HEADER PROTEIN BINDING/TRANSFERASE 11-NOV-15 5EP6
TITLE THE CRYSTAL STRUCTURE OF NAP1 IN COMPLEX WITH TBK1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 5-AZACYTIDINE-INDUCED PROTEIN 2;
COMPND 3 CHAIN: A, C;
COMPND 4 FRAGMENT: UNP RESIDUES 215-255;
COMPND 5 SYNONYM: NF-KAPPA-B-ACTIVATING KINASE-ASSOCIATED PROTEIN 1,NAK-
COMPND 6 ASSOCIATED PROTEIN 1,TILP;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: SERINE/THREONINE-PROTEIN KINASE TBK1;
COMPND 10 CHAIN: B, D;
COMPND 11 FRAGMENT: UNP RESIDUES 677-729;
COMPND 12 SYNONYM: NF-KAPPA-B-ACTIVATING KINASE,T2K,TANK-BINDING KINASE 1;
COMPND 13 EC: 2.7.11.1;
COMPND 14 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: AZI2, NAP1, TBKBP2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 GENE: TBK1, NAK;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS NAP1, TBK1, CALCOCO2, PROTEIN BINDING-TRANSFERASE COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR F.LI,X.XIE,J.LIU,L.PAN
REVDAT 1 28-SEP-16 5EP6 0
JRNL AUTH F.LI,X.XIE,Y.WANG,J.LIU,X.CHENG,Y.GUO,Y.GONG,S.HU,L.PAN
JRNL TITL STRUCTURAL INSIGHTS INTO THE INTERACTION AND DISEASE
JRNL TITL 2 MECHANISM OF NEURODEGENERATIVE DISEASE-ASSOCIATED OPTINEURIN
JRNL TITL 3 AND TBK1 PROTEINS.
JRNL REF NAT COMMUN V. 7 12708 2016
JRNL REFN ESSN 2041-1723
JRNL PMID 27620379
JRNL DOI 10.1038/NCOMMS12708
REMARK 2
REMARK 2 RESOLUTION. 1.45 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8.2_1309
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) : 1.45
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.09
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 3 NUMBER OF REFLECTIONS : 31329
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.188
REMARK 3 R VALUE (WORKING SET) : 0.187
REMARK 3 FREE R VALUE : 0.217
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.050
REMARK 3 FREE R VALUE TEST SET COUNT : 1583
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 43.1109 - 3.2260 0.95 2788 143 0.2146 0.2256
REMARK 3 2 3.2260 - 2.5606 1.00 2796 149 0.1999 0.2378
REMARK 3 3 2.5606 - 2.2370 1.00 2747 153 0.1716 0.1911
REMARK 3 4 2.2370 - 2.0324 1.00 2744 148 0.1547 0.1782
REMARK 3 5 2.0324 - 1.8868 1.00 2744 130 0.1616 0.2302
REMARK 3 6 1.8868 - 1.7755 1.00 2729 137 0.1642 0.2061
REMARK 3 7 1.7755 - 1.6866 1.00 2691 168 0.1535 0.2309
REMARK 3 8 1.6866 - 1.6132 1.00 2688 142 0.1513 0.2067
REMARK 3 9 1.6132 - 1.5511 1.00 2738 140 0.1587 0.2033
REMARK 3 10 1.5511 - 1.4975 0.99 2687 143 0.1715 0.2569
REMARK 3 11 1.4975 - 1.4507 0.89 2394 130 0.2042 0.2411
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) : 0.130
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.760
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 : 0.006 1541
REMARK 3 ANGLE : 0.994 2090
REMARK 3 CHIRALITY : 0.060 232
REMARK 3 PLANARITY : 0.003 266
REMARK 3 DIHEDRAL : 17.787 638
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 5EP6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-NOV-15.
