HEADER HYDROLASE/HYDROLASE INHIBITOR 09-AUG-12 4GJA
TITLE CRYSTAL STRUCTURE OF RENIN IN COMPLEX WITH NVP-AYL747 (COMPOUND 5)
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: CRICETULUS GRISEUS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 10029
KEYWDS RENIN INHIBITOR, FRAGMENT BASED SCREENING, 3, 5-DISUBSTITUTED
KEYWDS 2 PIPERIDINES, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR N.OSTERMANN,F.ZINK,M.KROEMER
REVDAT 4 13-SEP-23 4GJA 1 HETSYN
REVDAT 3 29-JUL-20 4GJA 1 COMPND REMARK HETNAM LINK
REVDAT 3 2 1 SITE
REVDAT 2 10-APR-13 4GJA 1 JRNL
REVDAT 1 13-FEB-13 4GJA 0
JRNL AUTH N.OSTERMANN,S.RUEDISSER,C.EHRHARDT,W.BREITENSTEIN,
JRNL AUTH 2 A.MARZINZIK,E.JACOBY,E.VANGREVELINGHE,J.OTTL,M.KLUMPP,
JRNL AUTH 3 J.C.HARTWIEG,F.CUMIN,U.HASSIEPEN,J.TRAPPE,R.SEDRANI,
JRNL AUTH 4 S.GEISSE,B.GERHARTZ,P.RICHERT,E.FRANCOTTE,T.WAGNER,M.KROMER,
JRNL AUTH 5 T.KOSAKA,R.L.WEBB,D.F.RIGEL,J.MAIBAUM,D.K.BAESCHLIN
JRNL TITL A NOVEL CLASS OF ORAL DIRECT RENIN INHIBITORS: HIGHLY POTENT
JRNL TITL 2 3,5-DISUBSTITUTED PIPERIDINES BEARING A TRICYCLIC P3-P1
JRNL TITL 3 PHARMACOPHORE.
JRNL REF J.MED.CHEM. V. 56 2196 2013
JRNL REFN ISSN 0022-2623
JRNL PMID 23360239
JRNL DOI 10.1021/JM301706J
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.2
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.05
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 29268
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) : 0.190
REMARK 3 R VALUE (WORKING SET) : 0.185
REMARK 3 FREE R VALUE : 0.230
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.090
REMARK 3 FREE R VALUE TEST SET COUNT : 2954
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 : 15
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.69
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.76
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2805
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2314
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2513
REMARK 3 BIN R VALUE (WORKING SET) : 0.2243
REMARK 3 BIN FREE R VALUE : 0.2942
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.41
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 292
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 : 111
REMARK 3 SOLVENT ATOMS : 215
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 71.32
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 60.61
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) : 0.311
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.432
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.258
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.422
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.260
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 : 0.949
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.927
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 5436 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 7384 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1810 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 112 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 794 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 5436 ; 20.000 ; HARMONIC
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 : 722 ; 5.000 ; SEMIHARMONIC
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 : 6219 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.20
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.54
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 17.93
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4GJA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-AUG-12.
REMARK 100 THE DEPOSITION ID IS D_1000074253.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-APR-04
REMARK 200 TEMPERATURE (KELVIN) : 95.0
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979347
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29317
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 50.050
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.06500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 21.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.40700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 2V0Z
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.22
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.17
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: RESERVOIR: 18-21% PEG4000, 0.4-0.6 M
REMARK 280 SODIUM CHLORIDE, 50 MM SODIUM CITRATE, PH 4-5, PROTEIN SOLUTION:
REMARK 280 10-15 MG/ML PROTEIN, 25 MM SODIUM CHLORIDE, 12.5 MM TRIS, PH 8,
REMARK 280 DROP: 1 UL PROTEIN SOLUTION + 1 UL RESERVOIR, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 293K
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 70.77800
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 70.77800
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 70.77800
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 70.77800
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 70.77800
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 70.77800
