HEADER IMMUNE SYSTEM 11-FEB-19 6NYH
TITLE STRUCTURE OF HUMAN RIPK1 KINASE DOMAIN IN COMPLEX WITH GNE684
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RECEPTOR-INTERACTING SERINE/THREONINE-PROTEIN KINASE 1;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: CELL DEATH PROTEIN RIP,RECEPTOR-INTERACTING PROTEIN 1,RIP-1;
COMPND 5 EC: 2.7.11.1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: RIPK1, RIP, RIP1;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS
KEYWDS RIP1, KINASE, RIP, RIP1K RIPK1, IMMUNE SYSTEM, TRANSFERASE-
KEYWDS 2 TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR R.FONG,P.J.LUPARDUS
REVDAT 3 11-OCT-23 6NYH 1 REMARK
REVDAT 2 01-JAN-20 6NYH 1 JRNL
REVDAT 1 29-MAY-19 6NYH 0
JRNL AUTH S.PATEL,J.D.WEBSTER,E.VARFOLOMEEV,Y.C.KWON,J.H.CHENG,
JRNL AUTH 2 J.ZHANG,D.L.DUGGER,K.E.WICKLIFFE,A.MALTZMAN,
JRNL AUTH 3 S.SUJATHA-BHASKAR,P.BIR KOHLI,S.RAMASWAMY,G.DESHMUKH,
JRNL AUTH 4 B.M.LIEDERER,R.FONG,G.HAMILTON,P.LUPARDUS,P.CAPLAZI,W.P.LEE,
JRNL AUTH 5 M.VAN LOOKEREN CAMPAGNE,A.JOHNSON,B.S.MCKENZIE,M.R.JUNTTILA,
JRNL AUTH 6 K.NEWTON,D.VUCIC
JRNL TITL RIP1 INHIBITION BLOCKS INFLAMMATORY DISEASES BUT NOT TUMOR
JRNL TITL 2 GROWTH OR METASTASES.
JRNL REF CELL DEATH DIFFER. V. 27 161 2020
JRNL REFN ISSN 1350-9047
JRNL PMID 31101885
JRNL DOI 10.1038/S41418-019-0347-0
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.10.1-2155_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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.52
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.0
REMARK 3 NUMBER OF REFLECTIONS : 32202
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.206
REMARK 3 R VALUE (WORKING SET) : 0.203
REMARK 3 FREE R VALUE : 0.246
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 6.690
REMARK 3 FREE R VALUE TEST SET COUNT : 2154
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 48.5299 - 5.1772 0.95 2160 172 0.2102 0.2188
REMARK 3 2 5.1772 - 4.1100 0.98 2162 156 0.1615 0.1874
REMARK 3 3 4.1100 - 3.5906 0.94 2009 137 0.1675 0.2250
REMARK 3 4 3.5906 - 3.2624 0.92 1981 143 0.1939 0.2665
REMARK 3 5 3.2624 - 3.0286 0.90 1935 138 0.2126 0.2452
REMARK 3 6 3.0286 - 2.8501 0.97 2062 144 0.2266 0.2731
REMARK 3 7 2.8501 - 2.7073 0.98 2065 158 0.2171 0.2559
REMARK 3 8 2.7073 - 2.5895 0.89 1901 124 0.2218 0.3302
REMARK 3 9 2.5895 - 2.4898 0.99 2066 170 0.2269 0.2719
REMARK 3 10 2.4898 - 2.4039 0.98 2052 149 0.2192 0.2973
REMARK 3 11 2.4039 - 2.3287 0.98 2065 138 0.2294 0.3017
REMARK 3 12 2.3287 - 2.2622 0.98 2064 157 0.2326 0.2753
REMARK 3 13 2.2622 - 2.2026 0.77 1618 105 0.2444 0.3358
REMARK 3 14 2.2026 - 2.1489 0.90 1879 125 0.2580 0.3018
REMARK 3 15 2.1489 - 2.1000 0.96 2029 138 0.2710 0.3335
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.290
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.250
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 30.20
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 : 0.008 4176
REMARK 3 ANGLE : 0.935 5639
REMARK 3 CHIRALITY : 0.054 628
REMARK 3 PLANARITY : 0.005 706
REMARK 3 DIHEDRAL : 13.292 2509
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 6NYH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-FEB-19.
