HEADER MEMBRANE PROTEIN 02-JUL-03 1PX2
TITLE CRYSTAL STRUCTURE OF RAT SYNAPSIN I C DOMAIN COMPLEXED TO CA.ATP (FORM
TITLE 2 1)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SYNAPSIN I;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: A, B, & C DOMAINS;
COMPND 5 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 GENE: SYN1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR: PGEX;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PSYNABC
KEYWDS ATP BINDING, ATP GRASP, CALCIUM (II) ION, MEMBRANE PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR C.A.BRAUTIGAM,Y.CHELLIAH,J.DEISENHOFER
REVDAT 5 13-MAR-24 1PX2 1 COMPND SOURCE
REVDAT 4 16-AUG-23 1PX2 1 REMARK SEQADV LINK
REVDAT 3 13-JUL-11 1PX2 1 VERSN
REVDAT 2 24-FEB-09 1PX2 1 VERSN
REVDAT 1 23-MAR-04 1PX2 0
JRNL AUTH C.A.BRAUTIGAM,Y.CHELLIAH,J.DEISENHOFER
JRNL TITL TETRAMERIZATION AND ATP BINDING BY A PROTEIN COMPRISING THE
JRNL TITL 2 A, B, AND C DOMAINS OF RAT SYNAPSIN I.
JRNL REF J.BIOL.CHEM. V. 279 11948 2004
JRNL REFN ISSN 0021-9258
JRNL PMID 14688264
JRNL DOI 10.1074/JBC.M312015200
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH L.ESSER,C.R.WANG,M.HOSAKA,C.S.SMAGULA,T.C.SUDHOF,
REMARK 1 AUTH 2 J.DEISENHOFER
REMARK 1 TITL SYNAPSIN I IS STRUCTURALLY SIMILAR TO ATP-UTILIZING ENZYMES
REMARK 1 REF EMBO J. V. 17 977 1998
REMARK 1 REFN ISSN 0261-4189
REMARK 1 DOI 10.1093/EMBOJ/17.4.977
REMARK 2
REMARK 2 RESOLUTION. 2.23 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
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 : MODIFIED ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.23
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 97.1
REMARK 3 NUMBER OF REFLECTIONS : 40481
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) : 0.203
REMARK 3 FREE R VALUE : 0.240
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2033
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
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) : 2.23
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.37
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.80
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 5971
REMARK 3 BIN R VALUE (WORKING SET) : 0.2330
REMARK 3 BIN FREE R VALUE : 0.2870
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.70
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 297
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.017
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4678
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 64
REMARK 3 SOLVENT ATOMS : 326
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 28.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.11000
REMARK 3 B22 (A**2) : 1.11000
REMARK 3 B33 (A**2) : -2.21000
REMARK 3 B12 (A**2) : 2.73000
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) : 0.25
REMARK 3 ESD FROM SIGMAA (A) : 0.19
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) : 0.32
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.24
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.60
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.490
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 : 0.33
REMARK 3 BSOL : 41.00
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: ALTHOUGH THE A, B, AND C DOMAINS OF RAT
REMARK 3 SYNAPSIN I WERE INCLUDED IN CRYSTALLIZATION, ONLY THE C DOMAIN
REMARK 3 WAS OBSERVED. SOME RESIDUES HAVE SIDE CHAINS THAT ARE SET TO
REMARK 3 OCCUPANCIES OF 0.00 DUE TO DISORDER.
REMARK 4
REMARK 4 1PX2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-JUL-03.
