HEADER ENDOCYTOSIS 23-AUG-11 3ZYK
TITLE STRUCTURE OF CALM (PICALM) ANTH DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOSPHATIDYLINOSITOL-BINDING CLATHRIN ASSEMBLY PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: ANTH DOMAIN, RESIDUES 1-289;
COMPND 5 SYNONYM: CALM, CLATHRIN ASSEMBLY LYMPHOID MYELOID LEUKEMIA PROTEIN,
COMPND 6 RCALM;
COMPND 7 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_VARIANT: PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX 4T2 CALMANTH(1-289)
KEYWDS ENDOCYTOSIS, ENDOBREVIN, SYNAPTOBREVIN, VAMP2, VAMP3, AP180, PLASMA
KEYWDS 2 MEMBRANE, ADAPTOR PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR S.E.MILLER,D.A.SAHLENDER,S.C.GRAHAM,S.HONING,M.S.ROBINSON,A.A.PEDEN,
AUTHOR 2 D.J.OWEN
REVDAT 2 13-MAR-19 3ZYK 1 JRNL REMARK
REVDAT 1 07-DEC-11 3ZYK 0
JRNL AUTH S.E.MILLER,D.A.SAHLENDER,S.C.GRAHAM,S.HONING,M.S.ROBINSON,
JRNL AUTH 2 A.A.PEDEN,D.J.OWEN
JRNL TITL THE MOLECULAR BASIS FOR THE ENDOCYTOSIS OF SMALL R-SNARES BY
JRNL TITL 2 THE CLATHRIN ADAPTOR CALM.
JRNL REF CELL V. 147 1118 2011
JRNL REFN ISSN 1097-4172
JRNL PMID 22118466
JRNL DOI 10.1016/J.CELL.2011.10.038
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.01
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : 64141
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.183
REMARK 3 R VALUE (WORKING SET) : 0.182
REMARK 3 FREE R VALUE : 0.216
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3237
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 40.0184 - 5.1155 0.98 2853 141 0.2018 0.2034
REMARK 3 2 5.1155 - 4.0616 0.98 2718 133 0.1571 0.2098
REMARK 3 3 4.0616 - 3.5486 1.00 2711 146 0.1613 0.2075
REMARK 3 4 3.5486 - 3.2243 0.99 2710 136 0.1779 0.1880
REMARK 3 5 3.2243 - 2.9932 0.99 2670 143 0.1906 0.2307
REMARK 3 6 2.9932 - 2.8168 0.99 2677 134 0.1828 0.2275
REMARK 3 7 2.8168 - 2.6758 0.99 2700 133 0.1781 0.2095
REMARK 3 8 2.6758 - 2.5593 0.99 2615 158 0.1783 0.2138
REMARK 3 9 2.5593 - 2.4608 0.99 2649 154 0.1718 0.1671
REMARK 3 10 2.4608 - 2.3759 0.99 2635 152 0.1728 0.2049
REMARK 3 11 2.3759 - 2.3016 0.99 2637 134 0.1751 0.2130
REMARK 3 12 2.3016 - 2.2358 0.99 2621 132 0.1713 0.2109
REMARK 3 13 2.2358 - 2.1770 0.99 2630 148 0.1764 0.2116
REMARK 3 14 2.1770 - 2.1239 0.99 2622 156 0.1796 0.2388
REMARK 3 15 2.1239 - 2.0756 0.99 2631 139 0.1794 0.2244
REMARK 3 16 2.0756 - 2.0314 0.98 2601 144 0.1887 0.2172
REMARK 3 17 2.0314 - 1.9908 0.98 2590 135 0.1840 0.2451
REMARK 3 18 1.9908 - 1.9532 0.98 2624 137 0.1931 0.2390
REMARK 3 19 1.9532 - 1.9183 0.98 2597 139 0.1989 0.2544
