HEADER MEMBRANE PROTEIN 09-MAR-17 5NDZ
TITLE CRYSTAL STRUCTURE OF A THERMOSTABILISED HUMAN PROTEASE-ACTIVATED
TITLE 2 RECEPTOR-2 (PAR2) IN COMPLEX WITH AZ3451 AT 3.6 ANGSTROM RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LYSOZYME,PROTEINASE-ACTIVATED RECEPTOR 2,SOLUBLE CYTOCHROME
COMPND 3 B562,PROTEINASE-ACTIVATED RECEPTOR 2;
COMPND 4 CHAIN: A;
COMPND 5 SYNONYM: PAR-2,COAGULATION FACTOR II RECEPTOR-LIKE 1,G-PROTEIN
COMPND 6 COUPLED RECEPTOR 11,THROMBIN RECEPTOR-LIKE 1,CYTOCHROME B-562,PAR-2,
COMPND 7 COAGULATION FACTOR II RECEPTOR-LIKE 1,G-PROTEIN COUPLED RECEPTOR 11,
COMPND 8 THROMBIN RECEPTOR-LIKE 1;
COMPND 9 EC: 3.2.1.17;
COMPND 10 ENGINEERED: YES;
COMPND 11 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ENTEROBACTERIA PHAGE T4, HOMO SAPIENS,
SOURCE 3 ESCHERICHIA COLI;
SOURCE 4 ORGANISM_COMMON: HUMAN;
SOURCE 5 ORGANISM_TAXID: 10665, 9606, 562;
SOURCE 6 GENE: E, T4TP126, F2RL1, GPR11, PAR2, CYBC;
SOURCE 7 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 8 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 10 EXPRESSION_SYSTEM_VARIANT: SF9;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PFASTBAC
KEYWDS MEMBRANE PROTEIN, GPCR, 7TM
EXPDTA X-RAY DIFFRACTION
AUTHOR R.K.Y.CHENG,C.FIEZ-VANDAL,O.SCHLENKER,K.EDMAN,B.AGGELER,D.G.BROWN,
AUTHOR 2 G.BROWN,R.M.COOKE,C.E.DUMELIN,A.S.DORE,S.GESCHWINDNER,C.GREBNER,N.-
AUTHOR 3 O.HERMANSSON,A.JAZAYERI,P.JOHANSSON,L.LEONG,R.PRIHANDOKO,M.RAPPAS,
AUTHOR 4 H.SOUTTER,A.SNIJDER,L.SUNDSTROM,B.TEHAN,P.THORNTON,D.TROAST,
AUTHOR 5 G.WIGGIN,A.ZHUKOV,F.H.MARSHALL,N.DEKKER
REVDAT 3 17-JAN-24 5NDZ 1 REMARK
REVDAT 2 17-MAY-17 5NDZ 1 JRNL
REVDAT 1 03-MAY-17 5NDZ 0
JRNL AUTH R.K.Y.CHENG,C.FIEZ-VANDAL,O.SCHLENKER,K.EDMAN,B.AGGELER,
JRNL AUTH 2 D.G.BROWN,G.A.BROWN,R.M.COOKE,C.E.DUMELIN,A.S.DORE,
JRNL AUTH 3 S.GESCHWINDNER,C.GREBNER,N.O.HERMANSSON,A.JAZAYERI,
JRNL AUTH 4 P.JOHANSSON,L.LEONG,R.PRIHANDOKO,M.RAPPAS,H.SOUTTER,
JRNL AUTH 5 A.SNIJDER,L.SUNDSTROM,B.TEHAN,P.THORNTON,D.TROAST,G.WIGGIN,
JRNL AUTH 6 A.ZHUKOV,F.H.MARSHALL,N.DEKKER
JRNL TITL STRUCTURAL INSIGHT INTO ALLOSTERIC MODULATION OF
JRNL TITL 2 PROTEASE-ACTIVATED RECEPTOR 2.
