HEADER HYDROLASE 03-SEP-10 3OQK
TITLE CRYSTAL STRUCTURE ANALYSIS OF RENIN-INDOLE-PIPERAZIN INHIBITOR
TITLE 2 COMPLEXES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RENIN;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 67-406;
COMPND 5 SYNONYM: ANGIOTENSINOGENASE;
COMPND 6 EC: 3.4.23.15;
COMPND 7 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: REN;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: HUMAN EMBRYONIC KIDNEY CELL (CRL-1573)
KEYWDS RENIN HUMAN, ASPARTYL PROTEASE, RENIN INHIBITION, HYPERTENSION,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Z.BOCSKEI
REVDAT 3 29-JUL-20 3OQK 1 COMPND REMARK HETNAM LINK
REVDAT 3 2 1 SITE
REVDAT 2 08-NOV-17 3OQK 1 REMARK
REVDAT 1 27-OCT-10 3OQK 0
JRNL AUTH B.SCHEIPER,H.MATTER,H.STEINHAGEN,U.STILZ,Z.BOCSKEI,V.FLEURY,
JRNL AUTH 2 G.MCCORT
JRNL TITL DISCOVERY AND OPTIMIZATION OF A NEW CLASS OF POTENT AND
JRNL TITL 2 NON-CHIRAL INDOLE-3-CARBOXAMIDE-BASED RENIN INHIBITORS.
JRNL REF BIOORG.MED.CHEM.LETT. V. 20 6268 2010
JRNL REFN ISSN 0960-894X
JRNL PMID 20850300
JRNL DOI 10.1016/J.BMCL.2010.08.092
REMARK 2
REMARK 2 RESOLUTION. 2.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER-TNT
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SMART,VONRHEIN,WOMACK,
REMARK 3 : MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.99
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 21100
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.224
REMARK 3 R VALUE (WORKING SET) : 0.222
REMARK 3 FREE R VALUE : 0.253
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.120
REMARK 3 FREE R VALUE TEST SET COUNT : 1081
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 11
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 3.04
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.80
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2759
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2349
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2611
REMARK 3 BIN R VALUE (WORKING SET) : 0.2331
REMARK 3 BIN FREE R VALUE : 0.2658
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.36
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 148
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5196
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 94
REMARK 3 SOLVENT ATOMS : 144
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 78.66
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.390
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.914
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.895
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 5425 ; 2.000 ; NULL
REMARK 3 BOND ANGLES : 7367 ; 2.000 ; NULL
REMARK 3 TORSION ANGLES : 1798 ; 2.000 ; NULL
REMARK 3 TRIGONAL CARBON PLANES : 118 ; 2.000 ; NULL
REMARK 3 GENERAL PLANES : 798 ; 5.000 ; NULL
REMARK 3 ISOTROPIC THERMAL FACTORS : 5425 ; 20.000 ; NULL
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 716 ; 5.000 ; NULL
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 6165 ; 4.000 ; NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.14
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 4.35
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 17.85
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: POSITION OF WATER MOLECULES WERE TAKEN
REMARK 3 FROM A HIGHER RESOLUTION STRUCTURE (2.05 A). WATERS WERE REFINED
REMARK 3 AND RETAINED ONLY IF THE ISOTROPIC DISPLACEMENT PARAMETER
REMARK 3 REMAINED BELOW 80 A**2
REMARK 4
REMARK 4 3OQK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-SEP-10.
