HEADER TRANSFERASE 25-SEP-13 3J4Q
TITLE PSEUDO-ATOMIC MODEL OF THE AKAP18-PKA COMPLEX IN A BENT CONFORMATION
TITLE 2 DERIVED FROM ELECTRON MICROSCOPY
CAVEAT 3J4Q CHAIN B RESIDUES 45-92 AND CHAIN C RESIDUES 45-91 ARE
CAVEAT 2 3J4Q DISORDERED LINKER REGIONS CONNECTING THE STRUCTURED DOMAINS
CAVEAT 3 3J4Q IN THE PSEUDO-ATOMIC MODEL AND ARE NOT DEFINED BY MAP
CAVEAT 4 3J4Q DENSITY.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: A-KINASE ANCHOR PROTEIN 18;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SEE REMARK 999;
COMPND 5 SYNONYM: AKAP18;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE TYPE II-ALPHA REGULATORY
COMPND 9 SUBUNIT;
COMPND 10 CHAIN: B, C;
COMPND 11 SYNONYM: PROTEIN KINASE, CAMP DEPENDENT REGULATORY, TYPE II ALPHA,
COMPND 12 ISOFORM CRA_B, CAMP-DEPENDENT PROTEIN KINASE TYPE II-ALPHA REGULATORY
COMPND 13 CHAIN, CAMP-DEPENDENT PROTEIN KINASE TYPE II-ALPHA REGULATORY
COMPND 14 SUBUNIT;
COMPND 15 ENGINEERED: YES;
COMPND 16 MOL_ID: 3;
COMPND 17 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT ALPHA;
COMPND 18 CHAIN: D, E;
COMPND 19 SYNONYM: PKA C-ALPHA;
COMPND 20 EC: 2.7.11.11;
COMPND 21 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: SF-9;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 11 ORGANISM_COMMON: MOUSE;
SOURCE 12 ORGANISM_TAXID: 10090;
SOURCE 13 GENE: PRKAR2A, MCG_16488;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 16 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;
SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PET15A;
SOURCE 19 MOL_ID: 3;
SOURCE 20 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 21 ORGANISM_COMMON: MOUSE;
SOURCE 22 ORGANISM_TAXID: 10090;
SOURCE 23 GENE: PRKACA, PKACA;
SOURCE 24 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 25 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 26 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;
SOURCE 27 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 28 EXPRESSION_SYSTEM_PLASMID: PET28B
KEYWDS A-KINASE ANCHORING PROTEIN, CAMP-DEPENDENT KINASE, RII, PKA
KEYWDS 2 REGULATORY SUBUNIT II, PHOSPHORYLATION, ANCHORING, INTRINSIC
KEYWDS 3 DISORDER, TRANSFERASE
EXPDTA ELECTRON MICROSCOPY
AUTHOR S.L.REICHOW,T.GONEN
REVDAT 4 21-FEB-24 3J4Q 1 REMARK
REVDAT 3 18-JUL-18 3J4Q 1 REMARK
REVDAT 2 27-NOV-13 3J4Q 1 JRNL
REVDAT 1 13-NOV-13 3J4Q 0
JRNL AUTH F.D.SMITH,S.L.REICHOW,J.L.ESSELTINE,D.SHI,L.K.LANGEBERG,
JRNL AUTH 2 J.D.SCOTT,T.GONEN
JRNL TITL INTRINSIC DISORDER WITHIN AN AKAP-PROTEIN KINASE A COMPLEX
JRNL TITL 2 GUIDES LOCAL SUBSTRATE PHOSPHORYLATION.
JRNL REF ELIFE V. 2 01319 2013
JRNL REFN ESSN 2050-084X
JRNL PMID 24192038
JRNL DOI 10.7554/ELIFE.01319
REMARK 2
REMARK 2 RESOLUTION. 35.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : UCSF CHIMERA, FREALIGN, IMAGIC
REMARK 3 RECONSTRUCTION SCHEMA : NULL
REMARK 3
REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT
REMARK 3 PDB ENTRY : 2IZX
REMARK 3 REFINEMENT SPACE : REAL
REMARK 3 REFINEMENT PROTOCOL : RIGID BODY FIT
REMARK 3 REFINEMENT TARGET : CROSS-CORRELATION
REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL
REMARK 3
REMARK 3 FITTING PROCEDURE : REFINEMENT PROTOCOL--RIGID BODY DETAILS--THIS
REMARK 3 DOMAIN WAS LINKED TO THE AKAP18 CENTRAL DOMAIN (PDB 2VFL) USING
REMARK 3 COOT AND THEY WERE FIT TOGETHER INTO THE EM DENSITY.
REMARK 3
REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS
REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : 4.200
REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 35.00
REMARK 3 NUMBER OF PARTICLES : 1000
REMARK 3 CTF CORRECTION METHOD : NULL
REMARK 3
REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL
REMARK 3
REMARK 3 OTHER DETAILS: (SINGLE PARTICLE DETAILS: IMAGES WERE PROCESSED IN
REMARK 3 IMAGIC AND ISAC. 3D RECONSTRUCTION WAS DONE IN IMAGIC AND
REMARK 3 FREALIGN.) (SINGLE PARTICLE--APPLIED SYMMETRY: C1)
REMARK 4
REMARK 4 3J4Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-OCT-13.
REMARK 100 THE DEPOSITION ID IS D_1000160248.
REMARK 245
REMARK 245 EXPERIMENTAL DETAILS
REMARK 245 RECONSTRUCTION METHOD : SINGLE PARTICLE
REMARK 245 SPECIMEN TYPE : NEGATIVE STAINING
REMARK 245
REMARK 245 ELECTRON MICROSCOPE SAMPLE
REMARK 245 SAMPLE TYPE : PARTICLE
REMARK 245 PARTICLE TYPE : POINT
REMARK 245 NAME OF SAMPLE : AKAP18-PKA COMPLEX IN BENT
REMARK 245 CONFORMATION; A-KINASE
REMARK 245 ANCHORING PROTEIN 18; A-PROTEIN
REMARK 245 KINASE REGULATORY SUBUNIT II
REMARK 245 ALPHA; A-PROTEIN KINASE
REMARK 245 CATALYTIC SUBUNIT
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 0.01
REMARK 245 SAMPLE SUPPORT DETAILS : 200 MESH COPPER GRID WITH THIN
REMARK 245 CARBON SUPPORT
REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL
REMARK 245 SAMPLE BUFFER : 25 MM HEPES, PH 7.4, 200 MM
REMARK 245 NACL, 0.5 MM EDTA, 1 MM DTT
REMARK 245 PH : 7.40
REMARK 245 SAMPLE DETAILS : HETERO-PENTAMER COMPOSED OF ONE
REMARK 245 AKAP18 BOUND TO A DIMER OF THE PKA REGULATORY SUBUNIT II AND TWO
REMARK 245 COPIES OF THE PKA CATALYTIC SUBUNIT
REMARK 245
REMARK 245 DATA ACQUISITION
REMARK 245 DATE OF EXPERIMENT : 01-MAY-12
REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL
REMARK 245 TEMPERATURE (KELVIN) : 298.00
REMARK 245 MICROSCOPE MODEL : FEI TECNAI 12
REMARK 245 DETECTOR TYPE : GENERIC GATAN
REMARK 245 MINIMUM DEFOCUS (NM) : 1000.00
REMARK 245 MAXIMUM DEFOCUS (NM) : 2500.00
REMARK 245 MINIMUM TILT ANGLE (DEGREES) : 0.00
REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : 50.00
REMARK 245 NOMINAL CS : 6.30
REMARK 245 IMAGING MODE : BRIGHT FIELD
REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 1500.00
REMARK 245 ILLUMINATION MODE : FLOOD BEAM
REMARK 245 NOMINAL MAGNIFICATION : 52000
REMARK 245 CALIBRATED MAGNIFICATION : NULL
REMARK 245 SOURCE : LAB6
REMARK 245 ACCELERATION VOLTAGE (KV) : 120
REMARK 245 IMAGING DETAILS : NULL
REMARK 247
REMARK 247 ELECTRON MICROSCOPY
REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON
REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE
REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES
REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION
REMARK 247 OF THE STRUCTURE FACTORS.