JRNL REF NATURE V. 545 112 2017
JRNL REFN ESSN 1476-4687
JRNL PMID 28445455
JRNL DOI 10.1038/NATURE22309
REMARK 2
REMARK 2 RESOLUTION. 3.60 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.44
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.920
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.0
REMARK 3 NUMBER OF REFLECTIONS : 8135
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.246
REMARK 3 R VALUE (WORKING SET) : 0.244
REMARK 3 FREE R VALUE : 0.291
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.700
REMARK 3 FREE R VALUE TEST SET COUNT : 382
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 34.4428 - 5.1886 0.93 2559 122 0.2127 0.2323
REMARK 3 2 5.1886 - 4.1206 0.94 2578 130 0.2405 0.2883
REMARK 3 3 4.1206 - 3.6003 0.95 2616 130 0.2910 0.3677
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) : 0.640
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.130
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.00
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 4564
REMARK 3 ANGLE : 0.506 6179
REMARK 3 CHIRALITY : 0.035 715
REMARK 3 PLANARITY : 0.004 762
REMARK 3 DIHEDRAL : 11.917 2708
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 5NDZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 09-MAR-17.
REMARK 100 THE DEPOSITION ID IS D_1200003951.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-APR-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5-6.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I24
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.96862
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS 2014
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.3.11
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 8205
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.590
REMARK 200 RESOLUTION RANGE LOW (A) : 34.441
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.2
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.39900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 4.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.59
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.94
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.50
REMARK 200 R MERGE FOR SHELL (I) : 1.18600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.5.6
REMARK 200 STARTING MODEL: 5NDD
REMARK 200
REMARK 200 REMARK: NEEDLE-SHAPED CRYSTALS (ON AVERAGE 0.1MM LONG)
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM CITRATE/CITRATE ACID PH
REMARK 280 5.5-6.2, 0.2 M AMMONIUM PHOSPHATE DIBASIC, 38-43 % (W/V) PEG400,
REMARK 280 PH 5.8, LIPIDIC CUBIC PHASE, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
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: MONOMERIC
