HEADER TRANSFERASE 06-FEB-17 5N1M
TITLE CAMP-DEPENDENT PROTEIN KINASE A FROM CRICETULUS GRISEUS IN COMPLEX
TITLE 2 WITH FRAGMENT LIKE MOLECULE (5-CHLORO-2-METHOXYPHENYL)METHANAMINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT ALPHA;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PKA C-ALPHA;
COMPND 5 EC: 2.7.11.11;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: PHOSPHORYLATION OF S11, S140, T198 AND S339;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE INHIBITOR ALPHA-LIKE PROTEIN;
COMPND 10 CHAIN: B;
COMPND 11 ENGINEERED: YES;
COMPND 12 OTHER_DETAILS: CAMP DEPENDENT PROTEIN KINASE INHIBITOR PEPTIDE
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CRICETULUS GRISEUS;
SOURCE 3 ORGANISM_COMMON: CHINESE HAMSTER;
SOURCE 4 ORGANISM_TAXID: 10029;
SOURCE 5 GENE: PRKACA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET-16BTEV;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 ORGANISM_SCIENTIFIC: CRICETULUS GRISEUS;
SOURCE 14 ORGANISM_COMMON: CHINESE HAMSTER;
SOURCE 15 ORGANISM_TAXID: 10029
KEYWDS FRAGMENT, COMPLEX, TRANSFERASE, SERINE THREONINE KINASE, CAMP,
KEYWDS 2 KINASE, PKA
EXPDTA X-RAY DIFFRACTION
AUTHOR C.SIEFKER,A.HEINE,G.KLEBE
REVDAT 2 17-JAN-24 5N1M 1 REMARK
REVDAT 1 28-FEB-18 5N1M 0
JRNL AUTH C.SIEFKER,A.HEINE,G.KLEBE
JRNL TITL A CRYSTALLOGRAPHIC FRAGMENT STUDY WITH CAMP-DEPENDENT
JRNL TITL 2 PROTEIN KINASE A
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.44 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10.1_2155: ???)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.44
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.50
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.380
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 84434
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.153
REMARK 3 R VALUE (WORKING SET) : 0.152
REMARK 3 FREE R VALUE : 0.170
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4222
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 45.5243 - 4.4597 0.99 2891 153 0.1768 0.1848
REMARK 3 2 4.4597 - 3.5402 1.00 2780 146 0.1500 0.1596
REMARK 3 3 3.5402 - 3.0928 1.00 2741 144 0.1633 0.1892
REMARK 3 4 3.0928 - 2.8101 1.00 2718 144 0.1595 0.1695
REMARK 3 5 2.8101 - 2.6087 1.00 2733 143 0.1571 0.1719
REMARK 3 6 2.6087 - 2.4549 1.00 2697 142 0.1492 0.1660
REMARK 3 7 2.4549 - 2.3320 1.00 2693 142 0.1411 0.1794
REMARK 3 8 2.3320 - 2.2305 1.00 2720 143 0.1373 0.1506
REMARK 3 9 2.2305 - 2.1446 1.00 2682 141 0.1399 0.1480
REMARK 3 10 2.1446 - 2.0706 1.00 2678 141 0.1428 0.1481
REMARK 3 11 2.0706 - 2.0059 1.00 2709 143 0.1445 0.1625
REMARK 3 12 2.0059 - 1.9485 1.00 2665 140 0.1384 0.1394
REMARK 3 13 1.9485 - 1.8972 1.00 2692 142 0.1435 0.1727
REMARK 3 14 1.8972 - 1.8509 1.00 2684 141 0.1339 0.1793
REMARK 3 15 1.8509 - 1.8089 1.00 2668 141 0.1311 0.1448
REMARK 3 16 1.8089 - 1.7704 1.00 2650 139 0.1266 0.1471
REMARK 3 17 1.7704 - 1.7349 1.00 2689 141 0.1217 0.1408
REMARK 3 18 1.7349 - 1.7022 1.00 2659 140 0.1244 0.1784
REMARK 3 19 1.7022 - 1.6718 1.00 2665 141 0.1253 0.1605
REMARK 3 20 1.6718 - 1.6435 1.00 2673 140 0.1316 0.1813
REMARK 3 21 1.6435 - 1.6169 1.00 2662 140 0.1277 0.1573
REMARK 3 22 1.6169 - 1.5921 1.00 2667 141 0.1368 0.1519
REMARK 3 23 1.5921 - 1.5687 1.00 2673 141 0.1419 0.1725
REMARK 3 24 1.5687 - 1.5466 1.00 2655 139 0.1553 0.1988
REMARK 3 25 1.5466 - 1.5257 1.00 2650 140 0.1578 0.2177
REMARK 3 26 1.5257 - 1.5058 1.00 2639 139 0.1825 0.2279
REMARK 3 27 1.5058 - 1.4870 1.00 2655 139 0.1750 0.2187
REMARK 3 28 1.4870 - 1.4691 1.00 2685 142 0.1765 0.2314
REMARK 3 29 1.4691 - 1.4520 1.00 2633 138 0.1924 0.2033
REMARK 3 30 1.4520 - 1.4357 0.83 2206 116 0.2052 0.2374
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.120
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 15.100
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.005 3116
REMARK 3 ANGLE : 0.763 4244
REMARK 3 CHIRALITY : 0.066 451
REMARK 3 PLANARITY : 0.005 557
REMARK 3 DIHEDRAL : 17.867 1135
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5N1M COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 06-FEB-17.
