HEADER HYDROLASE/HYDROLASE INHIBITOR 09-AUG-12 4GJ5
TITLE CRYSTAL STRUCTURE OF RENIN IN COMPLEX WITH NVP-AMQ838 (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, PHARMACOPHORE SEARCH, TRANS-3, 4-DISUBSTITUTED
KEYWDS 2 PYRROLIDINE, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR N.OSTERMANN,F.ZINK,M.KROEMER
REVDAT 4 13-SEP-23 4GJ5 1 HETSYN
REVDAT 3 29-JUL-20 4GJ5 1 COMPND REMARK HETNAM LINK
REVDAT 3 2 1 SITE
REVDAT 2 10-APR-13 4GJ5 1 JRNL
REVDAT 1 06-MAR-13 4GJ5 0
JRNL AUTH E.LORTHIOIS,W.BREITENSTEIN,F.CUMIN,C.EHRHARDT,E.FRANCOTTE,
JRNL AUTH 2 E.JACOBY,N.OSTERMANN,H.SELLNER,T.KOSAKA,R.L.WEBB,D.F.RIGEL,
JRNL AUTH 3 U.HASSIEPEN,P.RICHERT,T.WAGNER,J.MAIBAUM
JRNL TITL THE DISCOVERY OF NOVEL POTENT TRANS-3,4-DISUBSTITUTED
JRNL TITL 2 PYRROLIDINE INHIBITORS OF THE HUMAN ASPARTIC PROTEASE RENIN
JRNL TITL 3 FROM IN SILICO THREE-DIMENSIONAL (3D) PHARMACOPHORE
JRNL TITL 4 SEARCHES.
JRNL REF J.MED.CHEM. V. 56 2207 2013
JRNL REFN ISSN 0022-2623
JRNL PMID 23425156
JRNL DOI 10.1021/JM3017078
REMARK 2
REMARK 2 RESOLUTION. 2.40 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) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.92
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 36850
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) : 0.173
REMARK 3 R VALUE (WORKING SET) : 0.169
REMARK 3 FREE R VALUE : 0.208
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.950
REMARK 3 FREE R VALUE TEST SET COUNT : 3665
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 : 18
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.47
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.15
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2986
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2099
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2691
REMARK 3 BIN R VALUE (WORKING SET) : 0.2028
REMARK 3 BIN FREE R VALUE : 0.2735
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.88
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 295
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 : 5098
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 76
REMARK 3 SOLVENT ATOMS : 513
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 43.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.01
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.25470
REMARK 3 B22 (A**2) : -1.72430
REMARK 3 B33 (A**2) : 0.46960
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) : 0.240
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.288
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.203
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.258
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.197
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 : 0.945
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.919
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 5302 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 7196 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1760 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 110 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 773 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 5302 ; 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 : 711 ; 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 : 6238 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.16
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.79
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 17.36
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 4GJ5 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_1000074248.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-MAR-03
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) : 0.98010
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 : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36892
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 28.600
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 4.500
REMARK 200 R MERGE (I) : 0.09600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.53
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.3
REMARK 200 DATA REDUNDANCY IN SHELL : 4.20
REMARK 200 R MERGE FOR SHELL (I) : 0.38100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
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 (%): 60.95
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.15
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 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 33.29300
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 68.76900
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 51.27350
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 68.76900
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 33.29300
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 51.27350
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 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 ARG A 46A
REMARK 465 LEU A 46B
REMARK 465 TYR A 46C
REMARK 465 SER A 158A
REMARK 465 GLU A 158B
REMARK 465 ASN A 158C
REMARK 465 SER A 158D