REMARK 100 THE DEPOSITION ID IS D_1000239669.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-AUG-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32257
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 48.520
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.4
REMARK 200 DATA REDUNDANCY : 5.700
REMARK 200 R MERGE (I) : 0.10600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.16
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.6
REMARK 200 DATA REDUNDANCY IN SHELL : 5.70
REMARK 200 R MERGE FOR SHELL (I) : 0.87200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.600
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: 4ITH
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.07
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.12
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS TRIS PROPANE BUFFER (PH
REMARK 280 6.5), 0.2 M SODIUM IODIDE, 20% PEG3350, VAPOR DIFFUSION,
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 23.49000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 62.61900
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 48.51700
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 62.61900
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 23.49000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 48.51700
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 GLY A -1
REMARK 465 SER A 0
REMARK 465 MET A 1
REMARK 465 GLN A 2
REMARK 465 PRO A 3
REMARK 465 ASP A 4
REMARK 465 MET A 5
REMARK 465 SER A 6
REMARK 465 LEU A 7
REMARK 465 SER A 20
REMARK 465 ALA A 21
REMARK 465 GLU A 22
REMARK 465 LEU A 23
REMARK 465 ASP A 24
REMARK 465 SER A 25
REMARK 465 GLY A 26
REMARK 465 GLY A 27
REMARK 465 PHE A 28
REMARK 465 GLY A 29
REMARK 465 LEU A 176
REMARK 465 ARG A 177
REMARK 465 GLU A 178
REMARK 465 VAL A 179
REMARK 465 ASP A 180
REMARK 465 GLY A 181
REMARK 465 THR A 182
REMARK 465 ALA A 183
REMARK 465 LYS A 184
REMARK 465 LYS A 185
REMARK 465 ASN A 186
REMARK 465 GLY A 187
REMARK 465 GLY B -1
REMARK 465 SER B 0
REMARK 465 MET B 1
REMARK 465 GLN B 2
REMARK 465 PRO B 3
REMARK 465 ASP B 4
REMARK 465 MET B 5
REMARK 465 SER B 6
REMARK 465 LEU B 7
REMARK 465 ASN B 8
REMARK 465 VAL B 9
REMARK 465 ILE B 10
REMARK 465 ALA B 21
REMARK 465 GLU B 22
REMARK 465 LEU B 23
REMARK 465 ASP B 24
REMARK 465 SER B 25
REMARK 465 GLY B 26
REMARK 465 GLY B 27
REMARK 465 PHE B 28
REMARK 465 GLY B 29
REMARK 465 ARG B 37
REMARK 465 THR B 38
REMARK 465 TYR B 48
REMARK 465 LYS B 49
REMARK 465 GLY B 50
REMARK 465 PRO B 51
REMARK 465 ASN B 52
REMARK 465 CYS B 53
REMARK 465 ILE B 54
REMARK 465 GLU B 107
REMARK 465 MET B 108
REMARK 465 ASN B 170
REMARK 465 GLU B 171
REMARK 465 GLU B 172
REMARK 465 HIS B 173
REMARK 465 ASN B 174
REMARK 465 GLU B 175