REMARK 100 THE DEPOSITION ID IS D_1000215298.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-JUN-04
REMARK 200 TEMPERATURE (KELVIN) : 298.15
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9791
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31428
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.450
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 (%) : 98.8
REMARK 200 DATA REDUNDANCY : 6.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 27.5000
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: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 32.76
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.83
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1% W/V TRYPTONE, 0.05 M HEPES SODIUM
REMARK 280 (PH 7.0), 12% W/V PEG 3350, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 291.15K
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 20.68000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 42.20800
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 25.05650
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 42.20800
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 20.68000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 25.05650
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: 1620 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 7030 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
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: 2520 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 7250 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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 THR A 251
REMARK 465 ALA A 252
REMARK 465 ILE A 253
REMARK 465 LYS A 254
REMARK 465 LYS A 255
REMARK 465 GLU A 256
REMARK 465 ASN A 257
REMARK 465 LEU A 258
REMARK 465 TYR A 259
REMARK 465 PHE A 260
REMARK 465 GLN A 261
REMARK 465 SER C 250
REMARK 465 THR C 251
REMARK 465 ALA C 252
REMARK 465 ILE C 253
REMARK 465 LYS C 254
REMARK 465 LYS C 255
REMARK 465 GLU C 256
REMARK 465 ASN C 257
REMARK 465 LEU C 258
REMARK 465 TYR C 259
REMARK 465 PHE C 260
REMARK 465 GLN C 261
REMARK 465 SER B 672
REMARK 465 GLY B 673
REMARK 465 SER B 674
REMARK 465 GLY B 675
REMARK 465 SER B 676
REMARK 465 TYR B 677
REMARK 465 PRO B 678
REMARK 465 ASN B 725
REMARK 465 VAL B 726
REMARK 465 ASP B 727
REMARK 465 CYS B 728
REMARK 465 LEU B 729
REMARK 465 SER D 672
REMARK 465 GLY D 673
REMARK 465 SER D 674
REMARK 465 GLY D 675
REMARK 465 SER D 676
REMARK 465 TYR D 677
REMARK 465 PRO D 678
REMARK 465 ASN D 725
REMARK 465 VAL D 726
REMARK 465 ASP D 727
REMARK 465 CYS D 728
REMARK 465 LEU D 729
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 GLU A 225 CD OE1 OE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OE2 GLU B 685 O2 GOL D 802 3755 2.13
REMARK 500 OE2 GLU A 242 NZ LYS C 227 3745 2.16
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 GOL A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 802
DBREF 5EP6 A 215 255 UNP Q9H6S1 AZI2_HUMAN 215 255
DBREF 5EP6 C 215 255 UNP Q9H6S1 AZI2_HUMAN 215 255
DBREF 5EP6 B 677 729 UNP Q9UHD2 TBK1_HUMAN 677 729
DBREF 5EP6 D 677 729 UNP Q9UHD2 TBK1_HUMAN 677 729
SEQADV 5EP6 GLU A 256 UNP Q9H6S1 EXPRESSION TAG
SEQADV 5EP6 ASN A 257 UNP Q9H6S1 EXPRESSION TAG