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: PENTAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E
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 MET A 1
REMARK 465 GLU A 2
REMARK 465 ARG A 3
REMARK 465 PRO A 4
REMARK 465 ALA A 5
REMARK 465 ALA A 6
REMARK 465 GLY A 7
REMARK 465 GLU A 8
REMARK 465 ILE A 9
REMARK 465 ASP A 10
REMARK 465 ALA A 11
REMARK 465 ASN A 12
REMARK 465 LYS A 13
REMARK 465 CYS A 14
REMARK 465 ASP A 15
REMARK 465 HIS A 16
REMARK 465 LEU A 17
REMARK 465 SER A 18
REMARK 465 ARG A 19
REMARK 465 GLY A 20
REMARK 465 GLU A 21
REMARK 465 GLU A 22
REMARK 465 GLY A 23
REMARK 465 THR A 24
REMARK 465 GLY A 25
REMARK 465 ASP A 26
REMARK 465 LEU A 27
REMARK 465 GLU A 28
REMARK 465 THR A 29
REMARK 465 SER A 30
REMARK 465 PRO A 31
REMARK 465 VAL A 32
REMARK 465 GLY A 33
REMARK 465 SER A 34
REMARK 465 LEU A 35
REMARK 465 ALA A 36
REMARK 465 ASP A 37
REMARK 465 LEU A 38
REMARK 465 PRO A 39
REMARK 465 PHE A 40
REMARK 465 ALA A 41
REMARK 465 ALA A 42
REMARK 465 VAL A 43
REMARK 465 ASP A 44
REMARK 465 ILE A 45
REMARK 465 GLN A 46
REMARK 465 ASP A 47
REMARK 465 ASP A 48
REMARK 465 CYS A 49
REMARK 465 GLY A 50
REMARK 465 LEU A 51
REMARK 465 PRO A 52
REMARK 465 ASP A 53
REMARK 465 VAL A 54
REMARK 465 PRO A 55
REMARK 465 GLN A 56
REMARK 465 GLY A 57
REMARK 465 ASN A 58
REMARK 465 VAL A 59
REMARK 465 PRO A 60
REMARK 465 GLN A 61
REMARK 465 GLY A 62
REMARK 465 ASN A 63
REMARK 465 PRO A 64
REMARK 465 LYS A 65
REMARK 465 ARG A 66
REMARK 465 SER A 67
REMARK 465 LYS A 68
REMARK 465 GLU A 69
REMARK 465 ASN A 70
REMARK 465 ARG A 71
REMARK 465 GLY A 72
REMARK 465 ASP A 73
REMARK 465 ARG A 74
REMARK 465 ASN A 75
REMARK 465 ASP A 76
REMARK 465 HIS A 77
REMARK 465 VAL A 78
REMARK 465 LYS A 79
REMARK 465 LYS A 80
REMARK 465 ARG A 81
REMARK 465 LYS A 82
REMARK 465 LYS A 83
REMARK 465 ALA A 84
REMARK 465 LYS A 85
REMARK 465 LYS A 86
REMARK 465 ASP A 87
REMARK 465 GLN A 318
REMARK 465 GLN A 319
REMARK 465 TYR A 320
REMARK 465 LEU A 321
REMARK 465 GLU A 322
REMARK 465 GLU A 323
REMARK 465 THR A 324
REMARK 465 GLN A 325
REMARK 465 ASN A 326
REMARK 465 LYS A 327
REMARK 465 LYS A 328
REMARK 465 GLN A 329
REMARK 465 PRO A 330
REMARK 465 GLY A 331
REMARK 465 GLU A 332
REMARK 465 GLY A 333
REMARK 465 ASN A 334
REMARK 465 SER A 335
REMARK 465 VAL A 336
REMARK 465 LYS A 337
REMARK 465 ALA A 338
REMARK 465 GLU A 339
REMARK 465 GLU A 340
REMARK 465 GLY A 341
REMARK 465 ASP A 342
REMARK 465 ARG A 343
REMARK 465 ASN A 344
REMARK 465 GLY A 345
REMARK 465 ASP A 346
REMARK 465 GLY A 347
REMARK 465 SER A 348
REMARK 465 ASP A 349
REMARK 465 ASN A 350
REMARK 465 ASN A 351
REMARK 465 ARG A 352
REMARK 465 LYS A 353
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 HIS B 3
REMARK 465 ILE B 4
REMARK 465 GLN B 5
REMARK 465 ILE B 6
REMARK 465 PRO B 7
REMARK 465 ALA B 8
REMARK 465 ASN B 112
REMARK 465 ASP B 113
REMARK 465 PRO B 114
REMARK 465 ARG B 115
REMARK 465 LEU B 395
REMARK 465 ASP B 396
REMARK 465 LEU B 397
REMARK 465 MET B 398
REMARK 465 ASP B 399
REMARK 465 PRO B 400
REMARK 465 GLY B 401
REMARK 465 GLN B 402
REMARK 465 MET C 1
REMARK 465 SER C 2
REMARK 465 HIS C 3
REMARK 465 ILE C 4
REMARK 465 GLN C 5
REMARK 465 ILE C 6
REMARK 465 PRO C 7
REMARK 465 ALA C 8
REMARK 465 ASN C 112
REMARK 465 ASP C 113
REMARK 465 PRO C 114
REMARK 465 ARG C 115
REMARK 465 LEU C 395
REMARK 465 ASP C 396
REMARK 465 LEU C 397
REMARK 465 MET C 398
REMARK 465 ASP C 399
REMARK 465 PRO C 400
REMARK 465 GLY C 401
REMARK 465 GLN C 402
REMARK 465 MET D 0
REMARK 465 GLY D 1
REMARK 465 ASN D 2
REMARK 465 ALA D 3
REMARK 465 ALA D 4
REMARK 465 ALA D 5
REMARK 465 ALA D 6
REMARK 465 LYS D 7
REMARK 465 LYS D 8
REMARK 465 GLY D 9
REMARK 465 SER D 10
REMARK 465 GLU D 11
REMARK 465 GLN D 12
REMARK 465 LYS D 319
REMARK 465 GLY D 320
REMARK 465 PRO D 321
REMARK 465 GLY D 322
REMARK 465 ASP D 323
REMARK 465 THR D 324
REMARK 465 SER D 325
REMARK 465 ASN D 326
REMARK 465 PHE D 327
REMARK 465 ASP D 328
REMARK 465 ASP D 329
REMARK 465 TYR D 330
REMARK 465 GLU D 331
REMARK 465 MET E 0
REMARK 465 GLY E 1
REMARK 465 ASN E 2
REMARK 465 ALA E 3
REMARK 465 ALA E 4
REMARK 465 ALA E 5
REMARK 465 ALA E 6
REMARK 465 LYS E 7
REMARK 465 LYS E 8