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: 27440 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 MET A 979
REMARK 465 VAL A 980
REMARK 465 SER A 981
REMARK 465 ALA A 982
REMARK 465 ILE A 983
REMARK 465 VAL A 984
REMARK 465 LEU A 985
REMARK 465 TYR A 986
REMARK 465 VAL A 987
REMARK 465 LEU A 988
REMARK 465 LEU A 989
REMARK 465 ALA A 990
REMARK 465 ALA A 991
REMARK 465 ALA A 992
REMARK 465 ALA A 993
REMARK 465 HIS A 994
REMARK 465 SER A 995
REMARK 465 ALA A 996
REMARK 465 PHE A 997
REMARK 465 ALA A 998
REMARK 465 ALA A 999
REMARK 465 ALA A 1000
REMARK 465 THR A 1021
REMARK 465 GLU A 1022
REMARK 465 GLY A 1023
REMARK 465 TYR A 1024
REMARK 465 SER A 1036
REMARK 465 PRO A 1037
REMARK 465 SER A 1038
REMARK 465 LEU A 1039
REMARK 465 ASN A 1040
REMARK 465 ALA A 1041
REMARK 465 LEU A 360
REMARK 465 CYS A 361
REMARK 465 ARG A 362
REMARK 465 SER A 363
REMARK 465 VAL A 364
REMARK 465 ARG A 365
REMARK 465 THR A 366
REMARK 465 VAL A 367
REMARK 465 LYS A 368
REMARK 465 GLN A 369
REMARK 465 MET A 370
REMARK 465 GLN A 371
REMARK 465 VAL A 372
REMARK 465 SER A 373
REMARK 465 LEU A 374
REMARK 465 THR A 375
REMARK 465 SER A 376
REMARK 465 LYS A 377
REMARK 465 ALA A 378
REMARK 465 ALA A 379
REMARK 465 ALA A 380
REMARK 465 HIS A 381
REMARK 465 HIS A 382
REMARK 465 HIS A 383
REMARK 465 HIS A 384
REMARK 465 HIS A 385
REMARK 465 HIS A 386
REMARK 465 HIS A 387
REMARK 465 HIS A 388
REMARK 465 HIS A 389
REMARK 465 HIS A 390
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 PHE A1165 O - C - N ANGL. DEV. = 9.9 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 LEU A1033 -61.78 -96.73
REMARK 500 VAL A 76 -50.08 -132.61
REMARK 500 HIS A 137 34.20 -94.30
REMARK 500 PRO A 208 15.03 -69.98
REMARK 500 HIS A 227 -43.70 68.37
REMARK 500 PHE A 251 -66.23 -126.19
REMARK 500 ASN A 277 60.09 -119.71
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A2202 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 121 OD1
REMARK 620 2 ASN A 158 OD1 80.1
REMARK 620 3 SER A 162 OG 156.6 78.0
REMARK 620 4 ASN A 336 OD1 95.6 93.2 93.7
REMARK 620 5 ASP A 340 OD2 75.8 155.9 125.9 88.8
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 8UN A 2201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 2202
DBREF 5NDZ A 1002 1161 UNP D9IEF7 D9IEF7_BPT4 2 161
DBREF 5NDZ A 59 269 UNP P55085 PAR2_HUMAN 59 269
DBREF 5NDZ A 2000 2104 UNP P0ABE7 C562_ECOLX 23 127
DBREF 5NDZ A 276 377 UNP P55085 PAR2_HUMAN 276 377
SEQADV 5NDZ MET A 979 UNP D9IEF7 INITIATING METHIONINE
SEQADV 5NDZ VAL A 980 UNP D9IEF7 EXPRESSION TAG
SEQADV 5NDZ SER A 981 UNP D9IEF7 EXPRESSION TAG
SEQADV 5NDZ ALA A 982 UNP D9IEF7 EXPRESSION TAG
SEQADV 5NDZ ILE A 983 UNP D9IEF7 EXPRESSION TAG
SEQADV 5NDZ VAL A 984 UNP D9IEF7 EXPRESSION TAG