REMARK 3 20 1.9183 - 1.8858 0.98 2605 127 0.2122 0.2705
REMARK 3 21 1.8858 - 1.8554 0.98 2600 154 0.2536 0.2667
REMARK 3 22 1.8554 - 1.8269 0.98 2579 147 0.2655 0.3331
REMARK 3 23 1.8269 - 1.8000 0.98 2629 115 0.3013 0.3472
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
REMARK 3 SHRINKAGE RADIUS : 0.83
REMARK 3 K_SOL : 0.36
REMARK 3 B_SOL : 50.68
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.200
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.410
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 25.84
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.69
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.45950
REMARK 3 B22 (A**2) : 1.86710
REMARK 3 B33 (A**2) : -5.32660
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.009 4510
REMARK 3 ANGLE : 1.077 6104
REMARK 3 CHIRALITY : 0.075 695
REMARK 3 PLANARITY : 0.005 782
REMARK 3 DIHEDRAL : 12.450 1740
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A
REMARK 3 ORIGIN FOR THE GROUP (A): -29.2251 -1.3104 0.4530
REMARK 3 T TENSOR
REMARK 3 T11: 0.0405 T22: 0.0651
REMARK 3 T33: 0.0699 T12: 0.0064
REMARK 3 T13: -0.0002 T23: -0.0079
REMARK 3 L TENSOR
REMARK 3 L11: 0.4246 L22: 0.9338
REMARK 3 L33: 1.3394 L12: -0.3856
REMARK 3 L13: 0.1143 L23: -0.3480
REMARK 3 S TENSOR
REMARK 3 S11: 0.0172 S12: 0.0371 S13: 0.0245
REMARK 3 S21: -0.0430 S22: -0.0021 S23: 0.0208
REMARK 3 S31: -0.0720 S32: -0.1917 S33: 0.0005
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN B
REMARK 3 ORIGIN FOR THE GROUP (A): -18.2652 -11.4547 30.3847
REMARK 3 T TENSOR
REMARK 3 T11: 0.0940 T22: 0.1616
REMARK 3 T33: 0.1099 T12: 0.0001
REMARK 3 T13: -0.0413 T23: 0.0272
REMARK 3 L TENSOR
REMARK 3 L11: 0.7357 L22: 1.4000
REMARK 3 L33: 3.9479 L12: -0.0772
REMARK 3 L13: 0.5114 L23: 0.0865
REMARK 3 S TENSOR
REMARK 3 S11: 0.0271 S12: -0.0381 S13: 0.0373
REMARK 3 S21: 0.1985 S22: -0.0224 S23: -0.1911
REMARK 3 S31: 0.3393 S32: 0.5942 S33: 0.0081
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 2
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A AND NOT (RESI 44 OR RESI 47:48 OR
REMARK 3 RESI 51 OR RESI 92 OR RESI 105 OR RESI
REMARK 3 115 OR RESI 118:119 OR RESI 147 OR RESI
REMARK 3 150 OR RESI 202 OR RESI 268:288)
REMARK 3 SELECTION : CHAIN B
REMARK 3 ATOM PAIRS NUMBER : 1929
REMARK 3 RMSD : 0.075
REMARK 3 NCS GROUP : 2
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A AND RESI 271:288
REMARK 3 SELECTION : CHAIN B
REMARK 3 ATOM PAIRS NUMBER : 111
REMARK 3 RMSD : 0.024
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3ZYK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-AUG-11.