REMARK 465 LEU B 176
REMARK 465 ARG B 177
REMARK 465 GLU B 178
REMARK 465 VAL B 179
REMARK 465 ASP B 180
REMARK 465 GLY B 181
REMARK 465 THR B 182
REMARK 465 ALA B 183
REMARK 465 LYS B 184
REMARK 465 LYS B 185
REMARK 465 ASN B 186
REMARK 465 GLY B 187
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 8 CG OD1 ND2
REMARK 470 GLU A 19 CG CD OE1 OE2
REMARK 470 LYS A 30 CG CD CE NZ
REMARK 470 GLU A 85 CG CD OE1 OE2
REMARK 470 LYS A 167 CG CD CE NZ
REMARK 470 GLU A 172 CG CD OE1 OE2
REMARK 470 LYS A 204 CG CD CE NZ
REMARK 470 LYS B 13 CG CD CE NZ
REMARK 470 ASP B 16 CG OD1 OD2
REMARK 470 GLU B 19 CG CD OE1 OE2
REMARK 470 SER B 20 OG
REMARK 470 LYS B 30 CG CD CE NZ
REMARK 470 GLN B 39 CG CD OE1 NE2
REMARK 470 GLU B 55 CG CD OE1 OE2
REMARK 470 GLU B 58 CG CD OE1 OE2
REMARK 470 GLU B 62 CG CD OE1 OE2
REMARK 470 GLU B 84 CG CD OE1 OE2
REMARK 470 GLU B 85 CG CD OE1 OE2
REMARK 470 LYS B 87 CG CD CE NZ
REMARK 470 LYS B 167 CG CD CE NZ
REMARK 470 GLN B 235 CG CD OE1 NE2
REMARK 470 GLN B 236 CG CD OE1 NE2
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 137 -10.18 77.85
REMARK 500 ASP A 138 44.02 -144.44
REMARK 500 ASP A 200 83.03 -166.61
REMARK 500 LYS B 137 -19.60 81.99
REMARK 500 LYS B 140 163.26 179.52
REMARK 500 ASP B 200 73.37 -152.16
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 L8D A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IOD A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue L8D B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IOD B 302
DBREF 6NYH A 1 294 UNP Q13546 RIPK1_HUMAN 1 294
DBREF 6NYH B 1 294 UNP Q13546 RIPK1_HUMAN 1 294
SEQADV 6NYH GLY A -1 UNP Q13546 EXPRESSION TAG
SEQADV 6NYH SER A 0 UNP Q13546 EXPRESSION TAG
SEQADV 6NYH ALA A 34 UNP Q13546 CYS 34 ENGINEERED MUTATION
SEQADV 6NYH ALA A 127 UNP Q13546 CYS 127 ENGINEERED MUTATION
SEQADV 6NYH ALA A 233 UNP Q13546 CYS 233 ENGINEERED MUTATION
SEQADV 6NYH ALA A 240 UNP Q13546 CYS 240 ENGINEERED MUTATION
SEQADV 6NYH GLY B -1 UNP Q13546 EXPRESSION TAG
SEQADV 6NYH SER B 0 UNP Q13546 EXPRESSION TAG
SEQADV 6NYH ALA B 34 UNP Q13546 CYS 34 ENGINEERED MUTATION
SEQADV 6NYH ALA B 127 UNP Q13546 CYS 127 ENGINEERED MUTATION
SEQADV 6NYH ALA B 233 UNP Q13546 CYS 233 ENGINEERED MUTATION
SEQADV 6NYH ALA B 240 UNP Q13546 CYS 240 ENGINEERED MUTATION
SEQRES 1 A 296 GLY SER MET GLN PRO ASP MET SER LEU ASN VAL ILE LYS
SEQRES 2 A 296 MET LYS SER SER ASP PHE LEU GLU SER ALA GLU LEU ASP
SEQRES 3 A 296 SER GLY GLY PHE GLY LYS VAL SER LEU ALA PHE HIS ARG
SEQRES 4 A 296 THR GLN GLY LEU MET ILE MET LYS THR VAL TYR LYS GLY
SEQRES 5 A 296 PRO ASN CYS ILE GLU HIS ASN GLU ALA LEU LEU GLU GLU
SEQRES 6 A 296 ALA LYS MET MET ASN ARG LEU ARG HIS SER ARG VAL VAL
SEQRES 7 A 296 LYS LEU LEU GLY VAL ILE ILE GLU GLU GLY LYS TYR SER