SEQADV 5NDZ LEU A 985 UNP D9IEF7 EXPRESSION TAG
SEQADV 5NDZ TYR A 986 UNP D9IEF7 EXPRESSION TAG
SEQADV 5NDZ VAL A 987 UNP D9IEF7 EXPRESSION TAG
SEQADV 5NDZ LEU A 988 UNP D9IEF7 EXPRESSION TAG
SEQADV 5NDZ LEU A 989 UNP D9IEF7 EXPRESSION TAG
SEQADV 5NDZ ALA A 990 UNP D9IEF7 EXPRESSION TAG
SEQADV 5NDZ ALA A 991 UNP D9IEF7 EXPRESSION TAG
SEQADV 5NDZ ALA A 992 UNP D9IEF7 EXPRESSION TAG
SEQADV 5NDZ ALA A 993 UNP D9IEF7 EXPRESSION TAG
SEQADV 5NDZ HIS A 994 UNP D9IEF7 EXPRESSION TAG
SEQADV 5NDZ SER A 995 UNP D9IEF7 EXPRESSION TAG
SEQADV 5NDZ ALA A 996 UNP D9IEF7 EXPRESSION TAG
SEQADV 5NDZ PHE A 997 UNP D9IEF7 EXPRESSION TAG
SEQADV 5NDZ ALA A 998 UNP D9IEF7 EXPRESSION TAG
SEQADV 5NDZ ALA A 999 UNP D9IEF7 EXPRESSION TAG
SEQADV 5NDZ ALA A 1000 UNP D9IEF7 EXPRESSION TAG
SEQADV 5NDZ SER A 1001 UNP D9IEF7 EXPRESSION TAG
SEQADV 5NDZ THR A 1054 UNP D9IEF7 CYS 54 CONFLICT
SEQADV 5NDZ ALA A 1097 UNP D9IEF7 CYS 97 CONFLICT
SEQADV 5NDZ ILE A 1162 UNP D9IEF7 LINKER
SEQADV 5NDZ TYR A 1163 UNP D9IEF7 LINKER
SEQADV 5NDZ GLU A 1164 UNP D9IEF7 LINKER
SEQADV 5NDZ PHE A 1165 UNP D9IEF7 LINKER
SEQADV 5NDZ ALA A 89 UNP P55085 GLY 89 ENGINEERED MUTATION
SEQADV 5NDZ ALA A 108 UNP P55085 HIS 108 ENGINEERED MUTATION
SEQADV 5NDZ ALA A 157 UNP P55085 GLY 157 ENGINEERED MUTATION
SEQADV 5NDZ LEU A 166 UNP P55085 MET 166 ENGINEERED MUTATION
SEQADV 5NDZ ALA A 174 UNP P55085 TYR 174 ENGINEERED MUTATION
SEQADV 5NDZ GLU A 176 UNP P55085 VAL 176 ENGINEERED MUTATION
SEQADV 5NDZ GLN A 222 UNP P55085 ASN 222 ENGINEERED MUTATION
SEQADV 5NDZ ALA A 268 UNP P55085 MET 268 ENGINEERED MUTATION
SEQADV 5NDZ TRP A 2006 UNP P0ABE7 MET 29 CONFLICT
SEQADV 5NDZ ILE A 2101 UNP P0ABE7 HIS 124 CONFLICT
SEQADV 5NDZ LEU A 2105 UNP P0ABE7 LINKER
SEQADV 5NDZ ALA A 289 UNP P55085 ILE 289 ENGINEERED MUTATION
SEQADV 5NDZ ALA A 293 UNP P55085 LEU 293 ENGINEERED MUTATION
SEQADV 5NDZ ALA A 378 UNP P55085 EXPRESSION TAG
SEQADV 5NDZ ALA A 379 UNP P55085 EXPRESSION TAG
SEQADV 5NDZ ALA A 380 UNP P55085 EXPRESSION TAG
SEQADV 5NDZ HIS A 381 UNP P55085 EXPRESSION TAG
SEQADV 5NDZ HIS A 382 UNP P55085 EXPRESSION TAG
SEQADV 5NDZ HIS A 383 UNP P55085 EXPRESSION TAG
SEQADV 5NDZ HIS A 384 UNP P55085 EXPRESSION TAG
SEQADV 5NDZ HIS A 385 UNP P55085 EXPRESSION TAG
SEQADV 5NDZ HIS A 386 UNP P55085 EXPRESSION TAG
SEQADV 5NDZ HIS A 387 UNP P55085 EXPRESSION TAG
SEQADV 5NDZ HIS A 388 UNP P55085 EXPRESSION TAG
SEQADV 5NDZ HIS A 389 UNP P55085 EXPRESSION TAG
SEQADV 5NDZ HIS A 390 UNP P55085 EXPRESSION TAG
SEQRES 1 A 619 MET VAL SER ALA ILE VAL LEU TYR VAL LEU LEU ALA ALA
SEQRES 2 A 619 ALA ALA HIS SER ALA PHE ALA ALA ALA SER ASN ILE PHE
SEQRES 3 A 619 GLU MET LEU ARG ILE ASP GLU GLY LEU ARG LEU LYS ILE
SEQRES 4 A 619 TYR LYS ASP THR GLU GLY TYR TYR THR ILE GLY ILE GLY
