HEADER PROTEIN TRANSPORT 28-APR-09 2KI6
TITLE THE FGF1-S100A13-C2A HETERO-HEXAMERIC COMPLEX STRUCTURE: A COMPONENT
TITLE 2 IN THE NON-CLASSICAL PATHWAY FOR FGF1 SECRETION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SYNAPTOTAGMIN-1;
COMPND 3 CHAIN: A, F;
COMPND 4 FRAGMENT: C2A DOMAIN;
COMPND 5 SYNONYM: SYNAPTOTAGMIN I, SYTI, P65;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: HEPARIN-BINDING GROWTH FACTOR 1;
COMPND 9 CHAIN: B, E;
COMPND 10 SYNONYM: HBGF-1, ACIDIC FIBROBLAST GROWTH FACTOR, AFGF, BETA-
COMPND 11 ENDOTHELIAL CELL GROWTH FACTOR, ECGF-BETA;
COMPND 12 ENGINEERED: YES;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: PROTEIN S100-A13;
COMPND 15 CHAIN: C;
COMPND 16 SYNONYM: S100 CALCIUM-BINDING PROTEIN A13;
COMPND 17 ENGINEERED: YES;
COMPND 18 MOL_ID: 4;
COMPND 19 MOLECULE: PROTEIN S100-A13;
COMPND 20 CHAIN: D;
COMPND 21 SYNONYM: S100 CALCIUM-BINDING PROTEIN A13;
COMPND 22 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: SYT1, SVP65, SYT;
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: PET(20);
SOURCE 10 OTHER_DETAILS: PURIFIED FROM HEPARIN AFFINITY COLUMN;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: FGF1, FGFA;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 19 EXPRESSION_SYSTEM_VECTOR: PGEX;
SOURCE 20 OTHER_DETAILS: PURIFIED FROM GST COLUMN;
SOURCE 21 MOL_ID: 3;
SOURCE 22 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 23 ORGANISM_COMMON: HUMAN;
SOURCE 24 ORGANISM_TAXID: 9606;
SOURCE 25 GENE: S100A13;
SOURCE 26 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 27 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 28 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 29 EXPRESSION_SYSTEM_VECTOR: PGEX;
SOURCE 30 OTHER_DETAILS: PURIFIED FROM GST COLUMN;
SOURCE 31 MOL_ID: 4;
SOURCE 32 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 33 ORGANISM_COMMON: HUMAN;
SOURCE 34 ORGANISM_TAXID: 9606;
SOURCE 35 GENE: S100A13;
SOURCE 36 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 37 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 38 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 39 EXPRESSION_SYSTEM_VECTOR: PGEX;
SOURCE 40 OTHER_DETAILS: PURIFIED FROM GST COLUMN
KEYWDS FGF1-S100A13-C2A HETERO-HEXAMERIC COMPLEX, FGF1, S100A13, C2A,
KEYWDS 2 CALCIUM, CELL JUNCTION, CYTOPLASMIC VESICLE, GLYCOPROTEIN,
KEYWDS 3 LIPOPROTEIN, MEMBRANE, METAL-BINDING, PALMITATE, PHOSPHOPROTEIN,
KEYWDS 4 SYNAPSE, TRANSMEMBRANE, ACETYLATION, ALTERNATIVE SPLICING,
KEYWDS 5 ANGIOGENESIS, DEVELOPMENTAL PROTEIN, DIFFERENTIATION, GROWTH FACTOR,
KEYWDS 6 HEPARIN-BINDING, MITOGEN, POLYMORPHISM, PROTEIN TRANSPORT
EXPDTA SOLUTION NMR
NUMMDL 18
AUTHOR S.M.KRISHNA,S.G.RANI,C.YU
REVDAT 2 19-MAY-10 2KI6 1 JRNL
REVDAT 1 09-MAR-10 2KI6 0
JRNL AUTH S.K.MOHAN,S.G.RANI,C.YU
JRNL TITL THE HETEROHEXAMERIC COMPLEX STRUCTURE, A COMPONENT IN THE
JRNL TITL 2 NON-CLASSICAL PATHWAY FOR FIBROBLAST GROWTH FACTOR 1 (FGF1)
JRNL TITL 3 SECRETION.
JRNL REF J.BIOL.CHEM. V. 285 15464 2010
JRNL REFN ISSN 0021-9258
JRNL PMID 20220137
JRNL DOI 10.1074/JBC.M109.066357
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNSSOLVE 1.1 & 1.2
REMARK 3 AUTHORS : BRUNGER, ADAMS, CLORE, GROS, NILGES AND READ
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: CNS
REMARK 4
REMARK 4 2KI6 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-JUN-09.