REMARK 465 GLY E 9
REMARK 465 SER E 10
REMARK 465 GLU E 11
REMARK 465 GLN E 12
REMARK 465 LYS E 319
REMARK 465 GLY E 320
REMARK 465 PRO E 321
REMARK 465 GLY E 322
REMARK 465 ASP E 323
REMARK 465 THR E 324
REMARK 465 SER E 325
REMARK 465 ASN E 326
REMARK 465 PHE E 327
REMARK 465 ASP E 328
REMARK 465 ASP E 329
REMARK 465 TYR E 330
REMARK 465 GLU E 331
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 SER B 310 OG
REMARK 470 LYS B 311 CG CD CE NZ
REMARK 470 THR B 312 OG1 CG2
REMARK 470 LYS B 313 CG CD CE NZ
REMARK 470 SER B 314 OG
REMARK 470 ASN B 315 CG OD1 ND2
REMARK 470 LYS B 316 CG CD CE NZ
REMARK 470 ASN B 317 CG OD1 ND2
REMARK 470 ASN B 320 CG OD1 ND2
REMARK 470 SER C 310 OG
REMARK 470 LYS C 311 CG CD CE NZ
REMARK 470 THR C 312 OG1 CG2
REMARK 470 LYS C 313 CG CD CE NZ
REMARK 470 SER C 314 OG
REMARK 470 ASN C 315 CG OD1 ND2
REMARK 470 LYS C 316 CG CD CE NZ
REMARK 470 ASN C 317 CG OD1 ND2
REMARK 470 ASN C 320 CG OD1 ND2
REMARK 470 GLN D 42 CG CD OE1 NE2
REMARK 470 PHE D 43 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASP D 44 CG OD1 OD2
REMARK 470 ARG D 45 CG CD NE CZ NH1 NH2
REMARK 470 ILE D 46 CG1 CG2 CD1
REMARK 470 LYS D 47 CG CD CE NZ
REMARK 470 THR D 48 OG1 CG2
REMARK 470 LEU D 49 CG CD1 CD2
REMARK 470 THR D 51 OG1 CG2
REMARK 470 SER D 53 OG
REMARK 470 PHE D 54 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG D 56 CG CD NE CZ NH1 NH2
REMARK 470 VAL D 57 CG1 CG2
REMARK 470 MET D 58 CG SD CE
REMARK 470 VAL D 60 CG1 CG2
REMARK 470 LYS D 61 CG CD CE NZ
REMARK 470 LYS D 63 CG CD CE NZ
REMARK 470 GLU D 64 CG CD OE1 OE2
REMARK 470 SER D 65 OG
REMARK 470 MET D 71 CG SD CE
REMARK 470 LYS D 72 CG CD CE NZ
REMARK 470 ILE D 73 CG1 CG2 CD1
REMARK 470 LEU D 74 CG CD1 CD2
REMARK 470 ASP D 75 CG OD1 OD2
REMARK 470 LYS D 76 CG CD CE NZ
REMARK 470 GLN D 77 CG CD OE1 NE2
REMARK 470 LYS D 78 CG CD CE NZ
REMARK 470 VAL D 79 CG1 CG2
REMARK 470 VAL D 80 CG1 CG2
REMARK 470 LYS D 81 CG CD CE NZ
REMARK 470 LEU D 82 CG CD1 CD2
REMARK 470 LYS D 111 CG CD CE NZ
REMARK 470 ASP D 112 CG OD1 OD2
REMARK 470 ASN D 113 CG OD1 ND2
REMARK 470 SER D 114 OG
REMARK 470 ASN D 115 CG OD1 ND2
REMARK 470 LEU D 116 CG CD1 CD2
REMARK 470 TYR D 117 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 MET D 118 CG SD CE
REMARK 470 VAL D 119 CG1 CG2
REMARK 470 GLU D 332 CG CD OE1 OE2
REMARK 470 GLU D 333 CG CD OE1 OE2
REMARK 470 GLU D 334 CG CD OE1 OE2
REMARK 470 ILE D 335 CG1 CG2 CD1
REMARK 470 ARG D 336 CG CD NE CZ NH1 NH2
REMARK 470 ILE D 339 CG1 CG2 CD1
REMARK 470 LYS D 345 CG CD CE NZ
REMARK 470 GLU D 349 CG CD OE1 OE2
REMARK 470 GLN E 42 CG CD OE1 NE2
REMARK 470 PHE E 43 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASP E 44 CG OD1 OD2
REMARK 470 ARG E 45 CG CD NE CZ NH1 NH2
REMARK 470 ILE E 46 CG1 CG2 CD1
REMARK 470 LYS E 47 CG CD CE NZ
REMARK 470 THR E 48 OG1 CG2
REMARK 470 LEU E 49 CG CD1 CD2
REMARK 470 THR E 51 OG1 CG2
REMARK 470 SER E 53 OG
REMARK 470 PHE E 54 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG E 56 CG CD NE CZ NH1 NH2
REMARK 470 VAL E 57 CG1 CG2
REMARK 470 MET E 58 CG SD CE
REMARK 470 VAL E 60 CG1 CG2
REMARK 470 LYS E 61 CG CD CE NZ
REMARK 470 LYS E 63 CG CD CE NZ
REMARK 470 GLU E 64 CG CD OE1 OE2
REMARK 470 SER E 65 OG
REMARK 470 MET E 71 CG SD CE
REMARK 470 LYS E 72 CG CD CE NZ
REMARK 470 ILE E 73 CG1 CG2 CD1
REMARK 470 LEU E 74 CG CD1 CD2
REMARK 470 ASP E 75 CG OD1 OD2
REMARK 470 LYS E 76 CG CD CE NZ
REMARK 470 GLN E 77 CG CD OE1 NE2
REMARK 470 LYS E 78 CG CD CE NZ
REMARK 470 VAL E 79 CG1 CG2
REMARK 470 VAL E 80 CG1 CG2
REMARK 470 LYS E 81 CG CD CE NZ
REMARK 470 LEU E 82 CG CD1 CD2
REMARK 470 LYS E 111 CG CD CE NZ
REMARK 470 ASP E 112 CG OD1 OD2
REMARK 470 ASN E 113 CG OD1 ND2
REMARK 470 SER E 114 OG
REMARK 470 ASN E 115 CG OD1 ND2
REMARK 470 LEU E 116 CG CD1 CD2
REMARK 470 TYR E 117 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 MET E 118 CG SD CE
REMARK 470 VAL E 119 CG1 CG2
REMARK 470 GLU E 332 CG CD OE1 OE2
REMARK 470 GLU E 333 CG CD OE1 OE2
REMARK 470 GLU E 334 CG CD OE1 OE2
REMARK 470 ILE E 335 CG1 CG2 CD1
REMARK 470 ARG E 336 CG CD NE CZ NH1 NH2
REMARK 470 ILE E 339 CG1 CG2 CD1
REMARK 470 LYS E 345 CG CD CE NZ
REMARK 470 GLU E 349 CG CD OE1 OE2