SEQRES 5 A 619 HIS LEU LEU THR LYS SER PRO SER LEU ASN ALA ALA LYS
SEQRES 6 A 619 SER GLU LEU ASP LYS ALA ILE GLY ARG ASN THR ASN GLY
SEQRES 7 A 619 VAL ILE THR LYS ASP GLU ALA GLU LYS LEU PHE ASN GLN
SEQRES 8 A 619 ASP VAL ASP ALA ALA VAL ARG GLY ILE LEU ARG ASN ALA
SEQRES 9 A 619 LYS LEU LYS PRO VAL TYR ASP SER LEU ASP ALA VAL ARG
SEQRES 10 A 619 ARG ALA ALA LEU ILE ASN MET VAL PHE GLN MET GLY GLU
SEQRES 11 A 619 THR GLY VAL ALA GLY PHE THR ASN SER LEU ARG MET LEU
SEQRES 12 A 619 GLN GLN LYS ARG TRP ASP GLU ALA ALA VAL ASN LEU ALA
SEQRES 13 A 619 LYS SER ARG TRP TYR ASN GLN THR PRO ASN ARG ALA LYS
SEQRES 14 A 619 ARG VAL ILE THR THR PHE ARG THR GLY THR TRP ASP ALA
SEQRES 15 A 619 TYR ILE TYR GLU PHE PHE SER VAL ASP GLU PHE SER ALA
SEQRES 16 A 619 SER VAL LEU THR GLY LYS LEU THR THR VAL PHE LEU PRO
SEQRES 17 A 619 ILE VAL TYR THR ILE VAL PHE VAL VAL ALA LEU PRO SER
SEQRES 18 A 619 ASN GLY MET ALA LEU TRP VAL PHE LEU PHE ARG THR LYS
SEQRES 19 A 619 LYS LYS ALA PRO ALA VAL ILE TYR MET ALA ASN LEU ALA
SEQRES 20 A 619 LEU ALA ASP LEU LEU SER VAL ILE TRP PHE PRO LEU LYS
SEQRES 21 A 619 ILE ALA TYR HIS ILE HIS GLY ASN ASN TRP ILE TYR GLY
SEQRES 22 A 619 GLU ALA LEU CYS ASN VAL LEU ILE GLY PHE PHE TYR ALA
SEQRES 23 A 619 ASN MET TYR CYS SER ILE LEU PHE LEU THR CYS LEU SER
SEQRES 24 A 619 VAL GLN ARG ALA TRP GLU ILE VAL ASN PRO MET GLY HIS
SEQRES 25 A 619 SER ARG LYS LYS ALA ASN ILE ALA ILE GLY ILE SER LEU
SEQRES 26 A 619 ALA ILE TRP LEU LEU ILE LEU LEU VAL THR ILE PRO LEU
SEQRES 27 A 619 TYR VAL VAL LYS GLN THR ILE PHE ILE PRO ALA LEU GLN
SEQRES 28 A 619 ILE THR THR CYS HIS ASP VAL LEU PRO GLU GLN LEU LEU
SEQRES 29 A 619 VAL GLY ASP MET PHE ASN TYR PHE LEU SER LEU ALA ILE
SEQRES 30 A 619 GLY VAL PHE LEU PHE PRO ALA PHE LEU THR ALA SER ALA
SEQRES 31 A 619 TYR VAL LEU MET ILE ARG ALA LEU ALA ASP LEU GLU ASP
SEQRES 32 A 619 ASN TRP GLU THR LEU ASN ASP ASN LEU LYS VAL ILE GLU
SEQRES 33 A 619 LYS ALA ASP ASN ALA ALA GLN VAL LYS ASP ALA LEU THR
SEQRES 34 A 619 LYS MET ARG ALA ALA ALA LEU ASP ALA GLN LYS ALA THR
SEQRES 35 A 619 PRO PRO LYS LEU GLU ASP LYS SER PRO ASP SER PRO GLU
SEQRES 36 A 619 MET LYS ASP PHE ARG HIS GLY PHE ASP ILE LEU VAL GLY
SEQRES 37 A 619 GLN ILE ASP ASP ALA LEU LYS LEU ALA ASN GLU GLY LYS
SEQRES 38 A 619 VAL LYS GLU ALA GLN ALA ALA ALA GLU GLN LEU LYS THR
SEQRES 39 A 619 THR ARG ASN ALA TYR ILE GLN LYS TYR LEU GLU ASN SER
SEQRES 40 A 619 GLU LYS LYS ARG LYS ARG ALA ILE LYS LEU ALA VAL THR
SEQRES 41 A 619 VAL ALA ALA MET TYR LEU ILE CYS PHE THR PRO SER ASN
SEQRES 42 A 619 LEU LEU LEU VAL VAL HIS TYR PHE LEU ILE LYS SER GLN
SEQRES 43 A 619 GLY GLN SER HIS VAL TYR ALA LEU TYR ILE VAL ALA LEU
SEQRES 44 A 619 CYS LEU SER THR LEU ASN SER CYS ILE ASP PRO PHE VAL