REMARK 100 THE DEPOSITION ID IS D_1000019656.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-JUL-00
REMARK 200 TEMPERATURE (KELVIN) : 93
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CHESS
REMARK 200 BEAMLINE : F1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.942
REMARK 200 MONOCHROMATOR : HORIZONTALLY BENT SI(111), WITH
REMARK 200 MONOCHROMATIC MIRRORS OF RH-
REMARK 200 COATED SI
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 41721
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.230
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 11.20
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 29.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.23
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.31
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 9.00
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.39100
REMARK 200 <I/SIGMA(I)> FOR SHELL : 6.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: EPMR
REMARK 200 STARTING MODEL: PDB ENTRY 1AUX, CA AND ATP-GAMMA-S REMOVED
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.89
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEGMME 5K, TRIS, NACL, CA.ATP, EDTA,
REMARK 280 PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 299K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
REMARK 290 7555 Y,X,-Z+2/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+1/3
REMARK 290 10555 -Y,-X,-Z+1/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+5/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 203.86667
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 101.93333
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 152.90000
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 50.96667
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 254.83333
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 203.86667
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 101.93333
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 50.96667
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 152.90000
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 254.83333
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 300 REMARK: THE SECOND HALF OF THE (PRESUMABLY) BIOLOGICAL TETRAMER IS
REMARK 300 GENERATED BY THE TWOFOLD AXIS: -Y + 1, -X + 1, -Z + 1/6
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 14980 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 48320 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -108.0 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 350 BIOMT1 2 0.500000 -0.866025 0.000000 48.00000
REMARK 350 BIOMT2 2 -0.866025 -0.500000 0.000000 83.13844
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 50.96667
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 0
REMARK 465 SER A 1