REMARK 100 THE RCSB ID CODE IS RCSB101150.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : 0.1
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.0MM [U-100% 13C; U-100% 15N]
REMARK 210 C2A DOMAIN OF SYT1-1, 1.0MM FGF1-
REMARK 210 2, 1.0MM S100A13-3, S100A13-4,
REMARK 210 25MM SODIUM PHOSPHATE-5, 100MM
REMARK 210 SODIUM CHLORIDE-6, 90% H2O/10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-15N HSQC; 2D 1H-13C HSQC;
REMARK 210 3D HNCO; 3D HNCA; 3D CBCA(CO)NH;
REMARK 210 3D C(CO)NH; 3D HBHA(CO)NH; 3D
REMARK 210 HCCH-TOCSY; 3D 1H-15N NOESY; 3D
REMARK 210 1H-13C NOESY; 3D-13C-FILTER
REMARK 210 NOESY; 3D-15N-FILTER NOESY; 3D
REMARK 210 H(CCO)NH
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : ARIA 1.2 &2.2, CNSSOLVE 1.1 &
REMARK 210 1.2, SPARKY, TOPSPIN 1.3
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 2000
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 18
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: C2A(15N&13C LABELED) MIXED WITH UNLABELED FGF1-S100A13
REMARK 210 COMPLEX BUFFER CONDITION (25MM PBD, 100MM NACL AND 2MM CACL2)
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
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: HEXAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F
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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
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 HD21 ASN B 88 HH TYR B 90 1.32
REMARK 500 HD21 ASN E 88 HH TYR E 90 1.32
REMARK 500 HG SER B 92 H VAL B 102 1.42
REMARK 500 H TYR F 41 O TYR F 90 1.46
REMARK 500 H TYR A 41 O TYR A 90 1.47
REMARK 500 H ASN B 88 O PHE B 125 1.47
REMARK 500 HD1 HIS B 14 O GLY B 26 1.48
REMARK 500 HD1 HIS E 14 O GLY E 26 1.48
REMARK 500 OD2 ASP F 39 HH11 ARG F 94 1.48
REMARK 500 H ASN E 88 O PHE E 125 1.49
REMARK 500 OD2 ASP A 39 HH11 ARG A 94 1.49
REMARK 500 HH11 ARG E 17 OG1 THR E 27 1.51
REMARK 500 HH11 ARG B 17 OG1 THR B 27 1.51
REMARK 500 O TYR E 8 H LEU E 126 1.52
REMARK 500 O TYR B 8 H LEU B 126 1.52
REMARK 500 O PRO A 40 HD1 HIS A 59 1.53
REMARK 500 O PRO F 40 HD1 HIS F 59 1.53
REMARK 500 O LEU A 10 H THR A 117 1.53
REMARK 500 OE1 GLU A 79 HZ3 LYS A 83 1.54
REMARK 500 OE1 GLU F 79 HZ3 LYS F 83 1.54
REMARK 500 O GLN F 7 H ILE F 24 1.55
REMARK 500 O GLN A 7 H ILE A 24 1.55
REMARK 500 H ALA B 59 O TYR B 67 1.56
REMARK 500 H ALA E 59 O TYR E 67 1.56
REMARK 500 OE2 GLU F 119 HH21 ARG F 121 1.56
REMARK 500 HH TYR B 1 HZ2 LYS B 3 1.57
REMARK 500 HH TYR E 1 HZ2 LYS E 3 1.57
REMARK 500 OD1 ASP B 25 HG1 THR B 27 1.58
REMARK 500 OE2 GLU E 46 HZ3 LYS E 93 1.58
REMARK 500 OD1 ASP E 25 HG1 THR E 27 1.58
REMARK 500 OE2 GLU B 46 HZ3 LYS B 93 1.58
REMARK 500 OD2 ASP F 93 H SER F 96 1.58
REMARK 500 OD2 ASP A 93 H SER A 96 1.58
REMARK 500 HG SER E 92 H VAL E 102 1.58
REMARK 500 O ILE E 18 HD1 HIS E 34 1.59
REMARK 500 O LYS A 5 H ALA A 27 1.59
REMARK 500 H ASP E 61 O LEU E 65 1.59
REMARK 500 O ILE B 18 HD1 HIS B 34 1.59
REMARK 500 OE2 GLU A 119 HH21 ARG A 121 1.59
REMARK 500 H ASP B 61 O LEU B 65 1.59
REMARK 500 O ASP F 11 H LEU F 20 1.60
