HEADER TRANSFERASE 31-MAR-17 5NKA
TITLE CRYSTAL STRUCTURE OF EPHRIN A2 (EPHA2) RECEPTOR PROTEIN KINASE WITH
TITLE 2 COMPOUND 2G
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EPHRIN TYPE-A RECEPTOR 2;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: EPITHELIAL CELL KINASE,TYROSINE-PROTEIN KINASE RECEPTOR ECK;
COMPND 5 EC: 2.7.10.1;
COMPND 6 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: EPHA2, ECK;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS INHIBITOR, COMPLEX, PROTEIN TYROSINE KINASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.KUDLINZKI,V.L.LINHARD,K.WITT,S.L.GANDE,K.SAXENA,S.HEINZLMEIR,
AUTHOR 2 G.MEDARD,B.KUESTER,H.SCHWALBE
REVDAT 5 17-JAN-24 5NKA 1 REMARK
REVDAT 4 14-AUG-19 5NKA 1 REMARK
REVDAT 3 12-JUN-19 5NKA 1 AUTHOR
REVDAT 2 28-JUN-17 5NKA 1 JRNL
REVDAT 1 07-JUN-17 5NKA 0
JRNL AUTH S.HEINZLMEIR,J.LOHSE,T.TREIBER,D.KUDLINZKI,V.LINHARD,
JRNL AUTH 2 S.L.GANDE,S.SREERAMULU,K.SAXENA,X.LIU,M.WILHELM,H.SCHWALBE,
JRNL AUTH 3 B.KUSTER,G.MEDARD
JRNL TITL CHEMOPROTEOMICS-AIDED MEDICINAL CHEMISTRY FOR THE DISCOVERY
JRNL TITL 2 OF EPHA2 INHIBITORS.
JRNL REF CHEMMEDCHEM V. 12 999 2017
JRNL REFN ESSN 1860-7187
JRNL PMID 28544567
JRNL DOI 10.1002/CMDC.201700217
REMARK 2
REMARK 2 RESOLUTION. 1.38 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) : 1.38
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.60
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.400
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 54903
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.161
REMARK 3 R VALUE (WORKING SET) : 0.160
REMARK 3 FREE R VALUE : 0.182
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.830
REMARK 3 FREE R VALUE TEST SET COUNT : 2101
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 39.6180 - 3.3961 0.99 3597 144 0.1509 0.1688
REMARK 3 2 3.3961 - 2.6958 0.99 3543 141 0.1468 0.1502
REMARK 3 3 2.6958 - 2.3551 1.00 3559 141 0.1467 0.1707
REMARK 3 4 2.3551 - 2.1398 1.00 3578 142 0.1500 0.1621
REMARK 3 5 2.1398 - 1.9864 0.99 3514 140 0.1450 0.1914
REMARK 3 6 1.9864 - 1.8693 1.00 3586 143 0.1526 0.1970
REMARK 3 7 1.8693 - 1.7757 0.99 3526 140 0.1583 0.1935
REMARK 3 8 1.7757 - 1.6984 0.99 3537 141 0.1640 0.2099
REMARK 3 9 1.6984 - 1.6330 0.99 3496 139 0.1677 0.1885
REMARK 3 10 1.6330 - 1.5766 0.99 3519 140 0.1791 0.2099
REMARK 3 11 1.5766 - 1.5273 0.99 3520 140 0.1921 0.2037
REMARK 3 12 1.5273 - 1.4837 0.99 3474 138 0.2079 0.2182
REMARK 3 13 1.4837 - 1.4446 0.99 3554 141 0.2251 0.2693
REMARK 3 14 1.4446 - 1.4094 0.98 3470 138 0.2579 0.2715
REMARK 3 15 1.4094 - 1.3773 0.94 3329 133 0.2710 0.2791
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) : 0.160
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.180
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 21.95
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 : 0.016 2349
REMARK 3 ANGLE : 1.591 3178
REMARK 3 CHIRALITY : 0.124 340
REMARK 3 PLANARITY : 0.010 404
REMARK 3 DIHEDRAL : 21.544 931
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 5NKA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 31-MAR-17.