REMARK 465 ASN A 2
REMARK 465 TYR A 3
REMARK 465 LEU A 4
REMARK 465 ARG A 5
REMARK 465 ARG A 6
REMARK 465 ARG A 7
REMARK 465 LEU A 8
REMARK 465 SER A 9
REMARK 465 ASP A 10
REMARK 465 SER A 11
REMARK 465 ASN A 12
REMARK 465 PHE A 13
REMARK 465 MET A 14
REMARK 465 ALA A 15
REMARK 465 ASN A 16
REMARK 465 LEU A 17
REMARK 465 PRO A 18
REMARK 465 ASN A 19
REMARK 465 GLY A 20
REMARK 465 TYR A 21
REMARK 465 MET A 22
REMARK 465 THR A 23
REMARK 465 ASP A 24
REMARK 465 LEU A 25
REMARK 465 GLN A 26
REMARK 465 ARG A 27
REMARK 465 PRO A 28
REMARK 465 GLN A 29
REMARK 465 PRO A 30
REMARK 465 PRO A 31
REMARK 465 PRO A 32
REMARK 465 PRO A 33
REMARK 465 PRO A 34
REMARK 465 PRO A 35
REMARK 465 SER A 36
REMARK 465 ALA A 37
REMARK 465 ALA A 38
REMARK 465 SER A 39
REMARK 465 PRO A 40
REMARK 465 GLY A 41
REMARK 465 ALA A 42
REMARK 465 THR A 43
REMARK 465 PRO A 44
REMARK 465 GLY A 45
REMARK 465 SER A 46
REMARK 465 ALA A 47
REMARK 465 ALA A 48
REMARK 465 ALA A 49
REMARK 465 SER A 50
REMARK 465 ALA A 51
REMARK 465 GLU A 52
REMARK 465 ARG A 53
REMARK 465 ALA A 54
REMARK 465 SER A 55
REMARK 465 THR A 56
REMARK 465 ALA A 57
REMARK 465 ALA A 58
REMARK 465 PRO A 59
REMARK 465 VAL A 60
REMARK 465 ALA A 61
REMARK 465 SER A 62
REMARK 465 PRO A 63
REMARK 465 ALA A 64
REMARK 465 ALA A 65
REMARK 465 PRO A 66
REMARK 465 SER A 67
REMARK 465 PRO A 68
REMARK 465 GLY A 69
REMARK 465 SER A 70
REMARK 465 SER A 71
REMARK 465 GLY A 72
REMARK 465 GLY A 73
REMARK 465 GLY A 74
REMARK 465 GLY A 75
REMARK 465 PHE A 76
REMARK 465 PHE A 77
REMARK 465 SER A 78
REMARK 465 SER A 79
REMARK 465 LEU A 80
REMARK 465 SER A 81
REMARK 465 ASN A 82
REMARK 465 ALA A 83
REMARK 465 VAL A 84
REMARK 465 LYS A 85
REMARK 465 GLN A 86
REMARK 465 THR A 87
REMARK 465 THR A 88
REMARK 465 ALA A 89
REMARK 465 ALA A 90
REMARK 465 ALA A 91
REMARK 465 ALA A 92
REMARK 465 ALA A 93
REMARK 465 THR A 94
REMARK 465 PHE A 95
REMARK 465 SER A 96
REMARK 465 GLU A 97
REMARK 465 GLN A 98
REMARK 465 VAL A 99
REMARK 465 GLY A 100
REMARK 465 GLY A 101
REMARK 465 GLY A 102
REMARK 465 SER A 103
REMARK 465 GLY A 104
REMARK 465 GLY A 105
REMARK 465 ALA A 106
REMARK 465 GLY A 107
REMARK 465 ARG A 108
REMARK 465 GLY A 109
REMARK 465 GLY A 110
REMARK 465 ALA A 111
REMARK 465 SER A 330
REMARK 465 VAL A 331
REMARK 465 SER A 332
REMARK 465 GLY A 333
REMARK 465 ASN A 334
REMARK 465 THR A 337
REMARK 465 ASN A 338
REMARK 465 THR A 339
REMARK 465 GLY A 340
REMARK 465 SER A 341
REMARK 465 ALA A 342
REMARK 465 MET A 343
REMARK 465 LEU A 418
REMARK 465 PRO A 419
REMARK 465 ARG A 420
REMARK 465 GLN A 421
REMARK 465 GLY B 0
REMARK 465 SER B 1
REMARK 465 ASN B 2
REMARK 465 TYR B 3
REMARK 465 LEU B 4
REMARK 465 ARG B 5
REMARK 465 ARG B 6
REMARK 465 ARG B 7
REMARK 465 LEU B 8
REMARK 465 SER B 9
REMARK 465 ASP B 10
REMARK 465 SER B 11