REMARK 100 THE DEPOSITION ID IS D_1000061448.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-FEB-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RUH3R
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : OSMIC BLUEMIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21155
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
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 (%) : 100.0
REMARK 200 DATA REDUNDANCY : 6.100
REMARK 200 R MERGE (I) : 0.06300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.10
REMARK 200 R MERGE FOR SHELL (I) : 0.69700
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: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.42
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.19
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.05M CITRATE PH=4.5, 10-12% PEG3350,
REMARK 280 0.6M NACL, 20 MG/ML RENIN, VAPOUR DIFFUSION, HANGING DROP,
REMARK 280 HANGING DROP, TEMPERATURE 298K, PH 4.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 3
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 5555 Z,X,Y
REMARK 290 6555 Z+1/2,-X+1/2,-Y
REMARK 290 7555 -Z+1/2,-X,Y+1/2
REMARK 290 8555 -Z,X+1/2,-Y+1/2
REMARK 290 9555 Y,Z,X
REMARK 290 10555 -Y,Z+1/2,-X+1/2
REMARK 290 11555 Y+1/2,-Z+1/2,-X
REMARK 290 12555 -Y+1/2,-Z,X+1/2
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 70.69350
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 70.69350
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 70.69350
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 70.69350
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 70.69350
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 70.69350
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 70.69350
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 70.69350
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 70.69350
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 70.69350
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 70.69350
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 70.69350
REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 70.69350
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 70.69350
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 70.69350
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 70.69350
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 70.69350
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 70.69350
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 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 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 LEU A -5