REMARK 100 THE DEPOSITION ID IS D_1200003192.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-APR-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.9
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.918409
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : SILICON, ACTIVE SURFACE
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 84440
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.440
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 6.420
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.0100
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.44
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.52
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.4
REMARK 200 DATA REDUNDANCY IN SHELL : 6.50
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.420
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 4WIH
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.84
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MES-BIS-TRIS MEGA8-SOLUTION DTT EDTA
REMARK 280 LICL METHANOL, PH 6.9, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 29.20200
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 54.36050
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.28950
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 54.36050
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 29.20200
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 36.28950
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2370 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16340 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 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 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 SER A 34
REMARK 465 GLN A 35
REMARK 465 ILE B 11
REMARK 465 LEU B 26
REMARK 465 VAL B 27
REMARK 465 ALA B 28
REMARK 465 ALA B 29
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 ASN A 2 CG OD1 ND2
REMARK 470 LYS A 7 CE NZ
REMARK 470 LYS A 8 NZ
REMARK 470 LYS A 21 CE NZ
REMARK 470 LYS A 23 CE NZ
REMARK 470 LYS A 28 CD CE NZ
REMARK 470 LYS A 29 CE NZ
REMARK 470 GLU A 31 CG CD OE1 OE2
REMARK 470 SER A 32 OG
REMARK 470 ASN A 36 CG OD1 ND2
REMARK 470 SER A 53 OG
REMARK 470 PHE A 54 CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 61 NZ
REMARK 470 GLU A 64 CG CD OE1 OE2
REMARK 470 LYS A 78 CG CD CE NZ
REMARK 470 LYS A 81 CG CD CE NZ
REMARK 470 LEU A 82 CD1 CD2
REMARK 470 LYS A 92 NZ
REMARK 470 ILE A 163 CD1
REMARK 470 GLN A 176 CD OE1 NE2
REMARK 470 LYS A 192 CD CE NZ
REMARK 470 LYS A 254 CG CD CE NZ
REMARK 470 ARG A 256 CZ NH1 NH2
REMARK 470 LYS A 285 CD CE NZ
REMARK 470 LYS A 295 CD CE NZ
REMARK 470 GLU A 311 CD OE1 OE2
REMARK 470 LYS A 317 CG CD CE NZ
REMARK 470 PHE A 318 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 319 CG CD CE NZ