REMARK 465 ASN B 12
REMARK 465 PHE B 13
REMARK 465 MET B 14
REMARK 465 ALA B 15
REMARK 465 ASN B 16
REMARK 465 LEU B 17
REMARK 465 PRO B 18
REMARK 465 ASN B 19
REMARK 465 GLY B 20
REMARK 465 TYR B 21
REMARK 465 MET B 22
REMARK 465 THR B 23
REMARK 465 ASP B 24
REMARK 465 LEU B 25
REMARK 465 GLN B 26
REMARK 465 ARG B 27
REMARK 465 PRO B 28
REMARK 465 GLN B 29
REMARK 465 PRO B 30
REMARK 465 PRO B 31
REMARK 465 PRO B 32
REMARK 465 PRO B 33
REMARK 465 PRO B 34
REMARK 465 PRO B 35
REMARK 465 SER B 36
REMARK 465 ALA B 37
REMARK 465 ALA B 38
REMARK 465 SER B 39
REMARK 465 PRO B 40
REMARK 465 GLY B 41
REMARK 465 ALA B 42
REMARK 465 THR B 43
REMARK 465 PRO B 44
REMARK 465 GLY B 45
REMARK 465 SER B 46
REMARK 465 ALA B 47
REMARK 465 ALA B 48
REMARK 465 ALA B 49
REMARK 465 SER B 50
REMARK 465 ALA B 51
REMARK 465 GLU B 52
REMARK 465 ARG B 53
REMARK 465 ALA B 54
REMARK 465 SER B 55
REMARK 465 THR B 56
REMARK 465 ALA B 57
REMARK 465 ALA B 58
REMARK 465 PRO B 59
REMARK 465 VAL B 60
REMARK 465 ALA B 61
REMARK 465 SER B 62
REMARK 465 PRO B 63
REMARK 465 ALA B 64
REMARK 465 ALA B 65
REMARK 465 PRO B 66
REMARK 465 SER B 67
REMARK 465 PRO B 68
REMARK 465 GLY B 69
REMARK 465 SER B 70
REMARK 465 SER B 71
REMARK 465 GLY B 72
REMARK 465 GLY B 73
REMARK 465 GLY B 74
REMARK 465 GLY B 75
REMARK 465 PHE B 76
REMARK 465 PHE B 77
REMARK 465 SER B 78
REMARK 465 SER B 79
REMARK 465 LEU B 80
REMARK 465 SER B 81
REMARK 465 ASN B 82
REMARK 465 ALA B 83
REMARK 465 VAL B 84
REMARK 465 LYS B 85
REMARK 465 GLN B 86
REMARK 465 THR B 87
REMARK 465 THR B 88
REMARK 465 ALA B 89
REMARK 465 ALA B 90
REMARK 465 ALA B 91
REMARK 465 ALA B 92
REMARK 465 ALA B 93
REMARK 465 THR B 94
REMARK 465 PHE B 95
REMARK 465 SER B 96
REMARK 465 GLU B 97
REMARK 465 GLN B 98
REMARK 465 VAL B 99
REMARK 465 GLY B 100
REMARK 465 GLY B 101
REMARK 465 GLY B 102
REMARK 465 SER B 103
REMARK 465 GLY B 104
REMARK 465 GLY B 105
REMARK 465 ALA B 106
REMARK 465 GLY B 107
REMARK 465 ARG B 108
REMARK 465 GLY B 109
REMARK 465 GLY B 110
REMARK 465 ALA B 111
REMARK 465 ALA B 112
REMARK 465 SER B 330
REMARK 465 VAL B 331
REMARK 465 SER B 332
REMARK 465 GLY B 333
REMARK 465 ASN B 334
REMARK 465 ASN B 338
REMARK 465 THR B 339
REMARK 465 GLY B 340
REMARK 465 SER B 341
REMARK 465 ALA B 342
REMARK 465 MET B 343
REMARK 465 LEU B 418
REMARK 465 PRO B 419
REMARK 465 ARG B 420
REMARK 465 GLN B 421
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 LYS A 128 CG CD CE NZ
REMARK 480 ARG B 194 CG CD NE CZ NH1 NH2
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 TYR A 312 159.94 179.07
REMARK 500 GLU B 138 -39.38 -133.86
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 CA A 817 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 386 OE2
REMARK 620 2 ATP A 800 O2A 75.5
REMARK 620 3 ATP A 800 O1G 88.0 109.3