REMARK 100 THE DEPOSITION ID IS D_1200004088.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JUN-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PETRA III, EMBL C/O DESY
REMARK 200 BEAMLINE : P13 (MX1)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.03320
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS XDSAPP 2.0
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 54909
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.377
REMARK 200 RESOLUTION RANGE LOW (A) : 39.602
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : 6.690
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.8100
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.38
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.46
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.8
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 : 2.310
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: 5I9U
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.23
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.99
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 37.5% MPD/PEG1000/PEG3350 (MD), 0.25 M
REMARK 280 AMINO ACIDS MIX (MD), 0.1 M BUFFER SYSTEM 3 (MD) PH8.5, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 53.02050
REMARK 290 SMTRY3 2 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: 210 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14190 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 3.0 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 595
REMARK 465 ASP A 596
REMARK 465 PRO A 597
REMARK 465 ASN A 598
REMARK 465 GLN A 599
REMARK 465 ALA A 600
REMARK 465 VAL A 601
REMARK 465 LEU A 602
REMARK 465 LYS A 603
REMARK 465 PHE A 604
REMARK 465 LEU A 760
REMARK 465 SER A 761
REMARK 465 ARG A 762
REMARK 465 VAL A 763
REMARK 465 LEU A 764
REMARK 465 GLU A 765
REMARK 465 ASP A 766
REMARK 465 ASP A 767
REMARK 465 PRO A 768
REMARK 465 GLU A 769
REMARK 465 ALA A 770
REMARK 465 THR A 771
REMARK 465 TYR A 772
REMARK 465 THR A 773
REMARK 465 THR A 774
REMARK 465 SER A 775
REMARK 465 GLY A 776
REMARK 465 GLY A 777
REMARK 465 PRO A 889
REMARK 465 ARG A 890
REMARK 465 PRO A 896
REMARK 465 SER A 897
REMARK 465 THR A 898
REMARK 465 SER A 899
REMARK 465 GLY A 900
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 HOH A 1263 O HOH A 1296 2.16
REMARK 500 OE1 GLN A 856 O HOH A 1101 2.17
REMARK 500 O HOH A 1201 O HOH A 1253 2.18
REMARK 500
REMARK 500 REMARK: NULL
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 O HOH A 1253 O HOH A 1307 1655 2.02
REMARK 500 O HOH A 1325 O HOH A 1326 1455 2.02
REMARK 500 O HOH A 1175 O HOH A 1214 1455 2.19
REMARK 500
REMARK 500 REMARK: NULL
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 ASP A 757 CB - CG - OD2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 ASP A 799 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ARG A 835 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG A 861 NE - CZ - NH1 ANGL. DEV. = 5.2 DEGREES
REMARK 500 ARG A 861 NE - CZ - NH2 ANGL. DEV. = -4.5 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 ARG A 738 -12.19 74.19
REMARK 500 ASP A 757 76.50 59.60
REMARK 500 ASP A 757 76.50 53.69
REMARK 500 TRP A 819 -129.01 52.41
REMARK 500 ARG A 894 -57.96 -142.19
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 91H A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 1002
DBREF 5NKA A 596 900 UNP P29317 EPHA2_HUMAN 596 900
SEQADV 5NKA GLY A 595 UNP P29317 EXPRESSION TAG