REMARK 470 GLU A 331 CG CD OE1 OE2
REMARK 470 GLU A 333 CG CD OE1 OE2
REMARK 470 GLU A 334 CG CD OE1 OE2
REMARK 470 ILE A 335 CG1 CG2 CD1
REMARK 470 ARG A 336 CG CD NE CZ NH1 NH2
REMARK 470 ILE A 339 CD1
REMARK 470 LYS A 345 CG CD CE NZ
REMARK 470 HIS B 23 CG ND1 CD2 CE1 NE2
REMARK 470 ILE B 25 CG1 CG2 CD1
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 ALA A 38 -175.92 -172.44
REMARK 500 ASP A 166 42.92 -148.92
REMARK 500 ASP A 184 101.23 65.19
REMARK 500 ASP A 184 76.11 63.43
REMARK 500 ASP B 24 20.97 -150.67
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BJK A 403
DBREF 5N1M A 0 350 UNP P25321 KAPCA_CRIGR 1 351
DBREF1 5N1M B 11 29 UNP A0A061IH64_CRIGR
DBREF2 5N1M B A0A061IH64 12 30
SEQADV 5N1M GLY A -2 UNP P25321 EXPRESSION TAG
SEQADV 5N1M HIS A -1 UNP P25321 EXPRESSION TAG
SEQADV 5N1M ALA B 13 UNP A0A061IH6 SER 14 CONFLICT
SEQADV 5N1M GLN B 20 UNP A0A061IH6 ASN 21 CONFLICT
SEQADV 5N1M ALA B 28 UNP A0A061IH6 SER 29 CONFLICT
SEQADV 5N1M ALA B 29 UNP A0A061IH6 SER 30 CONFLICT
SEQRES 1 A 353 GLY HIS MET GLY ASN ALA ALA ALA ALA LYS LYS GLY SEP
SEQRES 2 A 353 GLU GLN GLU SER VAL LYS GLU PHE LEU ALA LYS ALA LYS
SEQRES 3 A 353 GLU GLU PHE LEU LYS LYS TRP GLU SER PRO SER GLN ASN
SEQRES 4 A 353 THR ALA GLN LEU ASP HIS PHE ASP ARG ILE LYS THR LEU
SEQRES 5 A 353 GLY THR GLY SER PHE GLY ARG VAL MET LEU VAL LYS HIS
SEQRES 6 A 353 LYS GLU THR GLY ASN HIS TYR ALA MET LYS ILE LEU ASP
SEQRES 7 A 353 LYS GLN LYS VAL VAL LYS LEU LYS GLN ILE GLU HIS THR
SEQRES 8 A 353 LEU ASN GLU LYS ARG ILE LEU GLN ALA VAL ASN PHE PRO
SEQRES 9 A 353 PHE LEU VAL LYS LEU GLU PHE SER PHE LYS ASP ASN SER
SEQRES 10 A 353 ASN LEU TYR MET VAL MET GLU TYR VAL PRO GLY GLY GLU
SEQRES 11 A 353 MET PHE SER HIS LEU ARG ARG ILE GLY ARG PHE SEP GLU
SEQRES 12 A 353 PRO HIS ALA ARG PHE TYR ALA ALA GLN ILE VAL LEU THR
SEQRES 13 A 353 PHE GLU TYR LEU HIS SER LEU ASP LEU ILE TYR ARG ASP
SEQRES 14 A 353 LEU LYS PRO GLU ASN LEU LEU ILE ASP GLN GLN GLY TYR
SEQRES 15 A 353 ILE GLN VAL THR ASP PHE GLY PHE ALA LYS ARG VAL LYS
SEQRES 16 A 353 GLY ARG THR TRP TPO LEU CYS GLY THR PRO GLU TYR LEU
SEQRES 17 A 353 ALA PRO GLU ILE ILE LEU SER LYS GLY TYR ASN LYS ALA
SEQRES 18 A 353 VAL ASP TRP TRP ALA LEU GLY VAL LEU ILE TYR GLU MET
SEQRES 19 A 353 ALA ALA GLY TYR PRO PRO PHE PHE ALA ASP GLN PRO ILE
SEQRES 20 A 353 GLN ILE TYR GLU LYS ILE VAL SER GLY LYS VAL ARG PHE
SEQRES 21 A 353 PRO SER HIS PHE SER SER ASP LEU LYS ASP LEU LEU ARG
SEQRES 22 A 353 ASN LEU LEU GLN VAL ASP LEU THR LYS ARG PHE GLY ASN
SEQRES 23 A 353 LEU LYS ASN GLY VAL ASN ASP ILE LYS ASN HIS LYS TRP
SEQRES 24 A 353 PHE ALA THR THR ASP TRP ILE ALA ILE TYR GLN ARG LYS
SEQRES 25 A 353 VAL GLU ALA PRO PHE ILE PRO LYS PHE LYS GLY PRO GLY
SEQRES 26 A 353 ASP THR SER ASN PHE ASP ASP TYR GLU GLU GLU GLU ILE