REMARK 500 O ASP A 11 H LEU A 20 1.60
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 1 ASN A 17 64.17 74.60
REMARK 500 1 GLU A 28 75.08 60.40
REMARK 500 1 LEU A 32 -53.31 -131.03
REMARK 500 1 ASP A 39 64.48 -113.78
REMARK 500 1 LEU A 47 -173.41 -61.26
REMARK 500 1 PRO A 48 -44.70 -24.45
REMARK 500 1 LYS A 50 28.59 44.37
REMARK 500 1 LYS A 51 57.27 -96.71
REMARK 500 1 LYS A 52 137.14 169.88
REMARK 500 1 LYS A 61 76.73 37.48
REMARK 500 1 ASN A 64 55.35 -150.37
REMARK 500 1 PHE A 67 -49.03 -165.18
REMARK 500 1 ASN A 68 71.80 68.73
REMARK 500 1 LYS A 74 92.07 -62.50
REMARK 500 1 VAL A 75 130.21 -179.66
REMARK 500 1 ARG A 94 20.36 81.83
REMARK 500 1 PHE A 95 -59.57 -137.38
REMARK 500 1 ASP A 112 97.75 -63.41
REMARK 500 1 PHE A 113 66.30 -69.54
REMARK 500 1 HIS A 115 -78.75 -150.32
REMARK 500 1 LYS B 2 108.49 -50.69
REMARK 500 1 PRO B 4 105.10 -18.76
REMARK 500 1 SER B 10 120.10 75.90
REMARK 500 1 GLN B 33 76.21 -68.64
REMARK 500 1 HIS B 34 16.46 -144.25
REMARK 500 1 VAL B 44 93.79 -53.40
REMARK 500 1 THR B 52 -70.19 -54.32
REMARK 500 1 THR B 54 -41.08 175.11
REMARK 500 1 ALA B 59 84.35 -159.91
REMARK 500 1 ASP B 63 -52.44 68.79
REMARK 500 1 SER B 69 -62.64 171.13
REMARK 500 1 GLN B 70 -71.36 -62.62
REMARK 500 1 ASN B 85 21.35 -143.85
REMARK 500 1 SER B 92 80.02 -69.04
REMARK 500 1 VAL B 102 121.84 -15.24
REMARK 500 1 SER B 109 175.54 138.98
REMARK 500 1 LYS B 111 79.78 -179.49
REMARK 500 1 ARG B 112 32.11 -142.86
REMARK 500 1 SER B 132 65.50 -110.16
REMARK 500 1 GLU C 27 -160.56 -117.40
REMARK 500 1 ARG C 29 121.07 73.50
REMARK 500 1 LYS C 30 47.65 -91.10
REMARK 500 1 ASP C 31 -50.79 -141.17
REMARK 500 1 GLN C 44 -62.92 -100.45
REMARK 500 1 LEU C 50 78.97 -111.28
REMARK 500 1 LYS C 51 2.89 -67.27
REMARK 500 1 SER C 55 45.89 -97.95
REMARK 500 1 ASP C 92 73.36 -59.01
REMARK 500 1 LEU C 93 -51.72 -175.93
REMARK 500 1 ARG C 96 -46.55 -178.63
REMARK 500
REMARK 500 THIS ENTRY HAS 2014 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 LYS C 89 LYS C 90 1 -117.54
REMARK 500 ALA D 2 ALA D 3 1 143.13
REMARK 500 ALA D 3 GLU D 4 1 142.47
REMARK 500 GLY D 28 ARG D 29 1 137.21
REMARK 500 VAL D 35 ASN D 36 1 144.13
REMARK 500 ASP D 64 VAL D 65 1 -129.94
REMARK 500 ASN D 74 GLU D 75 1 112.56
REMARK 500 LYS D 91 ASP D 92 1 -145.57
REMARK 500 LYS C 89 LYS C 90 2 -117.49
REMARK 500 ALA D 2 ALA D 3 2 143.07
REMARK 500 ALA D 3 GLU D 4 2 142.33
REMARK 500 GLY D 28 ARG D 29 2 137.24
REMARK 500 VAL D 35 ASN D 36 2 144.09
REMARK 500 ASP D 64 VAL D 65 2 -129.90
REMARK 500 ASN D 74 GLU D 75 2 112.53
REMARK 500 LYS D 91 ASP D 92 2 -145.50
REMARK 500 LYS C 89 LYS C 90 3 -117.58
REMARK 500 ALA D 2 ALA D 3 3 143.16
REMARK 500 ALA D 3 GLU D 4 3 142.41
REMARK 500 GLY D 28 ARG D 29 3 137.18
REMARK 500 VAL D 35 ASN D 36 3 144.01
REMARK 500 ASP D 64 VAL D 65 3 -129.87
REMARK 500 ASN D 74 GLU D 75 3 112.57
REMARK 500 LYS D 91 ASP D 92 3 -145.49
REMARK 500 LYS C 89 LYS C 90 4 -117.48
REMARK 500 ALA D 2 ALA D 3 4 143.09
REMARK 500 ALA D 3 GLU D 4 4 142.39
REMARK 500 GLY D 28 ARG D 29 4 137.20