REMARK 465 GLN A 158E
REMARK 465 ARG B 46A
REMARK 465 LEU B 46B
REMARK 465 TYR B 46C
REMARK 465 SER B 158A
REMARK 465 GLU B 158B
REMARK 465 ASN B 158C
REMARK 465 SER B 158D
REMARK 465 GLN B 158E
REMARK 465 SER B 158F
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 MET A 10 29.06 49.05
REMARK 500 ASN A 67 -67.68 -133.81
REMARK 500 ARG A 240 -158.77 -88.56
REMARK 500 ALA A 285 43.88 -84.29
REMARK 500 MET B 10 29.28 49.11
REMARK 500 ASN B 67 -46.26 -139.28
REMARK 500 ARG B 240 -167.50 -102.82
REMARK 500 ALA B 285 43.49 -85.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4GJ6 RELATED DB: PDB
REMARK 900 RELATED ID: 4GJ7 RELATED DB: PDB
DBREF 4GJ5 A -5 326 UNP P00797 RENI_HUMAN 67 406
DBREF 4GJ5 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 4GJ5 ASN A 67 ASN GLYCOSYLATION SITE
MODRES 4GJ5 ASN B 67 ASN GLYCOSYLATION SITE
HET NAG A1000 14
HET 0LR A1001 24
HET NAG B1000 14
HET 0LR B1001 24
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM 0LR (3R,4R)-3-(NAPHTHALEN-2-YLMETHOXY)-4-PHENYLPIPERIDINE
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 0LR 2(C22 H23 N O)
FORMUL 7 HOH *513(H2 O)
HELIX 1 1 THR A 48 HIS A 53 5 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 GLY A 144 1 10
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 GLU A 251 LEU A 255 5 5
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 THR B 48 HIS B 53 5 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 GLU B 251 LEU B 255 5 5
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 GLY A 82 N LEU A 71
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 THR A 7 O TYR A 15
SHEET 5 A 9 GLY A 163 LEU A 167 -1 O GLY A 163 N LEU A 6
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 GLY A 82 N LEU A 71
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 THR A 7 O TYR A 15
SHEET 9 B13 GLY A 163 LEU A 167 -1 O GLY A 163 N LEU A 6
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 LEU A 269 N ILE A 258
SHEET 1 D 4 SER A 202 LEU A 205 0
SHEET 2 D 4 GLN A 191 VAL A 199 -1 N VAL A 197 O LEU A 205
SHEET 3 D 4 CYS A 210 VAL A 214 -1 O CYS A 210 N MET A 194
SHEET 4 D 4 TRP A 299 LEU A 301 1 O LEU A 301 N LEU A 213
SHEET 1 E 2 ILE A 221 GLY A 223 0
SHEET 2 E 2 ILE A 286 ALA A 288 1 O HIS A 287 N ILE A 221
SHEET 1 F 3 LYS A 238 LYS A 239 0
SHEET 2 F 3 TYR A 245 LYS A 248 -1 O VAL A 246 N LYS A 238
SHEET 3 F 3 LEU A 281 THR A 283 -1 O CYS A 282 N VAL A 247
SHEET 1 G 9 LYS B 65 ARG B 74 0
SHEET 2 G 9 THR B 79 VAL B 91 -1 O GLY B 82 N LEU B 71
SHEET 3 G 9 GLN B 13 ILE B 20 -1 N GLY B 19 O THR B 90
SHEET 4 G 9 SER B 2 TYR B 9 -1 N TYR B 9 O GLN B 13
SHEET 5 G 9 GLY B 163 LEU B 167 -1 O LEU B 167 N SER B 2
SHEET 6 G 9 VAL B 150 TYR B 155 -1 N SER B 152 O VAL B 166
SHEET 7 G 9 PHE B 309 ASP B 314 -1 O PHE B 313 N PHE B 151
SHEET 8 G 9 ARG B 319 ALA B 325 -1 O GLY B 321 N GLU B 312
SHEET 9 G 9 TYR B 175 ASN B 183 -1 N ILE B 182 O ILE B 320
SHEET 1 H13 LYS B 65 ARG B 74 0
SHEET 2 H13 THR B 79 VAL B 91 -1 O GLY B 82 N LEU B 71
SHEET 3 H13 ILE B 94 GLU B 106 -1 O PHE B 101 N SER B 85
SHEET 4 H13 VAL B 38 PRO B 41 1 N VAL B 38 O GLY B 102
SHEET 5 H13 GLY B 119 GLY B 122 -1 O VAL B 120 N TRP B 39
SHEET 6 H13 GLN B 25 ASP B 32 1 N VAL B 30 O VAL B 121
SHEET 7 H13 GLN B 13 ILE B 20 -1 N GLY B 16 O VAL B 29
SHEET 8 H13 SER B 2 TYR B 9 -1 N TYR B 9 O GLN B 13
SHEET 9 H13 GLY B 163 LEU B 167 -1 O LEU B 167 N SER B 2
SHEET 10 H13 VAL B 150 TYR B 155 -1 N SER B 152 O VAL B 166
SHEET 11 H13 PHE B 309 ASP B 314 -1 O PHE B 313 N PHE B 151
SHEET 12 H13 ARG B 319 ALA B 325 -1 O GLY B 321 N GLU B 312
SHEET 13 H13 TYR B 175 ASN B 183 -1 N ILE B 182 O ILE B 320
SHEET 1 I 3 GLN B 191 MET B 194 0
SHEET 2 I 3 CYS B 210 VAL B 214 -1 O CYS B 210 N MET B 194
SHEET 3 I 3 TRP B 299 LEU B 301 1 O LEU B 301 N LEU B 213
SHEET 1 J 4 SER B 202 LEU B 205 0
SHEET 2 J 4 GLY B 196 VAL B 199 -1 N VAL B 197 O LEU B 205
SHEET 3 J 4 ILE B 258 LEU B 262 -1 O HIS B 261 N GLY B 196
SHEET 4 J 4 LYS B 265 LEU B 269 -1 O LEU B 269 N ILE B 258
SHEET 1 K 2 ILE B 221 GLY B 223 0
SHEET 2 K 2 ILE B 286 ALA B 288 1 O HIS B 287 N ILE B 221
SHEET 1 L 3 LYS B 238 LYS B 239 0
SHEET 2 L 3 TYR B 245 LYS B 248 -1 O VAL B 246 N LYS B 238
SHEET 3 L 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 2.03
SSBOND 2 CYS A 206 CYS A 210 1555 1555 2.04
SSBOND 3 CYS A 249 CYS A 282 1555 1555 2.07
SSBOND 4 CYS B 45 CYS B 50 1555 1555 2.03
SSBOND 5 CYS B 206 CYS B 210 1555 1555 2.05
SSBOND 6 CYS B 249 CYS B 282 1555 1555 2.06
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 -5.48
CISPEP 2 LEU A 110 PRO A 111 0 13.72
CISPEP 3 PRO A 293 PRO A 294 0 5.68
CISPEP 4 GLY A 296 PRO A 297 0 -4.54
CISPEP 5 THR B 22 PRO B 23 0 -3.06
CISPEP 6 LEU B 110 PRO B 111 0 0.02
CISPEP 7 PRO B 293 PRO B 294 0 5.24
CISPEP 8 GLY B 296 PRO B 297 0 -5.26
CRYST1 66.586 102.547 137.538 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 0.015018 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009752 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007271 0.00000
(ATOM LINES ARE NOT SHOWN.)
END