REMARK 465 THR A -4
REMARK 465 LEU A -3
REMARK 465 LEU B -5
REMARK 465 THR B -4
REMARK 465 LEU B -3
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 ASN A 67 -65.09 -138.60
REMARK 500 ASP A 149 49.99 -84.27
REMARK 500 GLU A 160 -94.29 -78.99
REMARK 500 LEU A 161 109.83 85.02
REMARK 500 ASP A 208 10.71 85.23
REMARK 500 ARG A 240 -169.30 -121.57
REMARK 500 ALA A 285 37.37 -87.91
REMARK 500 ASN B 67 -64.06 -138.72
REMARK 500 ASP B 149 47.97 -79.52
REMARK 500 ASP B 158 89.82 38.01
REMARK 500 ASP B 208 9.49 87.71
REMARK 500 ARG B 240 -70.75 -69.74
REMARK 500 LEU B 242 -52.13 -134.88
REMARK 500 ALA B 285 39.82 -87.90
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3OOT RELATED DB: PDB
REMARK 900 RELATED ID: 3OQF RELATED DB: PDB
DBREF 3OQK A -5 326 UNP P00797 RENI_HUMAN 67 406
DBREF 3OQK B -5 326 UNP P00797 RENI_HUMAN 67 406
SEQRES 1 A 340 LEU THR LEU GLY ASN THR THR SER SER VAL ILE LEU THR
SEQRES 2 A 340 ASN TYR MET ASP THR GLN TYR TYR GLY GLU ILE GLY ILE
SEQRES 3 A 340 GLY THR PRO PRO GLN THR PHE LYS VAL VAL PHE ASP THR
SEQRES 4 A 340 GLY SER SER ASN VAL TRP VAL PRO SER SER LYS CYS SER
SEQRES 5 A 340 ARG LEU TYR THR ALA CYS VAL TYR HIS LYS LEU PHE ASP
SEQRES 6 A 340 ALA SER ASP SER SER SER TYR LYS HIS ASN GLY THR GLU
SEQRES 7 A 340 LEU THR LEU ARG TYR SER THR GLY THR VAL SER GLY PHE
SEQRES 8 A 340 LEU SER GLN ASP ILE ILE THR VAL GLY GLY ILE THR VAL
SEQRES 9 A 340 THR GLN MET PHE GLY GLU VAL THR GLU MET PRO ALA LEU
SEQRES 10 A 340 PRO PHE MET LEU ALA GLU PHE ASP GLY VAL VAL GLY MET
SEQRES 11 A 340 GLY PHE ILE GLU GLN ALA ILE GLY ARG VAL THR PRO ILE
SEQRES 12 A 340 PHE ASP ASN ILE ILE SER GLN GLY VAL LEU LYS GLU ASP
SEQRES 13 A 340 VAL PHE SER PHE TYR TYR ASN ARG ASP SER GLU ASN SER
SEQRES 14 A 340 GLN SER LEU GLY GLY GLN ILE VAL LEU GLY GLY SER ASP
SEQRES 15 A 340 PRO GLN HIS TYR GLU GLY ASN PHE HIS TYR ILE ASN LEU
SEQRES 16 A 340 ILE LYS THR GLY VAL TRP GLN ILE GLN MET LYS GLY VAL
SEQRES 17 A 340 SER VAL GLY SER SER THR LEU LEU CYS GLU ASP GLY CYS
SEQRES 18 A 340 LEU ALA LEU VAL ASP THR GLY ALA SER TYR ILE SER GLY
SEQRES 19 A 340 SER THR SER SER ILE GLU LYS LEU MET GLU ALA LEU GLY
SEQRES 20 A 340 ALA LYS LYS ARG LEU PHE ASP TYR VAL VAL LYS CYS ASN
SEQRES 21 A 340 GLU GLY PRO THR LEU PRO ASP ILE SER PHE HIS LEU GLY
SEQRES 22 A 340 GLY LYS GLU TYR THR LEU THR SER ALA ASP TYR VAL PHE
SEQRES 23 A 340 GLN GLU SER TYR SER SER LYS LYS LEU CYS THR LEU ALA
SEQRES 24 A 340 ILE HIS ALA MET ASP ILE PRO PRO PRO THR GLY PRO THR
SEQRES 25 A 340 TRP ALA LEU GLY ALA THR PHE ILE ARG LYS PHE TYR THR