REMARK 100 THE DEPOSITION ID IS D_1290049396.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-FEB-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9763
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 64198
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 73.500
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : 14.10
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.1
REMARK 200 DATA REDUNDANCY IN SHELL : 14.50
REMARK 200 R MERGE FOR SHELL (I) : 0.86000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.100
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 1HF8
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.35
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.58
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALS WERE GROWN IN SITTING DROPS
REMARK 280 CONTAINING EQUAL AMOUNTS (200-400 NL) OF PROTEIN (15 MG/ML IN 20
REMARK 280 MM HEPES PH 7.4, 120 MM NACL, 4 MM DTT) AND RESERVOIR SOLUTION
REMARK 280 (100 MM BIS TRIS PROPANE, 200 MM SODIUM MALONATE, 20% (W/V) PEG
REMARK 280 3350) AND EQUILIBRATED AGAINST 80 UL OF RESERVOIR SOLUTION AT
REMARK 280 16C. CRYSTALS WERE CRYOPROTECTED BY BRIEF IMMERSION (5-60 S) IN
REMARK 280 RESERVOIR SOLUTION SUPPLEMENTED WITH 25% GLYCEROL AND WERE
REMARK 280 RAPIDLY CRYOCOOLED IN LIQUID N2 OR A 100 K STREAM OF N2 GAS.,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 289K
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 36.77050
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 60.10850
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.15650
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 60.10850
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 36.77050
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 39.15650
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 GLY A -6
REMARK 465 SER A -5
REMARK 465 PRO A -4
REMARK 465 ILE A -3
REMARK 465 GLY A -2
REMARK 465 ILE A -1
REMARK 465 HIS A 0
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 GLY A 19
REMARK 465 LYS A 289
REMARK 465 GLY B -6
REMARK 465 SER B -5
REMARK 465 PRO B -4
REMARK 465 ILE B -3
REMARK 465 GLY B -2
REMARK 465 ILE B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 GLY B 3
REMARK 465 GLN B 4
REMARK 465 SER B 5
REMARK 465 LEU B 6
REMARK 465 THR B 7
REMARK 465 ASP B 8
REMARK 465 ARG B 9
REMARK 465 ILE B 10
REMARK 465 THR B 11
REMARK 465 ALA B 12
REMARK 465 ALA B 13
REMARK 465 GLN B 14
REMARK 465 HIS B 15
REMARK 465 SER B 16
REMARK 465 VAL B 17
REMARK 465 GLU B 286
REMARK 465 GLY B 287
REMARK 465 LYS B 288
REMARK 465 LYS B 289
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 -112.28 -115.44
REMARK 500 LEU B 103 -113.89 -115.12
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A2031 DISTANCE = 6.15 ANGSTROMS
REMARK 525 HOH A2044 DISTANCE = 6.49 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1HG2 RELATED DB: PDB
REMARK 900 CALM-N N-TERMINAL DOMAIN OF CLATHRIN ASSEMBLY LYMPHOID MYELOID
REMARK 900 LEUKAEMIA PROTEIN, I(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
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: 1HF8 RELATED DB: PDB
REMARK 900 CALM-N N-TERMINAL DOMAIN OF CLATHRIN ASSEMBLY LYMPHOID MYELOID
REMARK 900 LEUKAEMIA PROTEIN
REMARK 900 RELATED ID: 3ZYM RELATED DB: PDB
REMARK 900 STRUCTURE OF CALM (PICALM) IN COMPLEX WITH VAMP8
REMARK 900 RELATED ID: 3ZYL RELATED DB: PDB
REMARK 900 STRUCTURE OF A TRUNCATED CALM (PICALM) ANTH DOMAIN
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 N-TERMINAL GSPIGIH SEQUENCE IS RESIDUAL FROM AFFINITY TAG
REMARK 999 AND CLONING.