REMARK 500 VAL D 35 ASN D 36 4 144.05
REMARK 500 ASP D 64 VAL D 65 4 -129.84
REMARK 500 ASN D 74 GLU D 75 4 112.67
REMARK 500 LYS D 91 ASP D 92 4 -145.61
REMARK 500 LYS C 89 LYS C 90 5 -117.42
REMARK 500 ALA D 2 ALA D 3 5 143.18
REMARK 500 ALA D 3 GLU D 4 5 142.41
REMARK 500 GLY D 28 ARG D 29 5 137.17
REMARK 500 VAL D 35 ASN D 36 5 144.14
REMARK 500 ASP D 64 VAL D 65 5 -129.96
REMARK 500 ASN D 74 GLU D 75 5 112.63
REMARK 500 LYS D 91 ASP D 92 5 -145.60
REMARK 500 LYS C 89 LYS C 90 6 -117.42
REMARK 500 ALA D 2 ALA D 3 6 143.07
REMARK 500 ALA D 3 GLU D 4 6 142.39
REMARK 500 GLY D 28 ARG D 29 6 137.18
REMARK 500 VAL D 35 ASN D 36 6 144.09
REMARK 500 ASP D 64 VAL D 65 6 -129.85
REMARK 500 ASN D 74 GLU D 75 6 112.59
REMARK 500 LYS D 91 ASP D 92 6 -145.59
REMARK 500 LYS C 89 LYS C 90 7 -117.48
REMARK 500 ALA D 2 ALA D 3 7 143.07
REMARK 500
REMARK 500 THIS ENTRY HAS 144 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 1 PHE C 38 0.08 SIDE CHAIN
REMARK 500 1 ARG C 78 0.18 SIDE CHAIN
REMARK 500 1 ARG C 96 0.13 SIDE CHAIN
REMARK 500 1 TYR D 76 0.07 SIDE CHAIN
REMARK 500 1 ARG D 78 0.08 SIDE CHAIN
REMARK 500 2 PHE C 38 0.08 SIDE CHAIN
REMARK 500 2 ARG C 78 0.18 SIDE CHAIN
REMARK 500 2 ARG C 96 0.12 SIDE CHAIN
REMARK 500 2 TYR D 76 0.07 SIDE CHAIN
REMARK 500 2 ARG D 78 0.08 SIDE CHAIN
REMARK 500 3 PHE C 38 0.08 SIDE CHAIN
REMARK 500 3 ARG C 78 0.18 SIDE CHAIN
REMARK 500 3 ARG C 96 0.13 SIDE CHAIN
REMARK 500 3 TYR D 76 0.07 SIDE CHAIN
REMARK 500 3 ARG D 78 0.08 SIDE CHAIN
REMARK 500 4 PHE C 38 0.08 SIDE CHAIN
REMARK 500 4 ARG C 78 0.18 SIDE CHAIN
REMARK 500 4 ARG C 96 0.13 SIDE CHAIN
REMARK 500 4 TYR D 76 0.07 SIDE CHAIN
REMARK 500 4 ARG D 78 0.08 SIDE CHAIN
REMARK 500 5 PHE C 38 0.08 SIDE CHAIN
REMARK 500 5 ARG C 78 0.18 SIDE CHAIN
REMARK 500 5 ARG C 96 0.13 SIDE CHAIN
REMARK 500 5 TYR D 76 0.07 SIDE CHAIN
REMARK 500 5 ARG D 78 0.08 SIDE CHAIN
REMARK 500 6 PHE C 38 0.08 SIDE CHAIN
REMARK 500 6 ARG C 78 0.18 SIDE CHAIN
REMARK 500 6 ARG C 96 0.13 SIDE CHAIN
REMARK 500 6 TYR D 76 0.07 SIDE CHAIN
REMARK 500 6 ARG D 78 0.08 SIDE CHAIN
REMARK 500 7 PHE C 38 0.08 SIDE CHAIN
REMARK 500 7 ARG C 78 0.18 SIDE CHAIN
REMARK 500 7 ARG C 96 0.13 SIDE CHAIN
REMARK 500 7 TYR D 76 0.07 SIDE CHAIN
REMARK 500 7 ARG D 78 0.08 SIDE CHAIN
REMARK 500 8 PHE C 38 0.08 SIDE CHAIN
REMARK 500 8 ARG C 78 0.18 SIDE CHAIN
REMARK 500 8 ARG C 96 0.13 SIDE CHAIN
REMARK 500 8 TYR D 76 0.07 SIDE CHAIN
REMARK 500 8 ARG D 78 0.08 SIDE CHAIN
REMARK 500 9 PHE C 38 0.08 SIDE CHAIN
REMARK 500 9 ARG C 78 0.18 SIDE CHAIN
REMARK 500 9 ARG C 96 0.13 SIDE CHAIN
REMARK 500 9 TYR D 76 0.07 SIDE CHAIN
REMARK 500 9 ARG D 78 0.08 SIDE CHAIN
REMARK 500 10 PHE C 38 0.08 SIDE CHAIN
REMARK 500 10 ARG C 78 0.18 SIDE CHAIN
REMARK 500 10 ARG C 96 0.13 SIDE CHAIN
REMARK 500 10 TYR D 76 0.07 SIDE CHAIN
REMARK 500 10 ARG D 78 0.08 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 90 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE CHAIN C AND D ARE S100A13 MONOMERS; BUT IN CHAIN C AND D THE
REMARK 999 94, 97 AND 98 RESIDUES ARE DIFFERENT ISOMERS (DLY OR LYS).