SEQRES 26 A 340 GLU PHE ASP ARG ARG ASN ASN ARG ILE GLY PHE ALA LEU
SEQRES 27 A 340 ALA ARG
SEQRES 1 B 340 LEU THR LEU GLY ASN THR THR SER SER VAL ILE LEU THR
SEQRES 2 B 340 ASN TYR MET ASP THR GLN TYR TYR GLY GLU ILE GLY ILE
SEQRES 3 B 340 GLY THR PRO PRO GLN THR PHE LYS VAL VAL PHE ASP THR
SEQRES 4 B 340 GLY SER SER ASN VAL TRP VAL PRO SER SER LYS CYS SER
SEQRES 5 B 340 ARG LEU TYR THR ALA CYS VAL TYR HIS LYS LEU PHE ASP
SEQRES 6 B 340 ALA SER ASP SER SER SER TYR LYS HIS ASN GLY THR GLU
SEQRES 7 B 340 LEU THR LEU ARG TYR SER THR GLY THR VAL SER GLY PHE
SEQRES 8 B 340 LEU SER GLN ASP ILE ILE THR VAL GLY GLY ILE THR VAL
SEQRES 9 B 340 THR GLN MET PHE GLY GLU VAL THR GLU MET PRO ALA LEU
SEQRES 10 B 340 PRO PHE MET LEU ALA GLU PHE ASP GLY VAL VAL GLY MET
SEQRES 11 B 340 GLY PHE ILE GLU GLN ALA ILE GLY ARG VAL THR PRO ILE
SEQRES 12 B 340 PHE ASP ASN ILE ILE SER GLN GLY VAL LEU LYS GLU ASP
SEQRES 13 B 340 VAL PHE SER PHE TYR TYR ASN ARG ASP SER GLU ASN SER
SEQRES 14 B 340 GLN SER LEU GLY GLY GLN ILE VAL LEU GLY GLY SER ASP
SEQRES 15 B 340 PRO GLN HIS TYR GLU GLY ASN PHE HIS TYR ILE ASN LEU
SEQRES 16 B 340 ILE LYS THR GLY VAL TRP GLN ILE GLN MET LYS GLY VAL
SEQRES 17 B 340 SER VAL GLY SER SER THR LEU LEU CYS GLU ASP GLY CYS
SEQRES 18 B 340 LEU ALA LEU VAL ASP THR GLY ALA SER TYR ILE SER GLY
SEQRES 19 B 340 SER THR SER SER ILE GLU LYS LEU MET GLU ALA LEU GLY
SEQRES 20 B 340 ALA LYS LYS ARG LEU PHE ASP TYR VAL VAL LYS CYS ASN
SEQRES 21 B 340 GLU GLY PRO THR LEU PRO ASP ILE SER PHE HIS LEU GLY
SEQRES 22 B 340 GLY LYS GLU TYR THR LEU THR SER ALA ASP TYR VAL PHE
SEQRES 23 B 340 GLN GLU SER TYR SER SER LYS LYS LEU CYS THR LEU ALA
SEQRES 24 B 340 ILE HIS ALA MET ASP ILE PRO PRO PRO THR GLY PRO THR
SEQRES 25 B 340 TRP ALA LEU GLY ALA THR PHE ILE ARG LYS PHE TYR THR
SEQRES 26 B 340 GLU PHE ASP ARG ARG ASN ASN ARG ILE GLY PHE ALA LEU
SEQRES 27 B 340 ALA ARG
MODRES 3OQK ASN B 67 ASN GLYCOSYLATION SITE
MODRES 3OQK ASN A 67 ASN GLYCOSYLATION SITE
HET NAG A 367 14
HET S52 A 327 30
HET NAG B 367 14
HET S52 B 327 30
HET GOL B 328 6
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM S52 2-PHENOXY-1-PHENYL-3-(PIPERAZIN-1-YLCARBONYL)-1H-INDOLE
HETNAM GOL GLYCEROL
HETSYN S52 (2-PHENOXY-1-PHENYL-1H-INDOL-3-YL)-PIPERAZIN-1-YL-
HETSYN 2 S52 METHANONE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 NAG 2(C8 H15 N O6)
FORMUL 4 S52 2(C25 H23 N3 O2)
FORMUL 7 GOL C3 H8 O3
FORMUL 8 HOH *144(H2 O)
HELIX 1 1 TYR A 47 HIS A 53 1 7
HELIX 2 2 ASP A 57 SER A 61 5 5
HELIX 3 3 PRO A 108 MET A 113 1 6
HELIX 4 4 PHE A 125 VAL A 133 5 9
HELIX 5 5 PRO A 135 GLN A 143 1 9
HELIX 6 6 ASP A 171 GLN A 173 5 3