SEQRES 1 A 306 GLY ASP PRO ASN GLN ALA VAL LEU LYS PHE THR THR GLU
SEQRES 2 A 306 ILE HIS PRO SER CYS VAL THR ARG GLN LYS VAL ILE GLY
SEQRES 3 A 306 ALA GLY GLU PHE GLY GLU VAL TYR LYS GLY MET LEU LYS
SEQRES 4 A 306 THR SER SER GLY LYS LYS GLU VAL PRO VAL ALA ILE LYS
SEQRES 5 A 306 THR LEU LYS ALA GLY TYR THR GLU LYS GLN ARG VAL ASP
SEQRES 6 A 306 PHE LEU GLY GLU ALA GLY ILE MET GLY GLN PHE SER HIS
SEQRES 7 A 306 HIS ASN ILE ILE ARG LEU GLU GLY VAL ILE SER LYS TYR
SEQRES 8 A 306 LYS PRO MET MET ILE ILE THR GLU TYR MET GLU ASN GLY
SEQRES 9 A 306 ALA LEU ASP LYS PHE LEU ARG GLU LYS ASP GLY GLU PHE
SEQRES 10 A 306 SER VAL LEU GLN LEU VAL GLY MET LEU ARG GLY ILE ALA
SEQRES 11 A 306 ALA GLY MET LYS TYR LEU ALA ASN MET ASN TYR VAL HIS
SEQRES 12 A 306 ARG ASP LEU ALA ALA ARG ASN ILE LEU VAL ASN SER ASN
SEQRES 13 A 306 LEU VAL CYS LYS VAL SER ASP PHE GLY LEU SER ARG VAL
SEQRES 14 A 306 LEU GLU ASP ASP PRO GLU ALA THR TYR THR THR SER GLY
SEQRES 15 A 306 GLY LYS ILE PRO ILE ARG TRP THR ALA PRO GLU ALA ILE
SEQRES 16 A 306 SER TYR ARG LYS PHE THR SER ALA SER ASP VAL TRP SER
SEQRES 17 A 306 PHE GLY ILE VAL MET TRP GLU VAL MET THR TYR GLY GLU
SEQRES 18 A 306 ARG PRO TYR TRP GLU LEU SER ASN HIS GLU VAL MET LYS
SEQRES 19 A 306 ALA ILE ASN ASP GLY PHE ARG LEU PRO THR PRO MET ASP
SEQRES 20 A 306 CYS PRO SER ALA ILE TYR GLN LEU MET MET GLN CYS TRP
SEQRES 21 A 306 GLN GLN GLU ARG ALA ARG ARG PRO LYS PHE ALA ASP ILE
SEQRES 22 A 306 VAL SER ILE LEU ASP LYS LEU ILE ARG ALA PRO ASP SER
SEQRES 23 A 306 LEU LYS THR LEU ALA ASP PHE ASP PRO ARG VAL SER ILE
SEQRES 24 A 306 ARG LEU PRO SER THR SER GLY
HET 91H A1001 70
HET EDO A1002 4
HETNAM 91H 4-[[3-[[5-[(2-CHLORANYL-6-METHYL-PHENYL)CARBAMOYL]-1,3-
HETNAM 2 91H THIAZOL-2-YL]AMINO]PHENYL]CARBONYLAMINO]CYCLOHEXANE-1-
HETNAM 3 91H CARBOXYLIC ACID
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 91H C25 H25 CL N4 O4 S
FORMUL 3 EDO C2 H6 O2
FORMUL 4 HOH *227(H2 O)
HELIX 1 AA1 HIS A 609 SER A 611 5 3
HELIX 2 AA2 SER A 635 LYS A 638 5 4
HELIX 3 AA3 THR A 653 GLY A 668 1 16
HELIX 4 AA4 ALA A 699 LYS A 707 1 9
HELIX 5 AA5 SER A 712 MET A 733 1 22
HELIX 6 AA6 ALA A 741 ARG A 743 5 3
HELIX 7 AA7 PRO A 780 THR A 784 5 5
HELIX 8 AA8 ALA A 785 ARG A 792 1 8
HELIX 9 AA9 THR A 795 THR A 812 1 18
HELIX 10 AB1 SER A 822 ASP A 832 1 11
HELIX 11 AB2 PRO A 843 TRP A 854 1 12
HELIX 12 AB3 GLU A 857 ARG A 861 5 5
HELIX 13 AB4 LYS A 863 ALA A 877 1 15
HELIX 14 AB5 PRO A 878 THR A 883 5 6
SHEET 1 AA1 5 VAL A 613 ALA A 621 0
SHEET 2 AA1 5 GLU A 626 THR A 634 -1 O VAL A 627 N ILE A 619
SHEET 3 AA1 5 LYS A 639 LEU A 648 -1 O ILE A 645 N TYR A 628
SHEET 4 AA1 5 MET A 688 GLU A 693 -1 O ILE A 690 N LYS A 646
SHEET 5 AA1 5 LEU A 678 ILE A 682 -1 N GLY A 680 O ILE A 691
SHEET 1 AA2 2 ILE A 745 VAL A 747 0
SHEET 2 AA2 2 CYS A 753 VAL A 755 -1 O LYS A 754 N LEU A 746
CISPEP 1 LYS A 686 PRO A 687 0 1.59
SITE 1 AC1 16 LYS A 617 ILE A 619 ALA A 644 LYS A 646
SITE 2 AC1 16 GLU A 663 ILE A 690 THR A 692 GLU A 693
SITE 3 AC1 16 TYR A 694 MET A 695 GLU A 696 GLY A 698
SITE 4 AC1 16 LEU A 746 SER A 756 HOH A1123 HOH A1247
SITE 1 AC2 6 ASN A 732 GLU A 815 LYS A 863 PHE A 864
SITE 2 AC2 6 ALA A 865 HOH A1120
CRYST1 32.685 106.041 39.689 90.00 93.80 90.00 P 1 21 1 2
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 0.030595 0.000000 0.002034 0.00000
SCALE2 0.000000 0.009430 0.000000 0.00000
SCALE3 0.000000 0.000000 0.025252 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