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 PRO B 89 C - N - CD ANGL. DEV. = 13.0 DEGREES
REMARK 500 LYS B 316 CB - CA - C ANGL. DEV. = -12.7 DEGREES
REMARK 500 LYS B 316 N - CA - C ANGL. DEV. = 20.6 DEGREES
REMARK 500 LYS C 316 CB - CA - C ANGL. DEV. = -12.8 DEGREES
REMARK 500 LYS C 316 N - CA - C ANGL. DEV. = 20.7 DEGREES
REMARK 500 VAL D 80 CB - CA - C ANGL. DEV. = -17.0 DEGREES
REMARK 500 LYS D 81 N - CA - CB ANGL. DEV. = 16.4 DEGREES
REMARK 500 LYS D 81 CA - C - N ANGL. DEV. = -13.5 DEGREES
REMARK 500 ASN D 113 CB - CA - C ANGL. DEV. = -15.1 DEGREES
REMARK 500 SER D 114 CB - CA - C ANGL. DEV. = 15.3 DEGREES
REMARK 500 SER D 114 N - CA - CB ANGL. DEV. = 10.1 DEGREES
REMARK 500 SER D 114 CA - C - O ANGL. DEV. = 18.8 DEGREES
REMARK 500 SER D 114 CA - C - N ANGL. DEV. = -21.6 DEGREES
REMARK 500 ASN D 115 CB - CA - C ANGL. DEV. = -12.5 DEGREES
REMARK 500 ASN D 115 N - CA - C ANGL. DEV. = 23.8 DEGREES
REMARK 500 LEU D 116 CB - CA - C ANGL. DEV. = -12.7 DEGREES
REMARK 500 LEU D 116 CA - C - O ANGL. DEV. = 23.3 DEGREES
REMARK 500 LEU D 116 CA - C - N ANGL. DEV. = -23.7 DEGREES
REMARK 500 VAL E 80 CB - CA - C ANGL. DEV. = -17.1 DEGREES
REMARK 500 LYS E 81 N - CA - CB ANGL. DEV. = 16.4 DEGREES
REMARK 500 LYS E 81 CA - C - N ANGL. DEV. = -13.5 DEGREES
REMARK 500 ASN E 113 CB - CA - C ANGL. DEV. = -15.0 DEGREES
REMARK 500 SER E 114 CB - CA - C ANGL. DEV. = 15.3 DEGREES
REMARK 500 SER E 114 N - CA - CB ANGL. DEV. = 10.1 DEGREES
REMARK 500 SER E 114 CA - C - O ANGL. DEV. = 18.9 DEGREES
REMARK 500 SER E 114 CA - C - N ANGL. DEV. = -21.6 DEGREES
REMARK 500 ASN E 115 CB - CA - C ANGL. DEV. = -12.5 DEGREES
REMARK 500 ASN E 115 N - CA - C ANGL. DEV. = 23.8 DEGREES
REMARK 500 LEU E 116 CB - CA - C ANGL. DEV. = -12.7 DEGREES
REMARK 500 LEU E 116 CA - C - O ANGL. DEV. = 23.2 DEGREES
REMARK 500 LEU E 116 CA - C - N ANGL. DEV. = -23.6 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 LYS A 238 -17.74 -48.63
REMARK 500 TYR A 263 -71.93 -148.04
REMARK 500 LEU A 301 5.88 80.49
REMARK 500 GLU B 109 102.41 164.92
REMARK 500 GLU B 110 110.07 -12.94
REMARK 500 LYS B 139 -49.70 -28.68
REMARK 500 ASP B 161 -4.60 83.60
REMARK 500 ASP B 189 -138.82 63.38
REMARK 500 ASP B 282 132.22 -35.72
REMARK 500 SER B 301 143.26 -174.60
REMARK 500 SER B 310 77.04 -55.42
REMARK 500 LYS B 311 -43.74 -130.08
REMARK 500 THR B 312 50.54 -69.58
REMARK 500 SER B 314 -86.00 157.53
REMARK 500 ASN B 315 81.92 -176.62
REMARK 500 LYS B 316 74.25 69.45
REMARK 500 ASN B 317 179.05 135.12
REMARK 500 GLN B 321 -123.80 -157.92
REMARK 500 ASN B 342 56.06 -141.85
REMARK 500 SER B 393 -79.72 -46.41
REMARK 500 GLU C 109 102.37 164.94
REMARK 500 GLU C 110 110.04 -12.87
REMARK 500 LYS C 139 -49.65 -28.78
REMARK 500 ASP C 161 -4.49 83.59
REMARK 500 ASP C 189 -138.77 63.31
REMARK 500 ASP C 282 132.26 -35.67
REMARK 500 SER C 301 143.26 -174.60
REMARK 500 SER C 310 77.03 -55.38
REMARK 500 LYS C 311 -43.77 -130.13
REMARK 500 THR C 312 50.62 -69.60
REMARK 500 SER C 314 -85.92 157.56
REMARK 500 ASN C 315 81.91 -176.63
REMARK 500 LYS C 316 74.22 69.35
REMARK 500 ASN C 317 179.16 135.21
REMARK 500 GLN C 321 -123.82 -157.88
REMARK 500 ASN C 342 56.03 -141.85
REMARK 500 SER C 393 -79.66 -46.35
REMARK 500 THR D 32 62.35 -164.55
REMARK 500 ASN D 36 85.69 11.31
REMARK 500 THR D 37 -75.11 -84.71
REMARK 500 ASP D 44 -111.60 -86.72
REMARK 500 ARG D 45 138.97 172.45
REMARK 500 ILE D 46 -118.91 -126.54
REMARK 500 LYS D 47 -169.65 -67.39
REMARK 500 THR D 48 61.15 -150.30
REMARK 500 THR D 51 -109.70 -99.04
REMARK 500 SER D 53 11.89 -161.90
REMARK 500 LYS D 63 -97.18 -77.95
REMARK 500 VAL D 79 -159.74 -61.91
REMARK 500 VAL D 80 -28.14 71.65
REMARK 500
REMARK 500 THIS ENTRY HAS 101 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-5755 RELATED DB: EMDB
REMARK 900 35 ANGSTROM MAP OF THE AKAP18-PKA COMPLEX IN A BENT CONFORMATION
REMARK 900 RELATED ID: EMD-5756 RELATED DB: EMDB
REMARK 900 35 ANGSTROM MAP OF THE AKAP18-PKA COMPLEX IN A LINEAR CONFORMATION
REMARK 900 RELATED ID: 3J4R RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 AKAP18 IN THIS ENTRY IS FROM HOMO SAPIENS, BUT THE MODELED SEQUENCE
REMARK 999 IS FROM RATTUS NORVEGICUS (UNP Q6JP77).