DBREF 2KI6 A 1 128 UNP P21579 SYT1_HUMAN 141 268
DBREF 2KI6 B 1 133 UNP P05230 FGF1_HUMAN 23 155
DBREF 2KI6 C 1 98 UNP Q99584 S10AD_HUMAN 1 98
DBREF 2KI6 D 1 98 UNP Q99584 S10AD_HUMAN 1 98
DBREF 2KI6 E 1 133 UNP P05230 FGF1_HUMAN 23 155
DBREF 2KI6 F 1 128 UNP P21579 SYT1_HUMAN 141 268
SEQADV 2KI6 DLY C 97 UNP Q99584 LYS 97 SEE REMARK 999
SEQADV 2KI6 DLY C 98 UNP Q99584 LYS 98 SEE REMARK 999
SEQADV 2KI6 DLY D 94 UNP Q99584 LYS 94 SEE REMARK 999
SEQRES 1 A 128 GLU LYS LEU GLY LYS LEU GLN TYR SER LEU ASP TYR ASP
SEQRES 2 A 128 PHE GLN ASN ASN GLN LEU LEU VAL GLY ILE ILE GLN ALA
SEQRES 3 A 128 ALA GLU LEU PRO ALA LEU ASP MET GLY GLY THR SER ASP
SEQRES 4 A 128 PRO TYR VAL LYS VAL PHE LEU LEU PRO ASP LYS LYS LYS
SEQRES 5 A 128 LYS PHE GLU THR LYS VAL HIS ARG LYS THR LEU ASN PRO
SEQRES 6 A 128 VAL PHE ASN GLU GLN PHE THR PHE LYS VAL PRO TYR SER
SEQRES 7 A 128 GLU LEU GLY GLY LYS THR LEU VAL MET ALA VAL TYR ASP
SEQRES 8 A 128 PHE ASP ARG PHE SER LYS HIS ASP ILE ILE GLY GLU PHE
SEQRES 9 A 128 LYS VAL PRO MET ASN THR VAL ASP PHE GLY HIS VAL THR
SEQRES 10 A 128 GLU GLU TRP ARG ASP LEU GLN SER ALA GLU LYS
SEQRES 1 B 133 TYR LYS LYS PRO LYS LEU LEU TYR CYS SER ASN GLY GLY
SEQRES 2 B 133 HIS PHE LEU ARG ILE LEU PRO ASP GLY THR VAL ASP GLY
SEQRES 3 B 133 THR ARG ASP ARG SER ASP GLN HIS ILE GLN LEU GLN LEU
SEQRES 4 B 133 SER ALA GLU SER VAL GLY GLU VAL TYR ILE LYS SER THR
SEQRES 5 B 133 GLU THR GLY GLN TYR LEU ALA MET ASP THR ASP GLY LEU
SEQRES 6 B 133 LEU TYR GLY SER GLN THR PRO ASN GLU GLU CYS LEU PHE
SEQRES 7 B 133 LEU GLU ARG LEU GLU GLU ASN HIS TYR ASN THR TYR ILE
SEQRES 8 B 133 SER LYS LYS HIS ALA GLU LYS ASN TRP PHE VAL GLY LEU
SEQRES 9 B 133 LYS LYS ASN GLY SER CYS LYS ARG GLY PRO ARG THR HIS
SEQRES 10 B 133 TYR GLY GLN LYS ALA ILE LEU PHE LEU PRO LEU PRO VAL
SEQRES 11 B 133 SER SER ASP
SEQRES 1 C 98 MET ALA ALA GLU PRO LEU THR GLU LEU GLU GLU SER ILE
SEQRES 2 C 98 GLU THR VAL VAL THR THR PHE PHE THR PHE ALA ARG GLN
SEQRES 3 C 98 GLU GLY ARG LYS ASP SER LEU SER VAL ASN GLU PHE LYS
SEQRES 4 C 98 GLU LEU VAL THR GLN GLN LEU PRO HIS LEU LEU LYS ASP
SEQRES 5 C 98 VAL GLY SER LEU ASP GLU LYS MET LYS SER LEU ASP VAL
SEQRES 6 C 98 ASN GLN ASP SER GLU LEU LYS PHE ASN GLU TYR TRP ARG
SEQRES 7 C 98 LEU ILE GLY GLU LEU ALA LYS GLU ILE ARG LYS LYS LYS