SEQADV 5EP6 LEU A 258 UNP Q9H6S1 EXPRESSION TAG
SEQADV 5EP6 TYR A 259 UNP Q9H6S1 EXPRESSION TAG
SEQADV 5EP6 PHE A 260 UNP Q9H6S1 EXPRESSION TAG
SEQADV 5EP6 GLN A 261 UNP Q9H6S1 EXPRESSION TAG
SEQADV 5EP6 GLU C 256 UNP Q9H6S1 EXPRESSION TAG
SEQADV 5EP6 ASN C 257 UNP Q9H6S1 EXPRESSION TAG
SEQADV 5EP6 LEU C 258 UNP Q9H6S1 EXPRESSION TAG
SEQADV 5EP6 TYR C 259 UNP Q9H6S1 EXPRESSION TAG
SEQADV 5EP6 PHE C 260 UNP Q9H6S1 EXPRESSION TAG
SEQADV 5EP6 GLN C 261 UNP Q9H6S1 EXPRESSION TAG
SEQADV 5EP6 SER B 672 UNP Q9UHD2 EXPRESSION TAG
SEQADV 5EP6 GLY B 673 UNP Q9UHD2 EXPRESSION TAG
SEQADV 5EP6 SER B 674 UNP Q9UHD2 EXPRESSION TAG
SEQADV 5EP6 GLY B 675 UNP Q9UHD2 EXPRESSION TAG
SEQADV 5EP6 SER B 676 UNP Q9UHD2 EXPRESSION TAG
SEQADV 5EP6 SER D 672 UNP Q9UHD2 EXPRESSION TAG
SEQADV 5EP6 GLY D 673 UNP Q9UHD2 EXPRESSION TAG
SEQADV 5EP6 SER D 674 UNP Q9UHD2 EXPRESSION TAG
SEQADV 5EP6 GLY D 675 UNP Q9UHD2 EXPRESSION TAG
SEQADV 5EP6 SER D 676 UNP Q9UHD2 EXPRESSION TAG
SEQRES 1 A 47 SER SER ASP ASN MET GLN HIS ALA TYR TRP GLU LEU LYS
SEQRES 2 A 47 ARG GLU MET SER ASN LEU HIS LEU VAL THR GLN VAL GLN
SEQRES 3 A 47 ALA GLU LEU LEU ARG LYS LEU LYS THR SER THR ALA ILE
SEQRES 4 A 47 LYS LYS GLU ASN LEU TYR PHE GLN
SEQRES 1 C 47 SER SER ASP ASN MET GLN HIS ALA TYR TRP GLU LEU LYS
SEQRES 2 C 47 ARG GLU MET SER ASN LEU HIS LEU VAL THR GLN VAL GLN
SEQRES 3 C 47 ALA GLU LEU LEU ARG LYS LEU LYS THR SER THR ALA ILE
SEQRES 4 C 47 LYS LYS GLU ASN LEU TYR PHE GLN
SEQRES 1 B 58 SER GLY SER GLY SER TYR PRO SER SER ASN THR LEU VAL
SEQRES 2 B 58 GLU MET THR LEU GLY MET LYS LYS LEU LYS GLU GLU MET
SEQRES 3 B 58 GLU GLY VAL VAL LYS GLU LEU ALA GLU ASN ASN HIS ILE
SEQRES 4 B 58 LEU GLU ARG PHE GLY SER LEU THR MET ASP GLY GLY LEU
SEQRES 5 B 58 ARG ASN VAL ASP CYS LEU
SEQRES 1 D 58 SER GLY SER GLY SER TYR PRO SER SER ASN THR LEU VAL
SEQRES 2 D 58 GLU MET THR LEU GLY MET LYS LYS LEU LYS GLU GLU MET
SEQRES 3 D 58 GLU GLY VAL VAL LYS GLU LEU ALA GLU ASN ASN HIS ILE
SEQRES 4 D 58 LEU GLU ARG PHE GLY SER LEU THR MET ASP GLY GLY LEU
SEQRES 5 D 58 ARG ASN VAL ASP CYS LEU
HET GOL A 301 6
HET GOL C 301 6
HET GOL B 801 6
HET GOL D 801 6
HET GOL D 802 6
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 GOL 5(C3 H8 O3)
FORMUL 10 HOH *101(H2 O)
HELIX 1 AA1 SER A 215 LEU A 247 1 33
HELIX 2 AA2 SER C 216 LEU C 247 1 32
HELIX 3 AA3 SER B 680 PHE B 714 1 35
HELIX 4 AA4 SER D 680 PHE D 714 1 35
SHEET 1 AA1 3 LYS A 248 THR A 249 0
SHEET 2 AA1 3 GLY B 715 LEU B 717 1 O LEU B 717 N LYS A 248
SHEET 3 AA1 3 GLY D 715 LEU D 717 -1 O SER D 716 N SER B 716
SITE 1 AC1 7 ARG A 228 SER A 231 ASN A 232 LEU C 235
SITE 2 AC1 7 GOL C 301 HOH C 417 HOH C 420
SITE 1 AC2 7 ARG A 228 GOL A 301 VAL C 236 VAL C 239
SITE 2 AC2 7 HOH C 417 ALA D 705 ASN D 708
SITE 1 AC3 5 ARG C 228 GLU C 229 ASN C 232 HOH C 413
SITE 2 AC3 5 HOH D 910
SITE 1 AC4 2 GLU D 695 GLU D 696
SITE 1 AC5 6 GLU B 685 GLN C 220 TRP C 224 LYS C 227
SITE 2 AC5 6 HOH C 402 ARG D 724
CRYST1 41.360 50.113 84.416 90.00 90.00 90.00 P 21 21 21 8
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 0.024178 0.000000 0.000000 0.00000
SCALE2 0.000000 0.019955 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011846 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