DBREF 3J4Q B 1 402 UNP Q8K1M3 Q8K1M3_MOUSE 1 402
DBREF 3J4Q C 1 402 UNP Q8K1M3 Q8K1M3_MOUSE 1 402
DBREF 3J4Q D 0 350 UNP P05132 KAPCA_MOUSE 1 351
DBREF 3J4Q E 0 350 UNP P05132 KAPCA_MOUSE 1 351
DBREF 3J4Q A 1 353 PDB 3J4Q 3J4Q 1 353
SEQRES 1 A 353 MET GLU ARG PRO ALA ALA GLY GLU ILE ASP ALA ASN LYS
SEQRES 2 A 353 CYS ASP HIS LEU SER ARG GLY GLU GLU GLY THR GLY ASP
SEQRES 3 A 353 LEU GLU THR SER PRO VAL GLY SER LEU ALA ASP LEU PRO
SEQRES 4 A 353 PHE ALA ALA VAL ASP ILE GLN ASP ASP CYS GLY LEU PRO
SEQRES 5 A 353 ASP VAL PRO GLN GLY ASN VAL PRO GLN GLY ASN PRO LYS
SEQRES 6 A 353 ARG SER LYS GLU ASN ARG GLY ASP ARG ASN ASP HIS VAL
SEQRES 7 A 353 LYS LYS ARG LYS LYS ALA LYS LYS ASP TYR GLN PRO ASN
SEQRES 8 A 353 TYR PHE LEU SER ILE PRO ILE THR ASN LYS LYS ILE THR
SEQRES 9 A 353 ALA GLY ILE LYS VAL LEU GLN ASN SER ILE LEU ARG GLN
SEQRES 10 A 353 ASP ASN ARG LEU THR LYS ALA MET VAL GLY ASP GLY SER
SEQRES 11 A 353 PHE HIS ILE THR LEU LEU VAL MET GLN LEU LEU ASN GLU
SEQRES 12 A 353 ASP GLU VAL ASN ILE GLY THR ASP ALA LEU LEU GLU LEU
SEQRES 13 A 353 LYS PRO PHE VAL GLU GLU ILE LEU GLU GLY LYS HIS LEU
SEQRES 14 A 353 THR LEU PRO PHE HIS GLY ILE GLY THR PHE GLN GLY GLN
SEQRES 15 A 353 VAL GLY PHE VAL LYS LEU ALA ASP GLY ASP HIS VAL SER
SEQRES 16 A 353 ALA LEU LEU GLU ILE ALA GLU THR ALA LYS ARG THR PHE
SEQRES 17 A 353 GLN GLU LYS GLY ILE LEU ALA GLY GLU SER ARG THR PHE
SEQRES 18 A 353 LYS PRO HIS LEU THR PHE MET LYS LEU SER LYS ALA PRO
SEQRES 19 A 353 MET LEU TRP LYS LYS GLY VAL ARG LYS ILE GLU PRO GLY
SEQRES 20 A 353 LEU TYR GLU GLN PHE ILE ASP HIS ARG PHE GLY GLU GLU
SEQRES 21 A 353 ILE LEU TYR GLN ILE ASP LEU CYS SER MET LEU LYS LYS
SEQRES 22 A 353 LYS GLN SER ASN GLY TYR TYR HIS CYS GLU SER SER ILE
SEQRES 23 A 353 VAL ILE GLY GLU LYS ASP ARG LYS GLU PRO GLU ASP ALA
SEQRES 24 A 353 GLU LEU VAL ARG LEU SER LYS ARG LEU VAL GLU ASN ALA
SEQRES 25 A 353 VAL LEU LYS ALA VAL GLN GLN TYR LEU GLU GLU THR GLN
SEQRES 26 A 353 ASN LYS LYS GLN PRO GLY GLU GLY ASN SER VAL LYS ALA
SEQRES 27 A 353 GLU GLU GLY ASP ARG ASN GLY ASP GLY SER ASP ASN ASN
SEQRES 28 A 353 ARG LYS
SEQRES 1 B 402 MET SER HIS ILE GLN ILE PRO ALA GLY LEU THR GLU LEU
SEQRES 2 B 402 LEU GLN GLY TYR THR VAL GLU VAL LEU ARG GLN GLN PRO
SEQRES 3 B 402 PRO ASP LEU VAL ASP PHE ALA VAL GLU TYR PHE THR ARG
SEQRES 4 B 402 LEU ARG GLU ALA ARG ARG GLN GLU SER ASP THR PHE ILE
SEQRES 5 B 402 VAL SER PRO THR THR PHE HIS THR GLN GLU SER SER ALA
SEQRES 6 B 402 VAL PRO VAL ILE GLU GLU ASP GLY GLU SER ASP SER ASP
SEQRES 7 B 402 SER GLU ASP ALA ASP LEU GLU VAL PRO VAL PRO SER LYS
SEQRES 8 B 402 PHE THR ARG ARG VAL SER VAL CYS ALA GLU THR PHE ASN
SEQRES 9 B 402 PRO ASP GLU GLU GLU GLU ASP ASN ASP PRO ARG VAL VAL
SEQRES 10 B 402 HIS PRO LYS THR ASP GLU GLN ARG CYS ARG LEU GLN GLU
SEQRES 11 B 402 ALA CYS LYS ASP ILE LEU LEU PHE LYS ASN LEU ASP GLN
SEQRES 12 B 402 GLU GLN LEU SER GLN VAL LEU ASP ALA MET PHE GLU LYS
SEQRES 13 B 402 ILE VAL LYS THR ASP GLU HIS VAL ILE ASP GLN GLY ASP
SEQRES 14 B 402 ASP GLY ASP ASN PHE TYR VAL ILE GLU ARG GLY THR TYR
SEQRES 15 B 402 ASP ILE LEU VAL THR LYS ASP ASN GLN THR ARG SER VAL
SEQRES 16 B 402 GLY GLN TYR ASP ASN ARG GLY SER PHE GLY GLU LEU ALA
SEQRES 17 B 402 LEU MET TYR ASN THR PRO ARG ALA ALA THR ILE ILE ALA
SEQRES 18 B 402 THR SER GLU GLY SER LEU TRP GLY LEU ASP ARG VAL THR
SEQRES 19 B 402 PHE ARG ARG ILE ILE VAL LYS ASN ASN ALA LYS LYS ARG
SEQRES 20 B 402 LYS MET PHE GLU SER PHE ILE GLU SER VAL PRO LEU PHE
SEQRES 21 B 402 LYS SER LEU GLU MET SER GLU ARG MET LYS ILE VAL ASP
SEQRES 22 B 402 VAL ILE GLY GLU LYS ILE TYR LYS ASP GLY GLU ARG ILE
SEQRES 23 B 402 ILE ALA GLN GLY GLU LYS ALA ASP SER PHE TYR ILE ILE
SEQRES 24 B 402 GLU SER GLY GLU VAL SER ILE LEU ILE ARG SER LYS THR
SEQRES 25 B 402 LYS SER ASN LYS ASN GLY GLY ASN GLN GLU VAL GLU ILE
SEQRES 26 B 402 ALA HIS CYS HIS LYS GLY GLN TYR PHE GLY GLU LEU ALA
SEQRES 27 B 402 LEU VAL THR ASN LYS PRO ARG ALA ALA SER ALA TYR ALA