REMARK 620 4 ATP A 800 O1G 173.4 108.6 85.8
REMARK 620 5 ATP A 800 O3G 112.6 115.2 24.6 61.1
REMARK 620 6 ATP A 800 O2B 125.9 66.8 70.6 53.5 57.5
REMARK 620 7 ATP A 800 O3B 127.3 69.9 68.4 51.7 54.5 3.2
REMARK 620 8 ATP A 800 O2A 78.2 4.5 106.1 105.5 111.0 62.4 65.5
REMARK 620 9 HOH A 832 O 107.5 172.3 64.1 67.8 57.0 106.3 103.1 167.9
REMARK 620 N 1 2 3 4 5 6 7 8
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 817 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 373 OE2
REMARK 620 2 GLU B 373 OE1 44.4
REMARK 620 3 GLU B 386 OE2 68.1 83.6
REMARK 620 4 ATP B 800 O2A 101.6 64.7 76.8
REMARK 620 5 ATP B 800 O2A 104.2 63.4 86.8 10.2
REMARK 620 6 ATP B 800 O1G 125.1 111.8 164.2 106.1 97.0
REMARK 620 7 ATP B 800 O3G 112.8 152.0 70.6 117.3 123.7 94.8
REMARK 620 8 ATP B 800 O3G 132.9 163.2 111.4 124.7 122.9 53.9 41.0
REMARK 620 9 ATP B 800 O1B 140.8 132.3 72.8 69.7 74.2 93.4 50.3 62.3
REMARK 620 N 1 2 3 4 5 6 7 8
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 817
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 817
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP A 800
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP B 800
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1PK8 RELATED DB: PDB
REMARK 900 FORM 2 OF SAME STRUCTURE
REMARK 900 RELATED ID: 1AUX RELATED DB: PDB
REMARK 900 BOVINE SYNAPSIN I C DOMAIN COMPLEXED TO CA.ATP-GAMMA-S
DBREF 1PX2 A 1 421 UNP P09951 SYN1_RAT 1 421
DBREF 1PX2 B 1 421 UNP P09951 SYN1_RAT 1 421
SEQADV 1PX2 GLY A 0 UNP P09951 CLONING ARTIFACT
SEQADV 1PX2 SER A 1 UNP P09951 MET 1 CLONING ARTIFACT
SEQADV 1PX2 GLY B 0 UNP P09951 CLONING ARTIFACT
SEQADV 1PX2 SER B 1 UNP P09951 MET 1 CLONING ARTIFACT
SEQRES 1 A 422 GLY SER ASN TYR LEU ARG ARG ARG LEU SER ASP SER ASN
SEQRES 2 A 422 PHE MET ALA ASN LEU PRO ASN GLY TYR MET THR ASP LEU
SEQRES 3 A 422 GLN ARG PRO GLN PRO PRO PRO PRO PRO PRO SER ALA ALA
SEQRES 4 A 422 SER PRO GLY ALA THR PRO GLY SER ALA ALA ALA SER ALA
SEQRES 5 A 422 GLU ARG ALA SER THR ALA ALA PRO VAL ALA SER PRO ALA
SEQRES 6 A 422 ALA PRO SER PRO GLY SER SER GLY GLY GLY GLY PHE PHE
SEQRES 7 A 422 SER SER LEU SER ASN ALA VAL LYS GLN THR THR ALA ALA
SEQRES 8 A 422 ALA ALA ALA THR PHE SER GLU GLN VAL GLY GLY GLY SER
SEQRES 9 A 422 GLY GLY ALA GLY ARG GLY GLY ALA ALA ALA ARG VAL LEU
SEQRES 10 A 422 LEU VAL ILE ASP GLU PRO HIS THR ASP TRP ALA LYS TYR
SEQRES 11 A 422 PHE LYS GLY LYS LYS ILE HIS GLY GLU ILE ASP ILE LYS
SEQRES 12 A 422 VAL GLU GLN ALA GLU PHE SER ASP LEU ASN LEU VAL ALA
SEQRES 13 A 422 HIS ALA ASN GLY GLY PHE SER VAL ASP MET GLU VAL LEU
SEQRES 14 A 422 ARG ASN GLY VAL LYS VAL VAL ARG SER LEU LYS PRO ASP
SEQRES 15 A 422 PHE VAL LEU ILE ARG GLN HIS ALA PHE SER MET ALA ARG
SEQRES 16 A 422 ASN GLY ASP TYR ARG SER LEU VAL ILE GLY LEU GLN TYR