SEQRES 45 A 619 TYR TYR PHE VAL SER HIS ASP PHE ARG ASP HIS ALA LYS
SEQRES 46 A 619 ASN ALA LEU LEU CYS ARG SER VAL ARG THR VAL LYS GLN
SEQRES 47 A 619 MET GLN VAL SER LEU THR SER LYS ALA ALA ALA HIS HIS
SEQRES 48 A 619 HIS HIS HIS HIS HIS HIS HIS HIS
HET 8UN A2201 38
HET NA A2202 1
HETNAM 8UN 2-(6-BROMANYL-1,3-BENZODIOXOL-5-YL)-~{N}-(4-
HETNAM 2 8UN CYANOPHENYL)-1-[(1~{S})-1-
HETNAM 3 8UN CYCLOHEXYLETHYL]BENZIMIDAZOLE-5-CARBOXAMIDE
HETNAM NA SODIUM ION
FORMUL 2 8UN C30 H27 BR N4 O3
FORMUL 3 NA NA 1+
FORMUL 4 HOH *2(H2 O)
HELIX 1 AA1 SER A 1001 GLY A 1012 1 12
HELIX 2 AA2 LYS A 1043 GLY A 1051 1 9
HELIX 3 AA3 THR A 1059 ASN A 1081 1 23
HELIX 4 AA4 LEU A 1084 LEU A 1091 1 8
HELIX 5 AA5 ASP A 1092 GLY A 1113 1 22
HELIX 6 AA6 PHE A 1114 GLN A 1123 1 10
HELIX 7 AA7 ARG A 1125 LYS A 1135 1 11
HELIX 8 AA8 SER A 1136 THR A 1142 1 7
HELIX 9 AA9 THR A 1142 GLY A 1156 1 15
HELIX 10 AB1 TRP A 1158 TYR A 1163 1 6
HELIX 11 AB2 ASP A 62 LEU A 69 1 8
HELIX 12 AB3 GLY A 71 VAL A 76 1 6
HELIX 13 AB4 VAL A 76 ARG A 103 1 28
HELIX 14 AB5 ALA A 108 ILE A 126 1 19
HELIX 15 AB6 TRP A 127 HIS A 137 1 11
HELIX 16 AB7 GLY A 144 ASN A 179 1 36
HELIX 17 AB8 ARG A 185 THR A 206 1 22
HELIX 18 AB9 THR A 206 VAL A 211 1 6
HELIX 19 AC1 GLU A 232 LEU A 234 5 3
HELIX 20 AC2 LEU A 235 VAL A 250 1 16
HELIX 21 AC3 PHE A 251 GLU A 2017 1 37
HELIX 22 AC4 ASN A 2021 ALA A 2042 1 22
HELIX 23 AC5 SER A 2054 GLU A 2080 1 27
HELIX 24 AC6 LYS A 2082 ILE A 2101 1 20
HELIX 25 AC7 ILE A 2101 GLU A 276 1 6
HELIX 26 AC8 SER A 278 CYS A 299 1 22
HELIX 27 AC9 PHE A 300 GLN A 317 1 18
HELIX 28 AD1 VAL A 322 THR A 334 1 13
HELIX 29 AD2 LEU A 335 SER A 348 1 14
HELIX 30 AD3 SER A 348 LEU A 359 1 12
SHEET 1 AA1 3 ARG A1014 TYR A1018 0
SHEET 2 AA1 3 THR A1026 GLY A1028 -1 O GLY A1028 N ARG A1014
SHEET 3 AA1 3 HIS A1031 LEU A1032 -1 O HIS A1031 N ILE A1027
SHEET 1 AA2 2 THR A 215 PHE A 217 0
SHEET 2 AA2 2 THR A 224 CYS A 226 -1 O THR A 225 N ILE A 216
SSBOND 1 CYS A 148 CYS A 226 1555 1555 2.03
LINK OD1 ASP A 121 NA NA A2202 1555 1555 2.24
LINK OD1 ASN A 158 NA NA A2202 1555 1555 2.58
LINK OG SER A 162 NA NA A2202 1555 1555 2.29
LINK OD1 ASN A 336 NA NA A2202 1555 1555 2.40
LINK OD2 ASP A 340 NA NA A2202 1555 1555 2.51
SITE 1 AC1 11 VAL A 76 ALA A 120 LEU A 123 PHE A 154
SITE 2 AC1 11 ALA A 157 ASN A 158 CYS A 161 TRP A 199
SITE 3 AC1 11 LEU A 203 TYR A 210 VAL A 211
SITE 1 AC2 5 ASP A 121 ASN A 158 SER A 162 ASN A 336
SITE 2 AC2 5 ASP A 340
CRYST1 37.099 62.599 86.467 104.38 91.66 96.40 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 0.026955 0.003023 0.001601 0.00000
SCALE2 0.000000 0.016075 0.004209 0.00000
SCALE3 0.000000 0.000000 0.011960 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
