HEADER TRANSFERASE 19-NOV-15 5EUT
TITLE CRYSTAL STRUCTURE OF PHOSPHATIDYL INOSITOL 4-KINASE II ALPHA IN THE
TITLE 2 APO STATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOSPHATIDYLINOSITOL 4-KINASE TYPE 2-ALPHA,ENDOLYSIN,
COMPND 3 PHOSPHATIDYLINOSITOL 4-KINASE TYPE 2-ALPHA;
COMPND 4 CHAIN: A;
COMPND 5 SYNONYM: PHOSPHATIDYLINOSITOL 4-KINASE TYPE II-ALPHA,LYSIS PROTEIN,
COMPND 6 LYSOZYME,MURAMIDASE,PHOSPHATIDYLINOSITOL 4-KINASE TYPE II-ALPHA;
COMPND 7 EC: 2.7.1.67,3.2.1.17,2.7.1.67;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ENTEROBACTERIA PHAGE T4;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606, 10665;
SOURCE 5 GENE: PI4K2A;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS KINASE, LIPID, PHOSPHATIDYLINOSITOL, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.BAUMLOVA,E.BOURA
REVDAT 2 06-SEP-17 5EUT 1 REMARK
REVDAT 1 23-DEC-15 5EUT 0
JRNL AUTH A.BAUMLOVA,E.BOURA
JRNL TITL CRYSTAL STRUCTURE OF PHOSPHATIDYL INOSITOL 4-KINASE II ALPHA
JRNL TITL 2 IN THE APO STATE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
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) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.97
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 16072
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.249
REMARK 3 R VALUE (WORKING SET) : 0.246
REMARK 3 FREE R VALUE : 0.289
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 805
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 48.9740 - 5.0894 1.00 2690 142 0.1955 0.2277
REMARK 3 2 5.0894 - 4.0402 1.00 2574 136 0.2149 0.2729
REMARK 3 3 4.0402 - 3.5296 1.00 2538 133 0.2516 0.3216
REMARK 3 4 3.5296 - 3.2070 1.00 2512 133 0.3118 0.3629
REMARK 3 5 3.2070 - 2.9772 1.00 2517 132 0.3419 0.3511
REMARK 3 6 2.9772 - 2.8017 0.96 2436 129 0.4198 0.4149
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) : 0.590
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 36.080
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 : 0.003 3984
REMARK 3 ANGLE : 0.905 5403
REMARK 3 CHIRALITY : 0.036 588
REMARK 3 PLANARITY : 0.007 702
REMARK 3 DIHEDRAL : 14.796 1489
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 5EUT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-NOV-15.
REMARK 100 THE DEPOSITION ID IS D_1000215515.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-AUG-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
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) : 0.9796
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16220
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.802
REMARK 200 RESOLUTION RANGE LOW (A) : 48.970
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : 7.070
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.3800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.97