SEQRES 17 A 422 ALA GLY ILE PRO SER VAL ASN SER LEU HIS SER VAL TYR
SEQRES 18 A 422 ASN PHE CYS ASP LYS PRO TRP VAL PHE ALA GLN MET VAL
SEQRES 19 A 422 ARG LEU HIS LYS LYS LEU GLY THR GLU GLU PHE PRO LEU
SEQRES 20 A 422 ILE ASP GLN THR PHE TYR PRO ASN HIS LYS GLU MET LEU
SEQRES 21 A 422 SER SER THR THR TYR PRO VAL VAL VAL LYS MET GLY HIS
SEQRES 22 A 422 ALA HIS SER GLY MET GLY LYS VAL LYS VAL ASP ASN GLN
SEQRES 23 A 422 HIS ASP PHE GLN ASP ILE ALA SER VAL VAL ALA LEU THR
SEQRES 24 A 422 LYS THR TYR ALA THR ALA GLU PRO PHE ILE ASP ALA LYS
SEQRES 25 A 422 TYR ASP VAL ARG VAL GLN LYS ILE GLY GLN ASN TYR LYS
SEQRES 26 A 422 ALA TYR MET ARG THR SER VAL SER GLY ASN TRP LYS THR
SEQRES 27 A 422 ASN THR GLY SER ALA MET LEU GLU GLN ILE ALA MET SER
SEQRES 28 A 422 ASP ARG TYR LYS LEU TRP VAL ASP THR CYS SER GLU ILE
SEQRES 29 A 422 PHE GLY GLY LEU ASP ILE CYS ALA VAL GLU ALA LEU HIS
SEQRES 30 A 422 GLY LYS ASP GLY ARG ASP HIS ILE ILE GLU VAL VAL GLY
SEQRES 31 A 422 SER SER MET PRO LEU ILE GLY ASP HIS GLN ASP GLU ASP
SEQRES 32 A 422 LYS GLN LEU ILE VAL GLU LEU VAL VAL ASN LYS MET THR
SEQRES 33 A 422 GLN ALA LEU PRO ARG GLN
SEQRES 1 B 422 GLY SER ASN TYR LEU ARG ARG ARG LEU SER ASP SER ASN
SEQRES 2 B 422 PHE MET ALA ASN LEU PRO ASN GLY TYR MET THR ASP LEU
SEQRES 3 B 422 GLN ARG PRO GLN PRO PRO PRO PRO PRO PRO SER ALA ALA
SEQRES 4 B 422 SER PRO GLY ALA THR PRO GLY SER ALA ALA ALA SER ALA
SEQRES 5 B 422 GLU ARG ALA SER THR ALA ALA PRO VAL ALA SER PRO ALA
SEQRES 6 B 422 ALA PRO SER PRO GLY SER SER GLY GLY GLY GLY PHE PHE
SEQRES 7 B 422 SER SER LEU SER ASN ALA VAL LYS GLN THR THR ALA ALA
SEQRES 8 B 422 ALA ALA ALA THR PHE SER GLU GLN VAL GLY GLY GLY SER
SEQRES 9 B 422 GLY GLY ALA GLY ARG GLY GLY ALA ALA ALA ARG VAL LEU
SEQRES 10 B 422 LEU VAL ILE ASP GLU PRO HIS THR ASP TRP ALA LYS TYR
SEQRES 11 B 422 PHE LYS GLY LYS LYS ILE HIS GLY GLU ILE ASP ILE LYS
SEQRES 12 B 422 VAL GLU GLN ALA GLU PHE SER ASP LEU ASN LEU VAL ALA
SEQRES 13 B 422 HIS ALA ASN GLY GLY PHE SER VAL ASP MET GLU VAL LEU
SEQRES 14 B 422 ARG ASN GLY VAL LYS VAL VAL ARG SER LEU LYS PRO ASP
SEQRES 15 B 422 PHE VAL LEU ILE ARG GLN HIS ALA PHE SER MET ALA ARG
SEQRES 16 B 422 ASN GLY ASP TYR ARG SER LEU VAL ILE GLY LEU GLN TYR
SEQRES 17 B 422 ALA GLY ILE PRO SER VAL ASN SER LEU HIS SER VAL TYR
SEQRES 18 B 422 ASN PHE CYS ASP LYS PRO TRP VAL PHE ALA GLN MET VAL
SEQRES 19 B 422 ARG LEU HIS LYS LYS LEU GLY THR GLU GLU PHE PRO LEU
SEQRES 20 B 422 ILE ASP GLN THR PHE TYR PRO ASN HIS LYS GLU MET LEU
SEQRES 21 B 422 SER SER THR THR TYR PRO VAL VAL VAL LYS MET GLY HIS
SEQRES 22 B 422 ALA HIS SER GLY MET GLY LYS VAL LYS VAL ASP ASN GLN
SEQRES 23 B 422 HIS ASP PHE GLN ASP ILE ALA SER VAL VAL ALA LEU THR
SEQRES 24 B 422 LYS THR TYR ALA THR ALA GLU PRO PHE ILE ASP ALA LYS
SEQRES 25 B 422 TYR ASP VAL ARG VAL GLN LYS ILE GLY GLN ASN TYR LYS