SEQRES 8 A 296 LEU VAL MET GLU TYR MET GLU LYS GLY ASN LEU MET HIS
SEQRES 9 A 296 VAL LEU LYS ALA GLU MET SER THR PRO LEU SER VAL LYS
SEQRES 10 A 296 GLY ARG ILE ILE LEU GLU ILE ILE GLU GLY MET ALA TYR
SEQRES 11 A 296 LEU HIS GLY LYS GLY VAL ILE HIS LYS ASP LEU LYS PRO
SEQRES 12 A 296 GLU ASN ILE LEU VAL ASP ASN ASP PHE HIS ILE LYS ILE
SEQRES 13 A 296 ALA ASP LEU GLY LEU ALA SER PHE LYS MET TRP SER LYS
SEQRES 14 A 296 LEU ASN ASN GLU GLU HIS ASN GLU LEU ARG GLU VAL ASP
SEQRES 15 A 296 GLY THR ALA LYS LYS ASN GLY GLY THR LEU TYR TYR MET
SEQRES 16 A 296 ALA PRO GLU HIS LEU ASN ASP VAL ASN ALA LYS PRO THR
SEQRES 17 A 296 GLU LYS SER ASP VAL TYR SER PHE ALA VAL VAL LEU TRP
SEQRES 18 A 296 ALA ILE PHE ALA ASN LYS GLU PRO TYR GLU ASN ALA ILE
SEQRES 19 A 296 ALA GLU GLN GLN LEU ILE MET ALA ILE LYS SER GLY ASN
SEQRES 20 A 296 ARG PRO ASP VAL ASP ASP ILE THR GLU TYR CYS PRO ARG
SEQRES 21 A 296 GLU ILE ILE SER LEU MET LYS LEU CYS TRP GLU ALA ASN
SEQRES 22 A 296 PRO GLU ALA ARG PRO THR PHE PRO GLY ILE GLU GLU LYS
SEQRES 23 A 296 PHE ARG PRO PHE TYR LEU SER GLN LEU GLU
SEQRES 1 B 296 GLY SER MET GLN PRO ASP MET SER LEU ASN VAL ILE LYS
SEQRES 2 B 296 MET LYS SER SER ASP PHE LEU GLU SER ALA GLU LEU ASP
SEQRES 3 B 296 SER GLY GLY PHE GLY LYS VAL SER LEU ALA PHE HIS ARG
SEQRES 4 B 296 THR GLN GLY LEU MET ILE MET LYS THR VAL TYR LYS GLY
SEQRES 5 B 296 PRO ASN CYS ILE GLU HIS ASN GLU ALA LEU LEU GLU GLU
SEQRES 6 B 296 ALA LYS MET MET ASN ARG LEU ARG HIS SER ARG VAL VAL
SEQRES 7 B 296 LYS LEU LEU GLY VAL ILE ILE GLU GLU GLY LYS TYR SER
SEQRES 8 B 296 LEU VAL MET GLU TYR MET GLU LYS GLY ASN LEU MET HIS
SEQRES 9 B 296 VAL LEU LYS ALA GLU MET SER THR PRO LEU SER VAL LYS
SEQRES 10 B 296 GLY ARG ILE ILE LEU GLU ILE ILE GLU GLY MET ALA TYR
SEQRES 11 B 296 LEU HIS GLY LYS GLY VAL ILE HIS LYS ASP LEU LYS PRO
SEQRES 12 B 296 GLU ASN ILE LEU VAL ASP ASN ASP PHE HIS ILE LYS ILE
SEQRES 13 B 296 ALA ASP LEU GLY LEU ALA SER PHE LYS MET TRP SER LYS
SEQRES 14 B 296 LEU ASN ASN GLU GLU HIS ASN GLU LEU ARG GLU VAL ASP
SEQRES 15 B 296 GLY THR ALA LYS LYS ASN GLY GLY THR LEU TYR TYR MET
SEQRES 16 B 296 ALA PRO GLU HIS LEU ASN ASP VAL ASN ALA LYS PRO THR
SEQRES 17 B 296 GLU LYS SER ASP VAL TYR SER PHE ALA VAL VAL LEU TRP
SEQRES 18 B 296 ALA ILE PHE ALA ASN LYS GLU PRO TYR GLU ASN ALA ILE
SEQRES 19 B 296 ALA GLU GLN GLN LEU ILE MET ALA ILE LYS SER GLY ASN
SEQRES 20 B 296 ARG PRO ASP VAL ASP ASP ILE THR GLU TYR CYS PRO ARG
SEQRES 21 B 296 GLU ILE ILE SER LEU MET LYS LEU CYS TRP GLU ALA ASN
SEQRES 22 B 296 PRO GLU ALA ARG PRO THR PHE PRO GLY ILE GLU GLU LYS
SEQRES 23 B 296 PHE ARG PRO PHE TYR LEU SER GLN LEU GLU
HET L8D A 301 32
HET IOD A 302 1
HET IOD A 303 1
HET IOD A 304 1
HET L8D B 301 32
HET IOD B 302 1
HET IOD B 303 1