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.51
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 12.5% W/V PEG 1000, 12.5% W/V PEG
REMARK 280 3350, 12.5% V/V MPD, 0.1 M BICINE/TRIZMA BASE PH 8.5, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 40.00300
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 50.75750
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 40.00300
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 50.75750
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24750 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 72
REMARK 465 ALA A 73
REMARK 465 MET A 74
REMARK 465 GLY A 75
REMARK 465 THR A 76
REMARK 465 VAL A 77
REMARK 465 ALA A 78
REMARK 465 ALA A 79
REMARK 465 GLN A 80
REMARK 465 ALA A 81
REMARK 465 GLN A 82
REMARK 465 ALA A 83
REMARK 465 LEU A 84
REMARK 465 ALA A 85
REMARK 465 ALA A 86
REMARK 465 GLN A 87
REMARK 465 ALA A 88
REMARK 465 ALA A 89
REMARK 465 ALA A 90
REMARK 465 ALA A 91
REMARK 465 ALA A 92
REMARK 465 HIS A 93
REMARK 465 ALA A 94
REMARK 465 ALA A 95
REMARK 465 GLN A 96
REMARK 465 ALA A 97
REMARK 465 HIS A 98
REMARK 465 ARG A 99
REMARK 465 GLU A 100
REMARK 465 GLY A 233
REMARK 465 LYS A 234
REMARK 465 ARG A 235
REMARK 465 LEU A 236
REMARK 465 ALA A 237
REMARK 465 LEU A 238
REMARK 465 GLU A 239
REMARK 465 LYS A 240
REMARK 465 VAL A 241
REMARK 465 PRO A 242
REMARK 465 LYS A 243
REMARK 465 VAL A 244
REMARK 465 GLY A 245
REMARK 465 GLN A 246
REMARK 465 ARG A 247
REMARK 465 PHE A 248
REMARK 465 ASN A 249
REMARK 465 ARG A 250
REMARK 465 CYS A 320
REMARK 465 PRO A 321
REMARK 465 MET A 322
REMARK 465 ASP A 323
REMARK 465 SER A 324
REMARK 465 SER A 325
REMARK 465 SER A 326
REMARK 465 SER A 327
REMARK 465 ARG A 328
REMARK 465 ASP A 329
REMARK 465 THR A 330
REMARK 465 SER A 456
REMARK 465 HIS A 457
REMARK 465 GLN A 458
REMARK 465 ARG A 459
REMARK 465 SER A 460
REMARK 465 SER A 461
REMARK 465 SER A 462
REMARK 465 GLU A 463
REMARK 465 SER A 464
REMARK 465 TYR A 465
REMARK 465 THR A 466
REMARK 465 GLN A 467
REMARK 465 SER A 468
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 ARG A 101 CG CD NE CZ NH1 NH2
REMARK 470 TYR A 159 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG A1139 CG CD NE CZ NH1 NH2
REMARK 470 LYS A1164 CG CD CE NZ
REMARK 470 LEU A1166 CG CD1 CD2
REMARK 470 ARG A 181 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 336 CG CD CE NZ
REMARK 470 TYR A 365 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG A 455 CG CD NE CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
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 O PRO A 164 OG1 THR A 167 2.16
REMARK 500 O LEU A 162 ND2 ASN A 222 2.19
REMARK 500 OE2 GLU A 1013 NH1 ARG A 1147 2.19
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 SER A 135 -148.27 -144.85