SEQRES 27 A 353 ARG VAL SEP ILE ASN GLU LYS CYS GLY LYS GLU PHE THR
SEQRES 28 A 353 GLU PHE
SEQRES 1 B 19 ILE ALA ALA GLY ARG THR GLY ARG ARG GLN ALA ILE HIS
SEQRES 2 B 19 ASP ILE LEU VAL ALA ALA
MODRES 5N1M SEP A 10 SER MODIFIED RESIDUE
MODRES 5N1M SEP A 139 SER MODIFIED RESIDUE
MODRES 5N1M TPO A 197 THR MODIFIED RESIDUE
MODRES 5N1M SEP A 338 SER MODIFIED RESIDUE
HET SEP A 10 14
HET SEP A 139 14
HET TPO A 197 17
HET SEP A 338 14
HET MPD A 401 22
HET DMS A 402 10
HET BJK A 403 23
HETNAM SEP PHOSPHOSERINE
HETNAM TPO PHOSPHOTHREONINE
HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL
HETNAM DMS DIMETHYL SULFOXIDE
HETNAM BJK (4-METHOXY-3-OXIDANYL-PHENYL)METHYLAZANIUM
HETSYN SEP PHOSPHONOSERINE
HETSYN TPO PHOSPHONOTHREONINE
FORMUL 1 SEP 3(C3 H8 N O6 P)
FORMUL 1 TPO C4 H10 N O6 P
FORMUL 3 MPD C6 H14 O2
FORMUL 4 DMS C2 H6 O S
FORMUL 5 BJK C8 H12 N O2 1+
FORMUL 6 HOH *259(H2 O)
HELIX 1 AA1 GLY A 1 SER A 32 1 32
HELIX 2 AA2 GLN A 39 ASP A 41 5 3
HELIX 3 AA3 LYS A 81 GLN A 96 1 16
HELIX 4 AA4 GLU A 127 GLY A 136 1 10
HELIX 5 AA5 SEP A 139 LEU A 160 1 22
HELIX 6 AA6 LYS A 168 GLU A 170 5 3
HELIX 7 AA7 THR A 201 LEU A 205 5 5
HELIX 8 AA8 ALA A 206 LEU A 211 1 6
HELIX 9 AA9 LYS A 217 GLY A 234 1 18
HELIX 10 AB1 GLN A 242 GLY A 253 1 12
HELIX 11 AB2 SER A 262 LEU A 273 1 12
HELIX 12 AB3 VAL A 288 ASN A 293 1 6
HELIX 13 AB4 HIS A 294 ALA A 298 5 5
HELIX 14 AB5 ASP A 301 GLN A 307 1 7
HELIX 15 AB6 GLY A 344 THR A 348 5 5
SHEET 1 AA1 5 PHE A 43 THR A 51 0
SHEET 2 AA1 5 GLY A 55 HIS A 62 -1 O LEU A 59 N LYS A 47
SHEET 3 AA1 5 HIS A 68 ASP A 75 -1 O MET A 71 N MET A 58
SHEET 4 AA1 5 ASN A 115 GLU A 121 -1 O MET A 120 N ALA A 70
SHEET 5 AA1 5 LEU A 106 LYS A 111 -1 N GLU A 107 O VAL A 119
SHEET 1 AA2 2 LEU A 162 ILE A 163 0
SHEET 2 AA2 2 LYS A 189 ARG A 190 -1 O LYS A 189 N ILE A 163
SHEET 1 AA3 2 LEU A 172 ILE A 174 0
SHEET 2 AA3 2 ILE A 180 VAL A 182 -1 O GLN A 181 N LEU A 173
LINK C GLY A 9 N SEP A 10 1555 1555 1.33
LINK C SEP A 10 N GLU A 11 1555 1555 1.33
LINK C PHE A 138 N SEP A 139 1555 1555 1.33
LINK C SEP A 139 N GLU A 140 1555 1555 1.33
LINK C TRP A 196 N TPO A 197 1555 1555 1.33
LINK C TPO A 197 N LEU A 198 1555 1555 1.33
LINK C VAL A 337 N SEP A 338 1555 1555 1.33
LINK C SEP A 338 N ILE A 339 1555 1555 1.33
SITE 1 AC1 6 VAL A 15 PHE A 100 LEU A 152 GLU A 155
SITE 2 AC1 6 TYR A 306 HOH A 575
SITE 1 AC2 4 LEU A 82 GLU A 86 GLY A 136 ALA A 233
SITE 1 AC3 9 VAL A 57 ALA A 70 MET A 120 GLU A 121
SITE 2 AC3 9 GLU A 127 GLU A 170 LEU A 173 THR A 183
SITE 3 AC3 9 ASP A 184
CRYST1 58.404 72.579 108.721 90.00 90.00 90.00 P 21 21 21 4
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 0.017122 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013778 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009198 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