SEQRES 8 C 98 ASP LEU LYS ILE ARG DLY DLY
SEQRES 1 D 98 MET ALA ALA GLU PRO LEU THR GLU LEU GLU GLU SER ILE
SEQRES 2 D 98 GLU THR VAL VAL THR THR PHE PHE THR PHE ALA ARG GLN
SEQRES 3 D 98 GLU GLY ARG LYS ASP SER LEU SER VAL ASN GLU PHE LYS
SEQRES 4 D 98 GLU LEU VAL THR GLN GLN LEU PRO HIS LEU LEU LYS ASP
SEQRES 5 D 98 VAL GLY SER LEU ASP GLU LYS MET LYS SER LEU ASP VAL
SEQRES 6 D 98 ASN GLN ASP SER GLU LEU LYS PHE ASN GLU TYR TRP ARG
SEQRES 7 D 98 LEU ILE GLY GLU LEU ALA LYS GLU ILE ARG LYS LYS LYS
SEQRES 8 D 98 ASP LEU DLY ILE ARG LYS LYS
SEQRES 1 E 133 TYR LYS LYS PRO LYS LEU LEU TYR CYS SER ASN GLY GLY
SEQRES 2 E 133 HIS PHE LEU ARG ILE LEU PRO ASP GLY THR VAL ASP GLY
SEQRES 3 E 133 THR ARG ASP ARG SER ASP GLN HIS ILE GLN LEU GLN LEU
SEQRES 4 E 133 SER ALA GLU SER VAL GLY GLU VAL TYR ILE LYS SER THR
SEQRES 5 E 133 GLU THR GLY GLN TYR LEU ALA MET ASP THR ASP GLY LEU
SEQRES 6 E 133 LEU TYR GLY SER GLN THR PRO ASN GLU GLU CYS LEU PHE
SEQRES 7 E 133 LEU GLU ARG LEU GLU GLU ASN HIS TYR ASN THR TYR ILE
SEQRES 8 E 133 SER LYS LYS HIS ALA GLU LYS ASN TRP PHE VAL GLY LEU
SEQRES 9 E 133 LYS LYS ASN GLY SER CYS LYS ARG GLY PRO ARG THR HIS
SEQRES 10 E 133 TYR GLY GLN LYS ALA ILE LEU PHE LEU PRO LEU PRO VAL
SEQRES 11 E 133 SER SER ASP
SEQRES 1 F 128 GLU LYS LEU GLY LYS LEU GLN TYR SER LEU ASP TYR ASP
SEQRES 2 F 128 PHE GLN ASN ASN GLN LEU LEU VAL GLY ILE ILE GLN ALA
SEQRES 3 F 128 ALA GLU LEU PRO ALA LEU ASP MET GLY GLY THR SER ASP
SEQRES 4 F 128 PRO TYR VAL LYS VAL PHE LEU LEU PRO ASP LYS LYS LYS
SEQRES 5 F 128 LYS PHE GLU THR LYS VAL HIS ARG LYS THR LEU ASN PRO
SEQRES 6 F 128 VAL PHE ASN GLU GLN PHE THR PHE LYS VAL PRO TYR SER
SEQRES 7 F 128 GLU LEU GLY GLY LYS THR LEU VAL MET ALA VAL TYR ASP
SEQRES 8 F 128 PHE ASP ARG PHE SER LYS HIS ASP ILE ILE GLY GLU PHE
SEQRES 9 F 128 LYS VAL PRO MET ASN THR VAL ASP PHE GLY HIS VAL THR
SEQRES 10 F 128 GLU GLU TRP ARG ASP LEU GLN SER ALA GLU LYS
HET DLY C 97 22
HET DLY C 98 22
HET DLY D 94 22
HETNAM DLY D-LYSINE
FORMUL 3 DLY 3(C6 H14 N2 O2)
HELIX 1 1 PRO A 76 GLY A 81 1 6
HELIX 2 2 ASN A 109 VAL A 111 5 3
HELIX 3 3 ASN B 73 GLU B 75 5 3
HELIX 4 4 SER B 92 GLU B 97 1 6
HELIX 5 5 ARG B 112 THR B 116 5 5
HELIX 6 6 GLN B 120 ILE B 123 5 4
HELIX 7 7 THR C 7 ARG C 25 1 19
HELIX 8 8 SER C 34 LEU C 46 1 13