HELIX 7 7 SER A 224 GLY A 236 1 13
HELIX 8 8 ASN A 250 LEU A 255 5 6
HELIX 9 9 THR A 270 VAL A 275 1 6
HELIX 10 10 GLY A 302 LYS A 308 1 7
HELIX 11 11 TYR B 47 HIS B 53 1 7
HELIX 12 12 ASP B 57 SER B 61 5 5
HELIX 13 13 PRO B 108 MET B 113 1 6
HELIX 14 14 PHE B 125 VAL B 133 5 9
HELIX 15 15 PRO B 135 GLN B 143 1 9
HELIX 16 16 ASP B 171 GLN B 173 5 3
HELIX 17 17 SER B 224 GLY B 236 1 13
HELIX 18 18 ASN B 250 LEU B 255 5 6
HELIX 19 19 THR B 270 VAL B 275 1 6
HELIX 20 20 GLY B 302 LYS B 308 1 7
SHEET 1 A 9 LYS A 65 ARG A 74 0
SHEET 2 A 9 THR A 79 VAL A 91 -1 O VAL A 80 N LEU A 73
SHEET 3 A 9 GLN A 13 ILE A 20 -1 N GLY A 19 O THR A 90
SHEET 4 A 9 SER A 2 TYR A 9 -1 N TYR A 9 O GLN A 13
SHEET 5 A 9 GLY A 163 LEU A 167 -1 O LEU A 167 N SER A 2
SHEET 6 A 9 VAL A 150 TYR A 155 -1 N TYR A 154 O GLN A 164
SHEET 7 A 9 PHE A 309 ASP A 314 -1 O PHE A 313 N PHE A 151
SHEET 8 A 9 ARG A 319 ALA A 325 -1 O GLY A 321 N GLU A 312
SHEET 9 A 9 TYR A 175 ASN A 183 -1 N ILE A 182 O ILE A 320
SHEET 1 B13 LYS A 65 ARG A 74 0
SHEET 2 B13 THR A 79 VAL A 91 -1 O VAL A 80 N LEU A 73
SHEET 3 B13 ILE A 94 GLU A 106 -1 O VAL A 96 N ILE A 89
SHEET 4 B13 VAL A 38 PRO A 41 1 N VAL A 38 O GLY A 102
SHEET 5 B13 GLY A 119 GLY A 122 -1 O VAL A 120 N TRP A 39
SHEET 6 B13 GLN A 25 ASP A 32 1 N VAL A 30 O VAL A 121
SHEET 7 B13 GLN A 13 ILE A 20 -1 N GLY A 16 O VAL A 29
SHEET 8 B13 SER A 2 TYR A 9 -1 N TYR A 9 O GLN A 13
SHEET 9 B13 GLY A 163 LEU A 167 -1 O LEU A 167 N SER A 2
SHEET 10 B13 VAL A 150 TYR A 155 -1 N TYR A 154 O GLN A 164
SHEET 11 B13 PHE A 309 ASP A 314 -1 O PHE A 313 N PHE A 151
SHEET 12 B13 ARG A 319 ALA A 325 -1 O GLY A 321 N GLU A 312
SHEET 13 B13 TYR A 175 ASN A 183 -1 N ILE A 182 O ILE A 320
SHEET 1 C 4 SER A 202 LEU A 205 0
SHEET 2 C 4 GLN A 191 VAL A 199 -1 N VAL A 197 O LEU A 205
SHEET 3 C 4 ILE A 258 LEU A 262 -1 O HIS A 261 N LYS A 195
SHEET 4 C 4 LYS A 265 LEU A 269 -1 O TYR A 267 N PHE A 260
SHEET 1 D 6 SER A 202 LEU A 205 0
SHEET 2 D 6 GLN A 191 VAL A 199 -1 N VAL A 197 O LEU A 205
SHEET 3 D 6 CYS A 210 VAL A 214 -1 O CYS A 210 N MET A 194
SHEET 4 D 6 TRP A 299 LEU A 301 1 O LEU A 301 N LEU A 213
SHEET 5 D 6 ILE A 221 GLY A 223 -1 N SER A 222 O ALA A 300
SHEET 6 D 6 ILE A 286 ALA A 288 1 O HIS A 287 N ILE A 221
SHEET 1 E 3 LYS A 238 LYS A 239 0
SHEET 2 E 3 TYR A 245 LYS A 248 -1 O VAL A 246 N LYS A 238
SHEET 3 E 3 LEU A 281 THR A 283 -1 O CYS A 282 N VAL A 247
SHEET 1 F 9 LYS B 65 ARG B 74 0
SHEET 2 F 9 THR B 79 VAL B 91 -1 O GLY B 82 N LEU B 71
SHEET 3 F 9 GLN B 13 ILE B 20 -1 N GLY B 19 O THR B 90
SHEET 4 F 9 SER B 2 TYR B 9 -1 N TYR B 9 O GLN B 13