DBREF 3ZYK A 1 289 UNP O55012 PICA_RAT 1 289
DBREF 3ZYK B 1 289 UNP O55012 PICA_RAT 1 289
SEQADV 3ZYK GLY A -6 UNP O55012 EXPRESSION TAG
SEQADV 3ZYK SER A -5 UNP O55012 EXPRESSION TAG
SEQADV 3ZYK PRO A -4 UNP O55012 EXPRESSION TAG
SEQADV 3ZYK ILE A -3 UNP O55012 EXPRESSION TAG
SEQADV 3ZYK GLY A -2 UNP O55012 EXPRESSION TAG
SEQADV 3ZYK ILE A -1 UNP O55012 EXPRESSION TAG
SEQADV 3ZYK HIS A 0 UNP O55012 EXPRESSION TAG
SEQADV 3ZYK GLY B -6 UNP O55012 EXPRESSION TAG
SEQADV 3ZYK SER B -5 UNP O55012 EXPRESSION TAG
SEQADV 3ZYK PRO B -4 UNP O55012 EXPRESSION TAG
SEQADV 3ZYK ILE B -3 UNP O55012 EXPRESSION TAG
SEQADV 3ZYK GLY B -2 UNP O55012 EXPRESSION TAG
SEQADV 3ZYK ILE B -1 UNP O55012 EXPRESSION TAG
SEQADV 3ZYK HIS B 0 UNP O55012 EXPRESSION TAG
SEQRES 1 A 296 GLY SER PRO ILE GLY ILE HIS MET SER GLY GLN SER LEU
SEQRES 2 A 296 THR ASP ARG ILE THR ALA ALA GLN HIS SER VAL THR GLY
SEQRES 3 A 296 SER ALA VAL SER LYS THR VAL CYS LYS ALA THR THR HIS
SEQRES 4 A 296 GLU ILE MET GLY PRO LYS LYS LYS HIS LEU ASP TYR LEU
SEQRES 5 A 296 ILE GLN CYS THR ASN GLU MET ASN VAL ASN ILE PRO GLN
SEQRES 6 A 296 LEU ALA ASP SER LEU PHE GLU ARG THR THR ASN SER SER
SEQRES 7 A 296 TRP VAL VAL VAL PHE LYS SER LEU ILE THR THR HIS HIS
SEQRES 8 A 296 LEU MET VAL TYR GLY ASN GLU ARG PHE ILE GLN TYR LEU
SEQRES 9 A 296 ALA SER ARG ASN THR LEU PHE ASN LEU SER ASN PHE LEU
SEQRES 10 A 296 ASP LYS SER GLY LEU GLN GLY TYR ASP MET SER THR PHE
SEQRES 11 A 296 ILE ARG ARG TYR SER ARG TYR LEU ASN GLU LYS ALA VAL
SEQRES 12 A 296 SER TYR ARG GLN VAL ALA PHE ASP PHE THR LYS VAL LYS
SEQRES 13 A 296 ARG GLY ALA ASP GLY VAL MET ARG THR MET ASN THR GLU
SEQRES 14 A 296 LYS LEU LEU LYS THR VAL PRO ILE ILE GLN ASN GLN MET
SEQRES 15 A 296 ASP ALA LEU LEU ASP PHE ASN VAL ASN SER ASN GLU LEU
SEQRES 16 A 296 THR ASN GLY VAL ILE ASN ALA ALA PHE MET LEU LEU PHE
SEQRES 17 A 296 LYS ASP ALA ILE ARG LEU PHE ALA ALA TYR ASN GLU GLY
SEQRES 18 A 296 ILE ILE ASN LEU LEU GLU LYS TYR PHE ASP MET LYS LYS
SEQRES 19 A 296 ASN GLN CYS LYS GLU GLY LEU ASP ILE TYR LYS LYS PHE
SEQRES 20 A 296 LEU THR ARG MET THR ARG ILE SER GLU PHE LEU LYS VAL
SEQRES 21 A 296 ALA GLU GLN VAL GLY ILE ASP ARG GLY ASP ILE PRO ASP
SEQRES 22 A 296 LEU SER GLN ALA PRO SER SER LEU LEU ASP ALA LEU GLU
SEQRES 23 A 296 GLN HIS LEU ALA SER LEU GLU GLY LYS LYS
SEQRES 1 B 296 GLY SER PRO ILE GLY ILE HIS MET SER GLY GLN SER LEU
SEQRES 2 B 296 THR ASP ARG ILE THR ALA ALA GLN HIS SER VAL THR GLY
SEQRES 3 B 296 SER ALA VAL SER LYS THR VAL CYS LYS ALA THR THR HIS
SEQRES 4 B 296 GLU ILE MET GLY PRO LYS LYS LYS HIS LEU ASP TYR LEU