HELIX 9 9 SER C 55 ASP C 64 1 10
HELIX 10 10 LYS C 72 LYS C 90 1 19
HELIX 11 11 THR D 7 ARG D 25 1 19
HELIX 12 12 GLU D 37 GLN D 45 1 9
HELIX 13 13 SER D 55 ASP D 64 1 10
HELIX 14 14 TRP D 77 ILE D 87 1 11
HELIX 15 15 ASN E 73 GLU E 75 5 3
HELIX 16 16 SER E 92 GLU E 97 1 6
HELIX 17 17 ARG E 112 THR E 116 5 5
HELIX 18 18 GLN E 120 ILE E 123 5 4
HELIX 19 19 PRO F 76 GLY F 81 1 6
HELIX 20 20 PRO F 107 VAL F 111 5 5
SHEET 1 A 4 GLN A 70 LYS A 74 0
SHEET 2 A 4 GLN A 18 ALA A 27 -1 N LEU A 19 O PHE A 73
SHEET 3 A 4 GLY A 4 ASP A 13 -1 N LYS A 5 O ALA A 27
SHEET 4 A 4 VAL A 116 LEU A 123 -1 O THR A 117 N LEU A 10
SHEET 1 B 4 PHE A 54 GLU A 55 0
SHEET 2 B 4 TYR A 41 LEU A 46 -1 N VAL A 44 O PHE A 54
SHEET 3 B 4 THR A 84 TYR A 90 -1 O TYR A 90 N TYR A 41
SHEET 4 B 4 ILE A 100 PRO A 107 -1 O PHE A 104 N MET A 87
SHEET 1 C 2 LEU B 7 CYS B 9 0
SHEET 2 C 2 PHE B 125 PRO B 127 -1 O LEU B 126 N TYR B 8
SHEET 1 D 2 PHE B 15 ARG B 17 0
SHEET 2 D 2 ASP B 25 THR B 27 -1 O ASP B 25 N ARG B 17
SHEET 1 E 4 SER B 40 SER B 43 0
SHEET 2 E 4 GLU B 46 TYR B 48 -1 O TYR B 48 N SER B 40
SHEET 3 E 4 LEU B 77 GLU B 83 -1 O PHE B 78 N VAL B 47
SHEET 4 E 4 TYR B 87 ILE B 91 -1 O THR B 89 N ARG B 81
SHEET 1 F 2 TYR B 57 LEU B 58 0
SHEET 2 F 2 GLY B 68 SER B 69 -1 O SER B 69 N TYR B 57
SHEET 1 G 2 LEU B 104 LYS B 105 0
SHEET 2 G 2 SER B 109 CYS B 110 -1 O SER B 109 N LYS B 105
SHEET 1 H 2 LEU E 7 CYS E 9 0
SHEET 2 H 2 PHE E 125 PRO E 127 -1 O LEU E 126 N TYR E 8
SHEET 1 I 2 PHE E 15 ARG E 17 0
SHEET 2 I 2 ASP E 25 THR E 27 -1 O ASP E 25 N ARG E 17
SHEET 1 J 4 SER E 40 SER E 43 0
SHEET 2 J 4 GLU E 46 TYR E 48 -1 O TYR E 48 N SER E 40
SHEET 3 J 4 LEU E 77 GLU E 83 -1 O PHE E 78 N VAL E 47
SHEET 4 J 4 TYR E 87 ILE E 91 -1 O THR E 89 N ARG E 81
SHEET 1 K 2 TYR E 57 LEU E 58 0
SHEET 2 K 2 GLY E 68 SER E 69 -1 O SER E 69 N TYR E 57
SHEET 1 L 2 LEU E 104 LYS E 105 0
SHEET 2 L 2 SER E 109 CYS E 110 -1 O SER E 109 N LYS E 105
SHEET 1 M 4 GLN F 70 LYS F 74 0
SHEET 2 M 4 GLN F 18 ALA F 27 -1 N LEU F 19 O PHE F 73
SHEET 3 M 4 GLY F 4 ASP F 13 -1 N GLN F 7 O ILE F 24
SHEET 4 M 4 VAL F 116 LEU F 123 -1 O LEU F 123 N GLY F 4
SHEET 1 N 4 PHE F 54 GLU F 55 0
SHEET 2 N 4 TYR F 41 LEU F 46 -1 N VAL F 44 O PHE F 54
SHEET 3 N 4 LEU F 85 TYR F 90 -1 O TYR F 90 N TYR F 41