REMARK 500 LYS A1126 -0.65 79.63
REMARK 500 TYR A1141 -51.22 74.32
REMARK 500 LEU A1166 46.52 -91.13
REMARK 500 LYS A 354 164.05 178.01
REMARK 500
REMARK 500 REMARK: NULL
DBREF 5EUT A 76 172 UNP Q9BTU6 P4K2A_HUMAN 76 172
DBREF 5EUT A 1004 1165 UNP P00720 ENLYS_BPT4 2 163
DBREF 5EUT A 1166 468 UNP Q9BTU6 P4K2A_HUMAN 179 468
SEQADV 5EUT GLY A 72 UNP Q9BTU6 EXPRESSION TAG
SEQADV 5EUT ALA A 73 UNP Q9BTU6 EXPRESSION TAG
SEQADV 5EUT MET A 74 UNP Q9BTU6 EXPRESSION TAG
SEQADV 5EUT GLY A 75 UNP Q9BTU6 EXPRESSION TAG
SEQADV 5EUT GLY A 1001 UNP Q9BTU6 LINKER
SEQADV 5EUT THR A 1002 UNP Q9BTU6 LINKER
SEQADV 5EUT GLY A 1003 UNP Q9BTU6 LINKER
SEQADV 5EUT GLY A 1014 UNP P00720 ARG 12 CONFLICT
SEQADV 5EUT THR A 1056 UNP P00720 CYS 54 CONFLICT
SEQADV 5EUT ALA A 1099 UNP P00720 CYS 97 CONFLICT
SEQADV 5EUT ARG A 1139 UNP P00720 ILE 137 CONFLICT
SEQADV 5EUT LEU A 1166 UNP Q9BTU6 PHE 179 CONFLICT
SEQRES 1 A 556 GLY ALA MET GLY THR VAL ALA ALA GLN ALA GLN ALA LEU
SEQRES 2 A 556 ALA ALA GLN ALA ALA ALA ALA ALA HIS ALA ALA GLN ALA
SEQRES 3 A 556 HIS ARG GLU ARG ASN GLU PHE PRO GLU ASP PRO GLU PHE
SEQRES 4 A 556 GLU ALA VAL VAL ARG GLN ALA GLU LEU ALA ILE GLU ARG
SEQRES 5 A 556 CYS ILE PHE PRO GLU ARG ILE TYR GLN GLY SER SER GLY
SEQRES 6 A 556 SER TYR PHE VAL LYS ASP PRO GLN GLY ARG ILE ILE ALA
SEQRES 7 A 556 VAL PHE LYS PRO LYS ASN GLU GLU PRO TYR GLY HIS LEU
SEQRES 8 A 556 ASN PRO LYS TRP THR LYS TRP LEU GLN LYS GLY THR GLY
SEQRES 9 A 556 ASN ILE PHE GLU MET LEU ARG ILE ASP GLU GLY LEU ARG
SEQRES 10 A 556 LEU LYS ILE TYR LYS ASP THR GLU GLY TYR TYR THR ILE
SEQRES 11 A 556 GLY ILE GLY HIS LEU LEU THR LYS SER PRO SER LEU ASN
SEQRES 12 A 556 ALA ALA LYS SER GLU LEU ASP LYS ALA ILE GLY ARG ASN
SEQRES 13 A 556 THR ASN GLY VAL ILE THR LYS ASP GLU ALA GLU LYS LEU
SEQRES 14 A 556 PHE ASN GLN ASP VAL ASP ALA ALA VAL ARG GLY ILE LEU
SEQRES 15 A 556 ARG ASN ALA LYS LEU LYS PRO VAL TYR ASP SER LEU ASP
SEQRES 16 A 556 ALA VAL ARG ARG ALA ALA LEU ILE ASN MET VAL PHE GLN
SEQRES 17 A 556 MET GLY GLU THR GLY VAL ALA GLY PHE THR ASN SER LEU
SEQRES 18 A 556 ARG MET LEU GLN GLN LYS ARG TRP ASP GLU ALA ALA VAL
SEQRES 19 A 556 ASN LEU ALA LYS SER ARG TRP TYR ASN GLN THR PRO ASN
SEQRES 20 A 556 ARG ALA LYS ARG VAL ILE THR THR PHE ARG THR GLY THR
SEQRES 21 A 556 TRP ASP ALA TYR LYS ASN LEU GLY ARG ASP CYS LEU VAL
SEQRES 22 A 556 LEU ASN GLN GLY TYR LEU SER GLU ALA GLY ALA SER LEU
SEQRES 23 A 556 VAL ASP GLN LYS LEU GLU LEU ASN ILE VAL PRO ARG THR
SEQRES 24 A 556 LYS VAL VAL TYR LEU ALA SER GLU THR PHE ASN TYR SER
SEQRES 25 A 556 ALA ILE ASP ARG VAL LYS SER ARG GLY LYS ARG LEU ALA
SEQRES 26 A 556 LEU GLU LYS VAL PRO LYS VAL GLY GLN ARG PHE ASN ARG
SEQRES 27 A 556 ILE GLY LEU PRO PRO LYS VAL GLY SER PHE GLN LEU PHE
SEQRES 28 A 556 VAL GLU GLY TYR LYS ASP ALA ASP TYR TRP LEU ARG ARG