SEQRES 28 B 402 VAL GLY ASP VAL LYS CYS LEU VAL MET ASP VAL GLN ALA
SEQRES 29 B 402 PHE GLU ARG LEU LEU GLY PRO CYS MET ASP ILE MET LYS
SEQRES 30 B 402 ARG ASN ILE SER HIS TYR GLU GLU GLN LEU VAL LYS MET
SEQRES 31 B 402 PHE GLY SER ASN LEU ASP LEU MET ASP PRO GLY GLN
SEQRES 1 C 402 MET SER HIS ILE GLN ILE PRO ALA GLY LEU THR GLU LEU
SEQRES 2 C 402 LEU GLN GLY TYR THR VAL GLU VAL LEU ARG GLN GLN PRO
SEQRES 3 C 402 PRO ASP LEU VAL ASP PHE ALA VAL GLU TYR PHE THR ARG
SEQRES 4 C 402 LEU ARG GLU ALA ARG ARG GLN GLU SER ASP THR PHE ILE
SEQRES 5 C 402 VAL SER PRO THR THR PHE HIS THR GLN GLU SER SER ALA
SEQRES 6 C 402 VAL PRO VAL ILE GLU GLU ASP GLY GLU SER ASP SER ASP
SEQRES 7 C 402 SER GLU ASP ALA ASP LEU GLU VAL PRO VAL PRO SER LYS
SEQRES 8 C 402 PHE THR ARG ARG VAL SER VAL CYS ALA GLU THR PHE ASN
SEQRES 9 C 402 PRO ASP GLU GLU GLU GLU ASP ASN ASP PRO ARG VAL VAL
SEQRES 10 C 402 HIS PRO LYS THR ASP GLU GLN ARG CYS ARG LEU GLN GLU
SEQRES 11 C 402 ALA CYS LYS ASP ILE LEU LEU PHE LYS ASN LEU ASP GLN
SEQRES 12 C 402 GLU GLN LEU SER GLN VAL LEU ASP ALA MET PHE GLU LYS
SEQRES 13 C 402 ILE VAL LYS THR ASP GLU HIS VAL ILE ASP GLN GLY ASP
SEQRES 14 C 402 ASP GLY ASP ASN PHE TYR VAL ILE GLU ARG GLY THR TYR
SEQRES 15 C 402 ASP ILE LEU VAL THR LYS ASP ASN GLN THR ARG SER VAL
SEQRES 16 C 402 GLY GLN TYR ASP ASN ARG GLY SER PHE GLY GLU LEU ALA
SEQRES 17 C 402 LEU MET TYR ASN THR PRO ARG ALA ALA THR ILE ILE ALA
SEQRES 18 C 402 THR SER GLU GLY SER LEU TRP GLY LEU ASP ARG VAL THR
SEQRES 19 C 402 PHE ARG ARG ILE ILE VAL LYS ASN ASN ALA LYS LYS ARG
SEQRES 20 C 402 LYS MET PHE GLU SER PHE ILE GLU SER VAL PRO LEU PHE
SEQRES 21 C 402 LYS SER LEU GLU MET SER GLU ARG MET LYS ILE VAL ASP
SEQRES 22 C 402 VAL ILE GLY GLU LYS ILE TYR LYS ASP GLY GLU ARG ILE
SEQRES 23 C 402 ILE ALA GLN GLY GLU LYS ALA ASP SER PHE TYR ILE ILE
SEQRES 24 C 402 GLU SER GLY GLU VAL SER ILE LEU ILE ARG SER LYS THR
SEQRES 25 C 402 LYS SER ASN LYS ASN GLY GLY ASN GLN GLU VAL GLU ILE
SEQRES 26 C 402 ALA HIS CYS HIS LYS GLY GLN TYR PHE GLY GLU LEU ALA
SEQRES 27 C 402 LEU VAL THR ASN LYS PRO ARG ALA ALA SER ALA TYR ALA
SEQRES 28 C 402 VAL GLY ASP VAL LYS CYS LEU VAL MET ASP VAL GLN ALA
SEQRES 29 C 402 PHE GLU ARG LEU LEU GLY PRO CYS MET ASP ILE MET LYS
SEQRES 30 C 402 ARG ASN ILE SER HIS TYR GLU GLU GLN LEU VAL LYS MET
SEQRES 31 C 402 PHE GLY SER ASN LEU ASP LEU MET ASP PRO GLY GLN
SEQRES 1 D 351 MET GLY ASN ALA ALA ALA ALA LYS LYS GLY SER GLU GLN
SEQRES 2 D 351 GLU SER VAL LYS GLU PHE LEU ALA LYS ALA LYS GLU ASP
SEQRES 3 D 351 PHE LEU LYS LYS TRP GLU THR PRO SER GLN ASN THR ALA
SEQRES 4 D 351 GLN LEU ASP GLN PHE ASP ARG ILE LYS THR LEU GLY THR
SEQRES 5 D 351 GLY SER PHE GLY ARG VAL MET LEU VAL LYS HIS LYS GLU
SEQRES 6 D 351 SER GLY ASN HIS TYR ALA MET LYS ILE LEU ASP LYS GLN
SEQRES 7 D 351 LYS VAL VAL LYS LEU LYS GLN ILE GLU HIS THR LEU ASN
SEQRES 8 D 351 GLU LYS ARG ILE LEU GLN ALA VAL ASN PHE PRO PHE LEU
SEQRES 9 D 351 VAL LYS LEU GLU PHE SER PHE LYS ASP ASN SER ASN LEU
SEQRES 10 D 351 TYR MET VAL MET GLU TYR VAL ALA GLY GLY GLU MET PHE
SEQRES 11 D 351 SER HIS LEU ARG ARG ILE GLY ARG PHE SER GLU PRO HIS
SEQRES 12 D 351 ALA ARG PHE TYR ALA ALA GLN ILE VAL LEU THR PHE GLU
SEQRES 13 D 351 TYR LEU HIS SER LEU ASP LEU ILE TYR ARG ASP LEU LYS
SEQRES 14 D 351 PRO GLU ASN LEU LEU ILE ASP GLN GLN GLY TYR ILE GLN
SEQRES 15 D 351 VAL THR ASP PHE GLY PHE ALA LYS ARG VAL LYS GLY ARG
SEQRES 16 D 351 THR TRP THR LEU CYS GLY THR PRO GLU TYR LEU ALA PRO
SEQRES 17 D 351 GLU ILE ILE LEU SER LYS GLY TYR ASN LYS ALA VAL ASP
SEQRES 18 D 351 TRP TRP ALA LEU GLY VAL LEU ILE TYR GLU MET ALA ALA
SEQRES 19 D 351 GLY TYR PRO PRO PHE PHE ALA ASP GLN PRO ILE GLN ILE
SEQRES 20 D 351 TYR GLU LYS ILE VAL SER GLY LYS VAL ARG PHE PRO SER
SEQRES 21 D 351 HIS PHE SER SER ASP LEU LYS ASP LEU LEU ARG ASN LEU
SEQRES 22 D 351 LEU GLN VAL ASP LEU THR LYS ARG PHE GLY ASN LEU LYS
SEQRES 23 D 351 ASN GLY VAL ASN ASP ILE LYS ASN HIS LYS TRP PHE ALA