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 70.77800
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 70.77800
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 70.77800
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 70.77800
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 70.77800
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 70.77800
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 70.77800
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 70.77800
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 70.77800
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 70.77800
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 70.77800
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 70.77800
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 GLU A 159A
REMARK 465 ASN A 159B
REMARK 465 SER A 159C
REMARK 465 GLU B 159A
REMARK 465 ASN B 159B
REMARK 465 SER B 159C
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 -63.53 -140.87
REMARK 500 ALA A 285 30.72 -90.49
REMARK 500 ASN B 67 -60.51 -140.58
REMARK 500 ARG B 240 -103.82 -70.35
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4GJ8 RELATED DB: PDB
REMARK 900 RELATED ID: 4GJ9 RELATED DB: PDB
REMARK 900 RELATED ID: 4GJB RELATED DB: PDB
REMARK 900 RELATED ID: 4GJC RELATED DB: PDB
REMARK 900 RELATED ID: 4GJD RELATED DB: PDB
DBREF 4GJA A -5 326 UNP P00797 RENI_HUMAN 67 406
DBREF 4GJA 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 4GJA ASN A 67 ASN GLYCOSYLATION SITE
MODRES 4GJA ASN B 67 ASN GLYCOSYLATION SITE
HET NAG A1000 14
HET 0M3 A1001 34
HET SO4 A1002 5
HET SO4 A1003 5
HET NAG B1000 14
HET 0M3 B1001 34
HET SO4 B1002 5
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM 0M3 (3S,5R)-N-(2,2-DIPHENYLETHYL)-5-{[(4-METHYLPHENYL)
HETNAM 2 0M3 SULFONYL]AMINO}PIPERIDINE-3-CARBOXAMIDE
HETNAM SO4 SULFATE ION
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
FORMUL 3 NAG 2(C8 H15 N O6)
FORMUL 4 0M3 2(C27 H31 N3 O3 S)
FORMUL 5 SO4 3(O4 S 2-)
FORMUL 10 HOH *215(H2 O)
HELIX 1 1 TYR A 47B TYR A 52 1 6
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 47B TYR B 52 1 6
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 GLN A 86 N LYS A 65
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 SER A 152 O VAL A 166
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 ARG A 319 N ASP A 314
SHEET 9 A 9 TYR A 175 ASN A 183 -1 N GLU A 176 O LEU A 324
SHEET 1 B13 LYS A 65 ARG A 74 0
SHEET 2 B13 THR A 79 VAL A 91 -1 O GLN A 86 N LYS A 65
SHEET 3 B13 ILE A 94 GLU A 106 -1 O GLU A 103 N PHE A 83
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 SER A 152 O VAL A 166
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 ARG A 319 N ASP A 314
SHEET 13 B13 TYR A 175 ASN A 183 -1 N GLU A 176 O LEU A 324
SHEET 1 C 5 GLN A 191 MET A 194 0
SHEET 2 C 5 CYS A 210 VAL A 214 -1 O CYS A 210 N MET A 194
SHEET 3 C 5 TRP A 299 LEU A 301 1 O LEU A 301 N LEU A 213
SHEET 4 C 5 ILE A 221 GLY A 223 -1 N SER A 222 O ALA A 300
SHEET 5 C 5 ILE A 286 ALA A 288 1 O HIS A 287 N ILE A 221
SHEET 1 D 4 SER A 202 LEU A 205 0
SHEET 2 D 4 GLY A 196 VAL A 199 -1 N VAL A 197 O LEU A 205
SHEET 3 D 4 ILE A 258 LEU A 262 -1 O HIS A 261 N GLY A 196
SHEET 4 D 4 LYS A 265 LEU A 269 -1 O LEU A 269 N ILE A 258
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 281D 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 VAL B 80 N LEU B 73
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 SER B 152 O VAL B 166
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 ARG B 319 N ASP B 314
SHEET 9 F 9 TYR B 175 ASN B 183 -1 N GLU B 176 O LEU B 324
SHEET 1 G13 LYS B 65 ARG B 74 0
SHEET 2 G13 THR B 79 VAL B 91 -1 O VAL B 80 N LEU B 73
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 SER B 152 O VAL B 166
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 ARG B 319 N ASP B 314
SHEET 13 G13 TYR B 175 ASN B 183 -1 N GLU B 176 O LEU B 324
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 GLY B 196 VAL B 199 -1 N VAL B 197 O LEU B 205
SHEET 3 I 4 ILE B 258 LEU B 262 -1 O HIS B 261 N GLY B 196
SHEET 4 I 4 LYS B 265 LEU B 269 -1 O LEU B 269 N ILE B 258
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 281D 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 2.04
SSBOND 3 CYS A 249 CYS A 282 1555 1555 2.04
SSBOND 4 CYS B 45 CYS B 50 1555 1555 2.03
SSBOND 5 CYS B 206 CYS B 210 1555 1555 2.04
SSBOND 6 CYS B 249 CYS B 282 1555 1555 2.05
LINK ND2 ASN A 67 C1 NAG A1000 1555 1555 1.43
LINK ND2 ASN B 67 C1 NAG B1000 1555 1555 1.44
CISPEP 1 THR A 22 PRO A 23 0 -3.22
CISPEP 2 LEU A 110 PRO A 111 0 9.25
CISPEP 3 PRO A 293 PRO A 294 0 3.20
CISPEP 4 GLY A 296 PRO A 297 0 -2.45
CISPEP 5 THR B 22 PRO B 23 0 -3.71
CISPEP 6 LEU B 110 PRO B 111 0 7.62
CISPEP 7 PRO B 293 PRO B 294 0 3.61
CISPEP 8 GLY B 296 PRO B 297 0 -2.85
CRYST1 141.556 141.556 141.556 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 0.007064 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007064 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007064 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