SEQRES 26 B 422 ALA TYR MET ARG THR SER VAL SER GLY ASN TRP LYS THR
SEQRES 27 B 422 ASN THR GLY SER ALA MET LEU GLU GLN ILE ALA MET SER
SEQRES 28 B 422 ASP ARG TYR LYS LEU TRP VAL ASP THR CYS SER GLU ILE
SEQRES 29 B 422 PHE GLY GLY LEU ASP ILE CYS ALA VAL GLU ALA LEU HIS
SEQRES 30 B 422 GLY LYS ASP GLY ARG ASP HIS ILE ILE GLU VAL VAL GLY
SEQRES 31 B 422 SER SER MET PRO LEU ILE GLY ASP HIS GLN ASP GLU ASP
SEQRES 32 B 422 LYS GLN LEU ILE VAL GLU LEU VAL VAL ASN LYS MET THR
SEQRES 33 B 422 GLN ALA LEU PRO ARG GLN
HET CA A 817 1
HET ATP A 800 62
HET CA B 817 1
HET ATP B 800 62
HETNAM CA CALCIUM ION
HETNAM ATP ADENOSINE-5'-TRIPHOSPHATE
FORMUL 3 CA 2(CA 2+)
FORMUL 4 ATP 2(C10 H16 N5 O13 P3)
FORMUL 7 HOH *326(H2 O)
HELIX 1 1 ASP A 125 LYS A 131 1 7
HELIX 2 2 HIS A 136 GLU A 138 5 3
HELIX 3 3 GLU A 147 SER A 149 5 3
HELIX 4 4 TYR A 198 ALA A 208 1 11
HELIX 5 5 SER A 215 PHE A 222 1 8
HELIX 6 6 ASP A 224 PHE A 244 1 21
HELIX 7 7 ASN A 254 MET A 258 5 5
HELIX 8 8 ASN A 284 LYS A 299 1 16
HELIX 9 9 SER A 350 SER A 361 1 12
HELIX 10 10 GLU A 362 GLY A 366 5 5
HELIX 11 11 ILE A 395 ASP A 397 5 3
HELIX 12 12 HIS A 398 GLN A 416 1 19
HELIX 13 13 ASP B 125 LYS B 131 1 7
HELIX 14 14 HIS B 136 GLU B 138 5 3
HELIX 15 15 GLU B 147 SER B 149 5 3
HELIX 16 16 TYR B 198 ALA B 208 1 11
HELIX 17 17 SER B 215 PHE B 222 1 8
HELIX 18 18 ASP B 224 GLY B 240 1 17
HELIX 19 19 ASN B 254 MET B 258 5 5
HELIX 20 20 ASN B 284 LYS B 299 1 16
HELIX 21 21 SER B 350 SER B 361 1 12
HELIX 22 22 GLU B 362 GLY B 366 5 5
HELIX 23 23 ILE B 395 ASP B 397 5 3
HELIX 24 24 HIS B 398 GLN B 416 1 19
SHEET 1 A 5 LYS A 134 ILE A 135 0
SHEET 2 A 5 ILE A 139 ALA A 146 -1 O ILE A 139 N ILE A 135
SHEET 3 A 5 ARG A 114 ILE A 119 1 N LEU A 116 O LYS A 142
SHEET 4 A 5 PHE A 182 ILE A 185 1 O LEU A 184 N ILE A 119
SHEET 5 A 5 SER A 212 VAL A 213 1 O VAL A 213 N VAL A 183
SHEET 1 B 7 VAL A 172 LEU A 178 0
SHEET 2 B 7 PHE A 161 ARG A 169 -1 N VAL A 163 O LEU A 178
SHEET 3 B 7 LEU A 151 HIS A 156 -1 N ASN A 152 O ASP A 164
SHEET 4 B 7 THR B 250 TYR B 252 -1 O PHE B 251 N ALA A 155
SHEET 5 B 7 ALA B 302 PRO B 306 -1 O ALA B 302 N TYR B 252
SHEET 6 B 7 VAL B 266 MET B 270 -1 N VAL B 267 O GLU B 305
SHEET 7 B 7 LYS B 279 VAL B 282 -1 O VAL B 282 N VAL B 266
SHEET 1 C 7 LYS A 279 VAL A 282 0
SHEET 2 C 7 VAL A 266 MET A 270 -1 N VAL A 266 O VAL A 282
SHEET 3 C 7 ALA A 302 PRO A 306 -1 O GLU A 305 N VAL A 267
SHEET 4 C 7 THR A 250 TYR A 252 -1 N TYR A 252 O ALA A 302
SHEET 5 C 7 LEU B 151 HIS B 156 -1 O ALA B 155 N PHE A 251
SHEET 6 C 7 PHE B 161 ARG B 169 -1 O ASP B 164 N ASN B 152
SHEET 7 C 7 VAL B 172 LEU B 178 -1 O VAL B 174 N VAL B 167
SHEET 1 D 5 GLU A 345 ILE A 347 0
SHEET 2 D 5 ASN A 322 ARG A 328 -1 N MET A 327 O GLU A 345
SHEET 3 D 5 ALA A 310 ILE A 319 -1 N ASP A 313 O ARG A 328