SEQRES 29 A 556 PHE GLU ALA GLU PRO LEU PRO GLU ASN THR ASN ARG GLN
SEQRES 30 A 556 LEU LEU LEU GLN PHE GLU ARG LEU VAL VAL LEU ASP TYR
SEQRES 31 A 556 ILE ILE ARG ASN THR ASP ARG GLY ASN ASP ASN TRP LEU
SEQRES 32 A 556 ILE LYS TYR ASP CYS PRO MET ASP SER SER SER SER ARG
SEQRES 33 A 556 ASP THR ASP TRP VAL VAL VAL LYS GLU PRO VAL ILE LYS
SEQRES 34 A 556 VAL ALA ALA ILE ASP ASN GLY LEU ALA PHE PRO LEU LYS
SEQRES 35 A 556 HIS PRO ASP SER TRP ARG ALA TYR PRO PHE TYR TRP ALA
SEQRES 36 A 556 TRP LEU PRO GLN ALA LYS VAL PRO PHE SER GLN GLU ILE
SEQRES 37 A 556 LYS ASP LEU ILE LEU PRO LYS ILE SER ASP PRO ASN PHE
SEQRES 38 A 556 VAL LYS ASP LEU GLU GLU ASP LEU TYR GLU LEU PHE LYS
SEQRES 39 A 556 LYS ASP PRO GLY PHE ASP ARG GLY GLN PHE HIS LYS GLN
SEQRES 40 A 556 ILE ALA VAL MET ARG GLY GLN ILE LEU ASN LEU THR GLN
SEQRES 41 A 556 ALA LEU LYS ASP ASN LYS SER PRO LEU HIS LEU VAL GLN
SEQRES 42 A 556 MET PRO PRO VAL ILE VAL GLU THR ALA ARG SER HIS GLN
SEQRES 43 A 556 ARG SER SER SER GLU SER TYR THR GLN SER
HELIX 1 AA1 ASP A 107 ARG A 123 1 17
HELIX 2 AA2 ASN A 155 GLU A 157 5 3
HELIX 3 AA3 ASN A 163 GLY A 1001 1 11
HELIX 4 AA4 ASN A 1004 GLY A 1014 1 11
HELIX 5 AA5 SER A 1040 GLY A 1053 1 14
HELIX 6 AA6 THR A 1061 ARG A 1082 1 22
HELIX 7 AA7 LEU A 1086 LEU A 1093 1 8
HELIX 8 AA8 ASP A 1094 MET A 1108 1 15
HELIX 9 AA9 MET A 1108 ALA A 1114 1 7
HELIX 10 AB1 PHE A 1116 GLN A 1125 1 10
HELIX 11 AB2 ARG A 1127 LYS A 1137 1 11
HELIX 12 AB3 SER A 1138 GLN A 1143 1 6
HELIX 13 AB4 THR A 1144 THR A 1157 1 14
HELIX 14 AB5 TRP A 1160 LYS A 1164 5 5
HELIX 15 AB6 GLN A 188 GLU A 204 1 17
HELIX 16 AB7 SER A 224 SER A 231 1 8
HELIX 17 AB8 ALA A 270 GLU A 280 1 11
HELIX 18 AB9 PRO A 283 ARG A 305 1 23
HELIX 19 AC1 PHE A 364 VAL A 374 5 11
HELIX 20 AC2 SER A 377 SER A 389 1 13
HELIX 21 AC3 ASP A 390 LYS A 406 1 17
HELIX 22 AC4 ASP A 412 ASP A 436 1 25
HELIX 23 AC5 SER A 439 MET A 446 1 8
SHEET 1 AA1 5 GLU A 128 ARG A 129 0
SHEET 2 AA1 5 TYR A 138 LYS A 141 -1 O PHE A 139 N GLU A 128
SHEET 3 AA1 5 ILE A 147 PRO A 153 -1 O PHE A 151 N TYR A 138
SHEET 4 AA1 5 LYS A 256 LEU A 262 -1 O GLN A 261 N VAL A 150
SHEET 5 AA1 5 THR A 211 LEU A 216 -1 N LEU A 216 O LYS A 256
SHEET 1 AA2 3 ARG A1016 LYS A1021 0
SHEET 2 AA2 3 TYR A1027 GLY A1030 -1 O THR A1028 N TYR A1020
SHEET 3 AA2 3 HIS A1033 THR A1036 -1 O LEU A1035 N TYR A1027
SHEET 1 AA3 3 LYS A 268 ASP A 269 0
SHEET 2 AA3 3 TRP A 314 TYR A 318 -1 O ILE A 316 N LYS A 268
SHEET 3 AA3 3 ILE A 340 ALA A 344 -1 O ALA A 343 N LEU A 315
CRYST1 80.006 101.515 78.135 90.00 90.00 90.00 P 21 21 2 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 0.012499 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009851 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012798 0.00000
(ATOM LINES ARE NOT SHOWN.)
END