HET IOD B 304 1
HETNAM L8D (5S)-N-[(3S)-7-METHOXY-1-METHYL-2-OXO-2,3,4,5-
HETNAM 2 L8D TETRAHYDRO-1H-PYRIDO[3,4-B]AZEPIN-3-YL]-5-PHENYL-6,7-
HETNAM 3 L8D DIHYDRO-5H-PYRROLO[1,2-B][1,2,4]TRIAZOLE-2-CARBOXAMIDE
HETNAM IOD IODIDE ION
FORMUL 3 L8D 2(C23 H24 N6 O3)
FORMUL 4 IOD 6(I 1-)
FORMUL 11 HOH *201(H2 O)
HELIX 1 AA1 LYS A 13 PHE A 17 5 5
HELIX 2 AA2 CYS A 53 GLU A 55 5 3
HELIX 3 AA3 HIS A 56 ARG A 69 1 14
HELIX 4 AA4 ASN A 99 LYS A 105 1 7
HELIX 5 AA5 PRO A 111 LYS A 132 1 22
HELIX 6 AA6 LYS A 140 GLU A 142 5 3
HELIX 7 AA7 PHE A 162 GLU A 171 1 10
HELIX 8 AA8 ALA A 194 LEU A 198 5 5
HELIX 9 AA9 THR A 206 ASN A 224 1 19
HELIX 10 AB1 ALA A 233 SER A 243 1 11
HELIX 11 AB2 ASP A 248 ILE A 252 5 5
HELIX 12 AB3 PRO A 257 TRP A 268 1 12
HELIX 13 AB4 ASN A 271 ARG A 275 5 5
HELIX 14 AB5 THR A 277 LEU A 293 1 17
HELIX 15 AB6 LYS B 13 PHE B 17 5 5
HELIX 16 AB7 HIS B 56 ARG B 69 1 14
HELIX 17 AB8 LEU B 100 LYS B 105 1 6
HELIX 18 AB9 PRO B 111 LYS B 132 1 22
HELIX 19 AC1 LYS B 140 GLU B 142 5 3
HELIX 20 AC2 PHE B 162 ASN B 169 1 8
HELIX 21 AC3 ALA B 194 LEU B 198 5 5
HELIX 22 AC4 THR B 206 ASN B 224 1 19
HELIX 23 AC5 ALA B 233 SER B 243 1 11
HELIX 24 AC6 ASP B 248 ILE B 252 5 5
HELIX 25 AC7 PRO B 257 TRP B 268 1 12
HELIX 26 AC8 ASN B 271 ARG B 275 5 5
HELIX 27 AC9 THR B 277 LEU B 293 1 17
SHEET 1 AA1 5 ILE A 10 MET A 12 0
SHEET 2 AA1 5 LEU A 78 ILE A 83 1 O VAL A 81 N ILE A 10
SHEET 3 AA1 5 LYS A 87 GLU A 93 -1 O SER A 89 N ILE A 82
SHEET 4 AA1 5 GLY A 40 LYS A 49 -1 N VAL A 47 O TYR A 88
SHEET 5 AA1 5 VAL A 31 HIS A 36 -1 N HIS A 36 O GLY A 40
SHEET 1 AA2 2 ILE A 144 VAL A 146 0
SHEET 2 AA2 2 ILE A 152 ILE A 154 -1 O LYS A 153 N LEU A 145
SHEET 1 AA3 4 VAL B 31 PHE B 35 0
SHEET 2 AA3 4 LEU B 41 THR B 46 -1 O MET B 42 N ALA B 34
SHEET 3 AA3 4 TYR B 88 GLU B 93 -1 O LEU B 90 N LYS B 45
SHEET 4 AA3 4 LEU B 78 ILE B 83 -1 N ILE B 82 O SER B 89
SHEET 1 AA4 3 GLY B 98 ASN B 99 0
SHEET 2 AA4 3 ILE B 144 VAL B 146 -1 O VAL B 146 N GLY B 98
SHEET 3 AA4 3 ILE B 152 ILE B 154 -1 O LYS B 153 N LEU B 145
SITE 1 AC1 15 ILE A 43 LYS A 45 MET A 67 VAL A 75
SITE 2 AC1 15 VAL A 76 LEU A 78 LEU A 90 MET A 92
SITE 3 AC1 15 LEU A 129 HIS A 136 ILE A 154 ASP A 156
SITE 4 AC1 15 LEU A 157 LEU A 159 HOH A 481
SITE 1 AC2 1 HOH A 458
SITE 1 AC3 15 ILE B 43 LYS B 45 MET B 67 VAL B 75
SITE 2 AC3 15 VAL B 76 LEU B 78 LEU B 90 MET B 92
SITE 3 AC3 15 LEU B 129 HIS B 136 ILE B 154 ASP B 156
SITE 4 AC3 15 LEU B 157 LEU B 159 HOH B 447
SITE 1 AC4 1 ILE B 232
CRYST1 46.980 97.034 125.238 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 0.021286 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010306 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007985 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