SHEET 5 F 9 GLY B 163 LEU B 167 -1 O LEU B 167 N SER B 2
SHEET 6 F 9 VAL B 150 TYR B 155 -1 N TYR B 154 O GLN B 164
SHEET 7 F 9 PHE B 309 ASP B 314 -1 O PHE B 313 N PHE B 151
SHEET 8 F 9 ARG B 319 ALA B 325 -1 O GLY B 321 N GLU B 312
SHEET 9 F 9 TYR B 175 ASN B 183 -1 N ILE B 182 O ILE B 320
SHEET 1 G13 LYS B 65 ARG B 74 0
SHEET 2 G13 THR B 79 VAL B 91 -1 O GLY B 82 N LEU B 71
SHEET 3 G13 ILE B 94 GLU B 106 -1 O GLU B 103 N PHE B 83
SHEET 4 G13 VAL B 38 PRO B 41 1 N VAL B 38 O GLY B 102
SHEET 5 G13 GLY B 119 GLY B 122 -1 O VAL B 120 N TRP B 39
SHEET 6 G13 GLN B 25 ASP B 32 1 N VAL B 30 O VAL B 121
SHEET 7 G13 GLN B 13 ILE B 20 -1 N GLY B 16 O VAL B 29
SHEET 8 G13 SER B 2 TYR B 9 -1 N TYR B 9 O GLN B 13
SHEET 9 G13 GLY B 163 LEU B 167 -1 O LEU B 167 N SER B 2
SHEET 10 G13 VAL B 150 TYR B 155 -1 N TYR B 154 O GLN B 164
SHEET 11 G13 PHE B 309 ASP B 314 -1 O PHE B 313 N PHE B 151
SHEET 12 G13 ARG B 319 ALA B 325 -1 O GLY B 321 N GLU B 312
SHEET 13 G13 TYR B 175 ASN B 183 -1 N ILE B 182 O ILE B 320
SHEET 1 H 5 GLN B 191 MET B 194 0
SHEET 2 H 5 CYS B 210 VAL B 214 -1 O CYS B 210 N MET B 194
SHEET 3 H 5 TRP B 299 LEU B 301 1 O LEU B 301 N LEU B 213
SHEET 4 H 5 ILE B 221 GLY B 223 -1 N SER B 222 O ALA B 300
SHEET 5 H 5 ILE B 286 ALA B 288 1 O HIS B 287 N ILE B 221
SHEET 1 I 4 SER B 202 LEU B 205 0
SHEET 2 I 4 VAL B 197 VAL B 199 -1 N VAL B 197 O LEU B 205
SHEET 3 I 4 ILE B 258 LEU B 262 -1 O SER B 259 N SER B 198
SHEET 4 I 4 LYS B 265 LEU B 269 -1 O TYR B 267 N PHE B 260
SHEET 1 J 3 LYS B 238 LYS B 239 0
SHEET 2 J 3 TYR B 245 LYS B 248 -1 O VAL B 246 N LYS B 238
SHEET 3 J 3 LEU B 281 THR B 283 -1 O CYS B 282 N VAL B 247
SSBOND 1 CYS A 45 CYS A 50 1555 1555 2.02
SSBOND 2 CYS A 206 CYS A 210 1555 1555 2.03
SSBOND 3 CYS A 249 CYS A 282 1555 1555 2.04
SSBOND 4 CYS B 45 CYS B 50 1555 1555 2.01
SSBOND 5 CYS B 206 CYS B 210 1555 1555 2.03
SSBOND 6 CYS B 249 CYS B 282 1555 1555 2.03
LINK ND2 ASN A 67 C1 NAG A 367 1555 1555 1.47
LINK ND2 ASN B 67 C1 NAG B 367 1555 1555 1.47
CISPEP 1 THR A 22 PRO A 23 0 -3.04
CISPEP 2 LEU A 110 PRO A 111 0 6.97
CISPEP 3 PRO A 293 PRO A 294 0 3.11
CISPEP 4 GLY A 296 PRO A 297 0 -2.83
CISPEP 5 THR B 22 PRO B 23 0 -2.04
CISPEP 6 LEU B 110 PRO B 111 0 4.60
CISPEP 7 PRO B 293 PRO B 294 0 2.80
CISPEP 8 GLY B 296 PRO B 297 0 -1.04
CRYST1 141.387 141.387 141.387 90.00 90.00 90.00 P 21 3 24
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 0.007073 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007073 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007073 0.00000
(ATOM LINES ARE NOT SHOWN.)
END