SEQRES 5 B 296 ILE GLN CYS THR ASN GLU MET ASN VAL ASN ILE PRO GLN
SEQRES 6 B 296 LEU ALA ASP SER LEU PHE GLU ARG THR THR ASN SER SER
SEQRES 7 B 296 TRP VAL VAL VAL PHE LYS SER LEU ILE THR THR HIS HIS
SEQRES 8 B 296 LEU MET VAL TYR GLY ASN GLU ARG PHE ILE GLN TYR LEU
SEQRES 9 B 296 ALA SER ARG ASN THR LEU PHE ASN LEU SER ASN PHE LEU
SEQRES 10 B 296 ASP LYS SER GLY LEU GLN GLY TYR ASP MET SER THR PHE
SEQRES 11 B 296 ILE ARG ARG TYR SER ARG TYR LEU ASN GLU LYS ALA VAL
SEQRES 12 B 296 SER TYR ARG GLN VAL ALA PHE ASP PHE THR LYS VAL LYS
SEQRES 13 B 296 ARG GLY ALA ASP GLY VAL MET ARG THR MET ASN THR GLU
SEQRES 14 B 296 LYS LEU LEU LYS THR VAL PRO ILE ILE GLN ASN GLN MET
SEQRES 15 B 296 ASP ALA LEU LEU ASP PHE ASN VAL ASN SER ASN GLU LEU
SEQRES 16 B 296 THR ASN GLY VAL ILE ASN ALA ALA PHE MET LEU LEU PHE
SEQRES 17 B 296 LYS ASP ALA ILE ARG LEU PHE ALA ALA TYR ASN GLU GLY
SEQRES 18 B 296 ILE ILE ASN LEU LEU GLU LYS TYR PHE ASP MET LYS LYS
SEQRES 19 B 296 ASN GLN CYS LYS GLU GLY LEU ASP ILE TYR LYS LYS PHE
SEQRES 20 B 296 LEU THR ARG MET THR ARG ILE SER GLU PHE LEU LYS VAL
SEQRES 21 B 296 ALA GLU GLN VAL GLY ILE ASP ARG GLY ASP ILE PRO ASP
SEQRES 22 B 296 LEU SER GLN ALA PRO SER SER LEU LEU ASP ALA LEU GLU
SEQRES 23 B 296 GLN HIS LEU ALA SER LEU GLU GLY LYS LYS
FORMUL 3 HOH *415(H2 O)
HELIX 1 1 SER A 20 THR A 30 1 11
HELIX 2 2 LYS A 38 GLU A 51 1 14
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 ASN A 90 ARG A 100 1 11
HELIX 6 6 GLY A 114 ALA A 142 1 29
HELIX 7 7 GLY A 154 MET A 159 1 6
HELIX 8 8 ASN A 160 ASP A 180 1 21
HELIX 9 9 ASN A 184 LEU A 188 5 5
HELIX 10 10 ASN A 190 TYR A 222 1 33
HELIX 11 11 PHE A 223 MET A 225 5 3
HELIX 12 12 LYS A 226 GLY A 258 1 33
HELIX 13 13 ASP A 260 ILE A 264 5 5
HELIX 14 14 ASP A 266 ALA A 270 5 5
HELIX 15 15 LEU A 274 GLU A 286 1 13
HELIX 16 16 THR B 18 THR B 30 1 13
HELIX 17 17 LYS B 38 GLU B 51 1 14
HELIX 18 18 ASN B 55 THR B 67 1 13
HELIX 19 19 SER B 71 GLY B 89 1 19
HELIX 20 20 ASN B 90 ARG B 100 1 11
HELIX 21 21 GLY B 114 ALA B 142 1 29
HELIX 22 22 GLY B 154 MET B 159 1 6
HELIX 23 23 ASN B 160 ASP B 180 1 21
HELIX 24 24 ASN B 184 LEU B 188 5 5
HELIX 25 25 ASN B 190 TYR B 222 1 33
HELIX 26 26 PHE B 223 MET B 225 5 3
HELIX 27 27 LYS B 226 GLY B 258 1 33
HELIX 28 28 ASP B 260 ILE B 264 5 5
HELIX 29 29 ASP B 266 ALA B 270 5 5
HELIX 30 30 LEU B 274 LEU B 285 1 12
CRYST1 73.541 78.313 120.217 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 0.013598 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012769 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008318 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
