 289 ASP ILE TYR LYS LYS PHE LEU THR ARG MET THR ARG ILE
SEQRES 20 A 289 SER GLU PHE LEU LYS VAL ALA GLU GLN VAL GLY ILE ASP
SEQRES 21 A 289 ARG GLY ASP ILE PRO ASP LEU SER GLN ALA PRO SER SER
SEQRES 22 A 289 LEU LEU ASP ALA LEU GLU GLN HIS LEU ALA SER LEU GLU
SEQRES 23 A 289 GLY LYS LYS
HET IP2 A1282 40
HETNAM IP2 D-MYO-INOSITOL-4,5-BISPHOSPHATE
FORMUL 2 IP2 C6 H14 O12 P2
FORMUL 3 HOH *128(H2 O)
HELIX 1 1 GLY A 19 THR A 30 1 12
HELIX 2 2 LYS A 38 ASN A 50 1 13
HELIX 3 3 ASN A 55 THR A 67 1 13
HELIX 4 4 SER A 71 GLY A 89 1 19
HELIX 5 5 GLU A 91 ARG A 100 1 10
HELIX 6 6 GLY A 114 ALA A 142 1 29
HELIX 7 7 ASN A 160 ASP A 180 1 21
HELIX 8 8 ASN A 184 LEU A 188 5 5
HELIX 9 9 ASN A 190 PHE A 223 1 34
HELIX 10 10 LYS A 226 GLY A 258 1 33
HELIX 11 11 ASP A 260 ILE A 264 5 5
SITE 1 AC1 3 LYS A 38 LYS A 40 HIS A 41
CRYST1 77.859 77.859 122.333 90.00 90.00 90.00 P 41 21 2 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 0.012844 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012844 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008174 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