SEQRES 24 D 351 THR THR ASP TRP ILE ALA ILE TYR GLN ARG LYS VAL GLU
SEQRES 25 D 351 ALA PRO PHE ILE PRO LYS PHE LYS GLY PRO GLY ASP THR
SEQRES 26 D 351 SER ASN PHE ASP ASP TYR GLU GLU GLU GLU ILE ARG VAL
SEQRES 27 D 351 SER ILE ASN GLU LYS CYS GLY LYS GLU PHE THR GLU PHE
SEQRES 1 E 351 MET GLY ASN ALA ALA ALA ALA LYS LYS GLY SER GLU GLN
SEQRES 2 E 351 GLU SER VAL LYS GLU PHE LEU ALA LYS ALA LYS GLU ASP
SEQRES 3 E 351 PHE LEU LYS LYS TRP GLU THR PRO SER GLN ASN THR ALA
SEQRES 4 E 351 GLN LEU ASP GLN PHE ASP ARG ILE LYS THR LEU GLY THR
SEQRES 5 E 351 GLY SER PHE GLY ARG VAL MET LEU VAL LYS HIS LYS GLU
SEQRES 6 E 351 SER GLY ASN HIS TYR ALA MET LYS ILE LEU ASP LYS GLN
SEQRES 7 E 351 LYS VAL VAL LYS LEU LYS GLN ILE GLU HIS THR LEU ASN
SEQRES 8 E 351 GLU LYS ARG ILE LEU GLN ALA VAL ASN PHE PRO PHE LEU
SEQRES 9 E 351 VAL LYS LEU GLU PHE SER PHE LYS ASP ASN SER ASN LEU
SEQRES 10 E 351 TYR MET VAL MET GLU TYR VAL ALA GLY GLY GLU MET PHE
SEQRES 11 E 351 SER HIS LEU ARG ARG ILE GLY ARG PHE SER GLU PRO HIS
SEQRES 12 E 351 ALA ARG PHE TYR ALA ALA GLN ILE VAL LEU THR PHE GLU
SEQRES 13 E 351 TYR LEU HIS SER LEU ASP LEU ILE TYR ARG ASP LEU LYS
SEQRES 14 E 351 PRO GLU ASN LEU LEU ILE ASP GLN GLN GLY TYR ILE GLN
SEQRES 15 E 351 VAL THR ASP PHE GLY PHE ALA LYS ARG VAL LYS GLY ARG
SEQRES 16 E 351 THR TRP THR LEU CYS GLY THR PRO GLU TYR LEU ALA PRO
SEQRES 17 E 351 GLU ILE ILE LEU SER LYS GLY TYR ASN LYS ALA VAL ASP
SEQRES 18 E 351 TRP TRP ALA LEU GLY VAL LEU ILE TYR GLU MET ALA ALA
SEQRES 19 E 351 GLY TYR PRO PRO PHE PHE ALA ASP GLN PRO ILE GLN ILE
SEQRES 20 E 351 TYR GLU LYS ILE VAL SER GLY LYS VAL ARG PHE PRO SER
SEQRES 21 E 351 HIS PHE SER SER ASP LEU LYS ASP LEU LEU ARG ASN LEU
SEQRES 22 E 351 LEU GLN VAL ASP LEU THR LYS ARG PHE GLY ASN LEU LYS
SEQRES 23 E 351 ASN GLY VAL ASN ASP ILE LYS ASN HIS LYS TRP PHE ALA
SEQRES 24 E 351 THR THR ASP TRP ILE ALA ILE TYR GLN ARG LYS VAL GLU
SEQRES 25 E 351 ALA PRO PHE ILE PRO LYS PHE LYS GLY PRO GLY ASP THR
SEQRES 26 E 351 SER ASN PHE ASP ASP TYR GLU GLU GLU GLU ILE ARG VAL
SEQRES 27 E 351 SER ILE ASN GLU LYS CYS GLY LYS GLU PHE THR GLU PHE
HELIX 1 1 ASN A 100 ASP A 118 1 19
HELIX 2 2 ASN A 119 MET A 125 5 7
HELIX 3 3 ASN A 142 GLU A 165 1 24
HELIX 4 4 GLY A 191 GLU A 210 1 20
HELIX 5 5 SER A 231 ALA A 233 5 3
HELIX 6 6 PRO A 234 LYS A 239 1 6
HELIX 7 7 GLU A 245 ILE A 253 5 9
HELIX 8 8 ARG A 303 VAL A 317 1 15
HELIX 9 9 LEU B 10 GLN B 25 1 16
HELIX 10 10 ASP B 28 ARG B 44 1 17
HELIX 11 11 THR B 121 LYS B 133 1 13
HELIX 12 12 ILE B 135 ASN B 140 1 6
HELIX 13 13 ASP B 142 MET B 153 1 12
HELIX 14 14 GLY B 205 MET B 210 5 6
HELIX 15 15 ARG B 232 SER B 256 1 25
HELIX 16 16 VAL B 257 LYS B 261 5 5
HELIX 17 17 GLU B 264 ILE B 275 1 12
HELIX 18 18 GLY B 335 VAL B 340 5 6
HELIX 19 19 VAL B 362 GLY B 370 1 9
HELIX 20 20 PRO B 371 ASN B 379 1 9
HELIX 21 21 HIS B 382 GLY B 392 1 11
HELIX 22 22 LEU C 10 GLN C 25 1 16
HELIX 23 23 ASP C 28 ARG C 44 1 17
HELIX 24 24 THR C 121 LYS C 133 1 13
HELIX 25 25 ILE C 135 ASN C 140 1 6
HELIX 26 26 ASP C 142 MET C 153 1 12
HELIX 27 27 GLY C 205 MET C 210 5 6
HELIX 28 28 ARG C 232 SER C 256 1 25
HELIX 29 29 VAL C 257 LYS C 261 5 5
HELIX 30 30 GLU C 264 ILE C 275 1 12
HELIX 31 31 GLY C 335 VAL C 340 5 6
HELIX 32 32 VAL C 362 GLY C 370 1 9
HELIX 33 33 PRO C 371 ASN C 379 1 9
HELIX 34 34 HIS C 382 GLY C 392 1 11
HELIX 35 35 SER D 14 GLU D 31 1 18
HELIX 36 36 GLN D 39 PHE D 43 5 5
HELIX 37 37 ILE D 85 VAL D 98 1 14
HELIX 38 38 MET D 128 GLY D 136 1 9
HELIX 39 39 SER D 139 LEU D 160 1 22
HELIX 40 40 LYS D 168 GLU D 170 5 3
HELIX 41 41 THR D 201 LEU D 205 5 5
HELIX 42 42 ALA D 206 LEU D 211 1 6
HELIX 43 43 LYS D 217 GLY D 234 1 18
HELIX 44 44 GLN D 242 GLY D 253 1 12
HELIX 45 45 SER D 262 LEU D 273 1 12
HELIX 46 46 VAL D 288 ASN D 293 1 6
HELIX 47 47 HIS D 294 ALA D 298 5 5
HELIX 48 48 ASP D 301 GLN D 307 1 7
HELIX 49 49 LYS D 342 GLU D 346 5 5
HELIX 50 50 SER E 14 GLU E 31 1 18