SHEET 4 N 4 ILE F 100 VAL F 106 -1 O PHE F 104 N MET F 87
LINK C ARG C 96 N DLY C 97 1555 1555 1.34
LINK C DLY C 97 N DLY C 98 1555 1555 1.33
LINK C LEU D 93 N DLY D 94 1555 1555 1.33
LINK C DLY D 94 N ILE D 95 1555 1555 1.33
CISPEP 1 ILE C 95 ARG C 96 1 -9.26
CISPEP 2 ARG C 96 DLY C 97 1 5.14
CISPEP 3 DLY C 97 DLY C 98 1 11.10
CISPEP 4 ILE C 95 ARG C 96 2 -9.30
CISPEP 5 ARG C 96 DLY C 97 2 5.05
CISPEP 6 DLY C 97 DLY C 98 2 11.02
CISPEP 7 ILE C 95 ARG C 96 3 -9.31
CISPEP 8 ARG C 96 DLY C 97 3 5.12
CISPEP 9 DLY C 97 DLY C 98 3 11.13
CISPEP 10 ILE C 95 ARG C 96 4 -9.35
CISPEP 11 ARG C 96 DLY C 97 4 5.14
CISPEP 12 DLY C 97 DLY C 98 4 11.25
CISPEP 13 ILE C 95 ARG C 96 5 -9.36
CISPEP 14 ARG C 96 DLY C 97 5 5.12
CISPEP 15 DLY C 97 DLY C 98 5 10.97
CISPEP 16 ILE C 95 ARG C 96 6 -9.32
CISPEP 17 ARG C 96 DLY C 97 6 5.17
CISPEP 18 DLY C 97 DLY C 98 6 11.02
CISPEP 19 ILE C 95 ARG C 96 7 -9.35
CISPEP 20 ARG C 96 DLY C 97 7 5.19
CISPEP 21 DLY C 97 DLY C 98 7 10.97
CISPEP 22 ILE C 95 ARG C 96 8 -9.43
CISPEP 23 ARG C 96 DLY C 97 8 5.22
CISPEP 24 DLY C 97 DLY C 98 8 11.13
CISPEP 25 ILE C 95 ARG C 96 9 -9.28
CISPEP 26 ARG C 96 DLY C 97 9 5.21
CISPEP 27 DLY C 97 DLY C 98 9 11.02
CISPEP 28 ILE C 95 ARG C 96 10 -9.30
CISPEP 29 ARG C 96 DLY C 97 10 5.15
CISPEP 30 DLY C 97 DLY C 98 10 11.04
CISPEP 31 ILE C 95 ARG C 96 11 -9.16
CISPEP 32 ARG C 96 DLY C 97 11 5.07
CISPEP 33 DLY C 97 DLY C 98 11 11.05
CISPEP 34 ILE C 95 ARG C 96 12 -9.16
CISPEP 35 ARG C 96 DLY C 97 12 5.34
CISPEP 36 DLY C 97 DLY C 98 12 10.99
CISPEP 37 ILE C 95 ARG C 96 13 -9.42
CISPEP 38 ARG C 96 DLY C 97 13 5.12
CISPEP 39 DLY C 97 DLY C 98 13 11.04
CISPEP 40 ILE C 95 ARG C 96 14 -9.36
CISPEP 41 ARG C 96 DLY C 97 14 5.18
CISPEP 42 DLY C 97 DLY C 98 14 11.13
CISPEP 43 ILE C 95 ARG C 96 15 -9.33
CISPEP 44 ARG C 96 DLY C 97 15 5.08
CISPEP 45 DLY C 97 DLY C 98 15 10.99
CISPEP 46 ILE C 95 ARG C 96 16 -9.26
CISPEP 47 ARG C 96 DLY C 97 16 5.11
CISPEP 48 DLY C 97 DLY C 98 16 11.08
CISPEP 49 ILE C 95 ARG C 96 17 -9.32
CISPEP 50 ARG C 96 DLY C 97 17 5.13
CISPEP 51 DLY C 97 DLY C 98 17 11.11
CISPEP 52 ILE C 95 ARG C 96 18 -9.41
CISPEP 53 ARG C 96 DLY C 97 18 5.24
CISPEP 54 DLY C 97 DLY C 98 18 11.03
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
(ATOM LINES ARE NOT SHOWN.)
END