SHEET 4 D 5 ILE A 369 GLY A 377 -1 O ALA A 374 N VAL A 314
SHEET 5 D 5 ASP A 382 VAL A 388 -1 O GLU A 386 N GLU A 373
SHEET 1 E 5 LYS B 134 ILE B 135 0
SHEET 2 E 5 ILE B 139 ALA B 146 -1 O ILE B 139 N ILE B 135
SHEET 3 E 5 ARG B 114 ILE B 119 1 N VAL B 118 O GLU B 144
SHEET 4 E 5 PHE B 182 ILE B 185 1 O PHE B 182 N LEU B 117
SHEET 5 E 5 SER B 212 VAL B 213 1 O VAL B 213 N VAL B 183
SHEET 1 F 5 GLU B 345 ILE B 347 0
SHEET 2 F 5 ASN B 322 ARG B 328 -1 N MET B 327 O GLU B 345
SHEET 3 F 5 ALA B 310 ILE B 319 -1 N ASP B 313 O ARG B 328
SHEET 4 F 5 ILE B 369 GLY B 377 -1 O ALA B 374 N VAL B 314
SHEET 5 F 5 ASP B 382 VAL B 388 -1 O GLU B 386 N GLU B 373
LINK OE2 GLU A 386 CA CA A 817 1555 1555 2.37
LINK O2ABATP A 800 CA CA A 817 1555 1555 2.52
LINK O1GAATP A 800 CA CA A 817 1555 1555 2.64
LINK O1GBATP A 800 CA CA A 817 1555 1555 2.64
LINK O3GBATP A 800 CA CA A 817 1555 1555 2.38
LINK O2BAATP A 800 CA CA A 817 1555 1555 3.26
LINK O3BBATP A 800 CA CA A 817 1555 1555 2.95
LINK O2AAATP A 800 CA CA A 817 1555 1555 2.43
LINK CA CA A 817 O HOH A 832 1555 1555 3.17
LINK OE2AGLU B 373 CA CA B 817 1555 1555 2.20
LINK OE1AGLU B 373 CA CA B 817 1555 1555 3.15
LINK OE2 GLU B 386 CA CA B 817 1555 1555 2.66
LINK O2ABATP B 800 CA CA B 817 1555 1555 2.43
LINK O2AAATP B 800 CA CA B 817 1555 1555 2.53
LINK O1GBATP B 800 CA CA B 817 1555 1555 3.10
LINK O3GAATP B 800 CA CA B 817 1555 1555 2.94
LINK O3GBATP B 800 CA CA B 817 1555 1555 2.32
LINK O1BBATP B 800 CA CA B 817 1555 1555 3.08
LINK O2BAATP B 800 CA CA B 817 1555 1555 2.65
LINK O3BAATP B 800 CA CA B 817 1555 1555 3.35
LINK O3BBATP B 800 CA CA B 817 1555 1555 3.01
LINK CA CA B 817 O HOH B 883 1555 1555 2.96
LINK CA CA B 817 O HOH B 916 1555 1555 3.32
CISPEP 1 VAL A 213 ASN A 214 0 -1.86
CISPEP 2 TYR A 264 PRO A 265 0 0.25
CISPEP 3 VAL B 213 ASN B 214 0 -1.81
CISPEP 4 TYR B 264 PRO B 265 0 -0.56
SITE 1 AC1 3 GLU A 373 GLU A 386 ATP A 800
SITE 1 AC2 4 GLU B 373 GLU B 386 ATP B 800 HOH B 883
SITE 1 AC3 16 LYS A 225 LYS A 269 HIS A 274 SER A 275
SITE 2 AC3 16 GLY A 276 LYS A 279 GLU A 305 PRO A 306
SITE 3 AC3 16 PHE A 307 ILE A 308 LYS A 336 LEU A 375
SITE 4 AC3 16 GLU A 386 CA A 817 HOH A 832 HOH A 905
SITE 1 AC4 24 LYS B 225 ILE B 247 VAL B 267 LYS B 269
SITE 2 AC4 24 ALA B 273 HIS B 274 SER B 275 GLY B 276
SITE 3 AC4 24 LYS B 279 GLU B 305 PRO B 306 PHE B 307
SITE 4 AC4 24 ILE B 308 TRP B 335 THR B 337 GLU B 373
SITE 5 AC4 24 LEU B 375 ILE B 385 GLU B 386 CA B 817
SITE 6 AC4 24 HOH B 857 HOH B 863 HOH B 883 HOH B 916
CRYST1 96.000 96.000 305.800 90.00 90.00 120.00 P 65 2 2 24
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 0.010417 0.006014 0.000000 0.00000
SCALE2 0.000000 0.012028 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003270 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