HELIX 51 51 GLN E 39 PHE E 43 5 5
HELIX 52 52 ILE E 85 VAL E 98 1 14
HELIX 53 53 MET E 128 GLY E 136 1 9
HELIX 54 54 SER E 139 LEU E 160 1 22
HELIX 55 55 LYS E 168 GLU E 170 5 3
HELIX 56 56 THR E 201 LEU E 205 5 5
HELIX 57 57 ALA E 206 LEU E 211 1 6
HELIX 58 58 LYS E 217 GLY E 234 1 18
HELIX 59 59 GLN E 242 GLY E 253 1 12
HELIX 60 60 SER E 262 LEU E 273 1 12
HELIX 61 61 VAL E 288 ASN E 293 1 6
HELIX 62 62 HIS E 294 ALA E 298 5 5
HELIX 63 63 ASP E 301 GLN E 307 1 7
HELIX 64 64 LYS E 342 GLU E 346 5 5
SHEET 1 A 4 HIS A 132 MET A 138 0
SHEET 2 A 4 TYR A 92 PRO A 97 -1 N LEU A 94 O LEU A 135
SHEET 3 A 4 GLN A 264 SER A 269 -1 O CYS A 268 N PHE A 93
SHEET 4 A 4 HIS A 281 VAL A 287 -1 O SER A 284 N LEU A 267
SHEET 1 B 4 HIS A 224 LYS A 229 0
SHEET 2 B 4 VAL A 183 LEU A 188 -1 N GLY A 184 O PHE A 227
SHEET 3 B 4 THR A 170 PHE A 179 -1 N GLY A 177 O PHE A 185
SHEET 4 B 4 ARG A 256 ILE A 261 -1 O GLU A 260 N LEU A 171
SHEET 1 C 2 VAL B 98 CYS B 99 0
SHEET 2 C 2 CYS D 199 GLY D 200 -1 O GLY D 200 N VAL B 98
SHEET 1 D 4 PHE B 154 VAL B 158 0
SHEET 2 D 4 GLY B 225 ASP B 231 -1 O GLY B 229 N PHE B 154
SHEET 3 D 4 ASN B 173 ARG B 179 -1 N VAL B 176 O TRP B 228
SHEET 4 D 4 SER B 203 PHE B 204 -1 O PHE B 204 N TYR B 175
SHEET 1 E 4 HIS B 163 ILE B 165 0
SHEET 2 E 4 THR B 218 ALA B 221 -1 O ILE B 219 N VAL B 164
SHEET 3 E 4 THR B 181 LYS B 188 -1 N LEU B 185 O THR B 218
SHEET 4 E 4 GLN B 191 ASP B 199 -1 O GLY B 196 N ILE B 184
SHEET 1 F 4 GLY B 276 TYR B 280 0
SHEET 2 F 4 SER B 348 ASP B 361 -1 O VAL B 355 N TYR B 280
SHEET 3 F 4 SER B 295 ILE B 308 -1 N GLU B 303 O VAL B 352
SHEET 4 F 4 VAL B 323 HIS B 329 -1 O VAL B 323 N ILE B 308
SHEET 1 G 4 ARG B 285 ILE B 287 0
SHEET 2 G 4 SER B 348 ASP B 361 -1 O ALA B 349 N ILE B 286
SHEET 3 G 4 SER B 295 ILE B 308 -1 N GLU B 303 O VAL B 352
SHEET 4 G 4 TYR B 333 PHE B 334 -1 O PHE B 334 N TYR B 297
SHEET 1 H 2 VAL C 98 CYS C 99 0
SHEET 2 H 2 CYS E 199 GLY E 200 -1 O GLY E 200 N VAL C 98
SHEET 1 I 4 PHE C 154 VAL C 158 0
SHEET 2 I 4 GLY C 225 ASP C 231 -1 O GLY C 229 N PHE C 154
SHEET 3 I 4 ASN C 173 ARG C 179 -1 N VAL C 176 O TRP C 228
SHEET 4 I 4 SER C 203 PHE C 204 -1 O PHE C 204 N TYR C 175
SHEET 1 J 4 HIS C 163 ILE C 165 0
SHEET 2 J 4 THR C 218 ALA C 221 -1 O ILE C 219 N VAL C 164
SHEET 3 J 4 THR C 181 LYS C 188 -1 N LEU C 185 O THR C 218
SHEET 4 J 4 GLN C 191 ASP C 199 -1 O GLY C 196 N ILE C 184
SHEET 1 K 4 GLY C 276 TYR C 280 0
SHEET 2 K 4 SER C 348 ASP C 361 -1 O VAL C 355 N TYR C 280
SHEET 3 K 4 SER C 295 ILE C 308 -1 N GLU C 303 O VAL C 352
SHEET 4 K 4 VAL C 323 HIS C 329 -1 O VAL C 323 N ILE C 308
SHEET 1 L 4 ARG C 285 ILE C 287 0
SHEET 2 L 4 SER C 348 ASP C 361 -1 O ALA C 349 N ILE C 286
SHEET 3 L 4 SER C 295 ILE C 308 -1 N GLU C 303 O VAL C 352
SHEET 4 L 4 TYR C 333 PHE C 334 -1 O PHE C 334 N TYR C 297
SHEET 1 M 4 ARG D 56 LYS D 61 0
SHEET 2 M 4 HIS D 68 ILE D 73 -1 O TYR D 69 N VAL D 60
SHEET 3 M 4 TYR D 117 GLU D 121 -1 O MET D 120 N ALA D 70
SHEET 4 M 4 LEU D 106 PHE D 110 -1 N PHE D 108 O VAL D 119
SHEET 1 N 3 GLY D 126 GLU D 127 0
SHEET 2 N 3 LEU D 172 ILE D 174 -1 O ILE D 174 N GLY D 126
SHEET 3 N 3 ILE D 180 VAL D 182 -1 O GLN D 181 N LEU D 173
SHEET 1 O 2 LEU D 162 ILE D 163 0
SHEET 2 O 2 LYS D 189 ARG D 190 -1 O LYS D 189 N ILE D 163
SHEET 1 P 4 ARG E 56 LYS E 61 0
SHEET 2 P 4 HIS E 68 ILE E 73 -1 O TYR E 69 N VAL E 60
SHEET 3 P 4 TYR E 117 GLU E 121 -1 O MET E 120 N ALA E 70
SHEET 4 P 4 LEU E 106 PHE E 110 -1 N PHE E 108 O VAL E 119
SHEET 1 Q 3 GLY E 126 GLU E 127 0
SHEET 2 Q 3 LEU E 172 ILE E 174 -1 O ILE E 174 N GLY E 126
SHEET 3 Q 3 ILE E 180 VAL E 182 -1 O GLN E 181 N LEU E 173
SHEET 1 R 2 LEU E 162 ILE E 163 0
SHEET 2 R 2 LYS E 189 ARG E 190 -1 O LYS E 189 N ILE E 163
CISPEP 1 GLU A 290 LYS A 291 0 13.04
CISPEP 2 LYS A 291 ASP A 292 0 -7.09
CISPEP 3 ALA A 299 GLU A 300 0 0.05
CISPEP 4 ARG B 45 GLN B 46 0 -4.45
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
(ATOM LINES ARE NOT SHOWN.)
END
