HEADER HYDROLASE/HYDROLASE INHIBITOR 24-SEP-12 3VYF
TITLE HUMAN RENIN IN COMPLEX WITH INHIBITOR 9
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RENIN;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ANGIOTENSINOGENASE;
COMPND 5 EC: 3.4.23.15;
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: 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: 293F;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PCDNA3.1
KEYWDS ASPARTYL PROTEASE, RAS, HYPERTENSION, INHIBITOR, HYDROLASE-HYDROLASE
KEYWDS 2 INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR M.TAKAHASHI,H.HANZAWA
REVDAT 3 08-NOV-23 3VYF 1 HETSYN
REVDAT 2 29-JUL-20 3VYF 1 COMPND REMARK HETNAM LINK
REVDAT 2 2 1 SITE
REVDAT 1 19-DEC-12 3VYF 0
JRNL AUTH Y.MORI,Y.OGAWA,A.MOCHIZUKI,Y.NAKAMURA,C.SUGITA,S.MIYAZAKI,
JRNL AUTH 2 K.TAMAKI,Y.MATSUI,M.TAKAHASHI,T.NAGAYAMA,Y.NAGAI,S.INOUE,
JRNL AUTH 3 T.NISHI
JRNL TITL DESIGN AND DISCOVERY OF NEW
JRNL TITL 2 (3S,5R)-5-[4-(2-CHLOROPHENYL)-2,
JRNL TITL 3 2-DIMETHYL-5-OXOPIPERAZIN-1-YL]PIPERIDINE-3-CARBOXAMIDES AS
JRNL TITL 4 POTENT RENIN INHIBITORS
JRNL REF BIOORG.MED.CHEM.LETT. V. 22 7677 2012
JRNL REFN ISSN 0960-894X
JRNL PMID 23122821
JRNL DOI 10.1016/J.BMCL.2012.09.103
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.2
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.80
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1684691.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 23333
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 SET) : 0.218
REMARK 3 FREE R VALUE : 0.266
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2328
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.97
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.70
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3469
REMARK 3 BIN R VALUE (WORKING SET) : 0.3160
REMARK 3 BIN FREE R VALUE : 0.4070
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.90
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 381
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.021
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5170
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 96
REMARK 3 SOLVENT ATOMS : 97
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 83.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 42.52
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) : 0.35
REMARK 3 ESD FROM SIGMAA (A) : 0.41
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.45
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.52
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 31.50
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.710
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.210 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.040 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.810 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.790 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.35
REMARK 3 BSOL : 33.67
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER.PARAM
REMARK 3 PARAMETER FILE 3 : UNL.PARAM
REMARK 3 PARAMETER FILE 4 : CARBOHYDRATE.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : UNL.TOP
REMARK 3 TOPOLOGY FILE 4 : CARBOHYDRATE.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED
REMARK 4
REMARK 4 3VYF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-OCT-12.
REMARK 100 THE DEPOSITION ID IS D_1000095656.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-AUG-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 3.0-4.5
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 FR-E SUPERBRIGHT
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.502
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS VII
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23593
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
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 (%) : 99.9
REMARK 200 DATA REDUNDANCY : 5.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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 : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: 3VSW
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.11
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.16
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 5-12% PEG 3350, 0.6M NACL, 0.1M
REMARK 280 CITRATE PH3.0-4.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 295K, VAPOR DIFFUSION, HANGING DROP
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 70.71350
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 70.71350
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 70.71350
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 70.71350
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 70.71350
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 70.71350
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 70.71350
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 70.71350
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 70.71350
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 70.71350
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 70.71350
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 70.71350
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 70.71350
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 70.71350
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 70.71350
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 70.71350
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 70.71350
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 70.71350
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 13570 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 73410 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -52.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350 BIOMT1 2 0.000000 0.000000 1.000000 70.71350
REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 353.56750
REMARK 350 BIOMT3 2 0.000000 -1.000000 0.000000 282.85400
REMARK 350 BIOMT1 3 0.000000 -1.000000 0.000000 353.56750
REMARK 350 BIOMT2 3 0.000000 0.000000 -1.000000 282.85400
REMARK 350 BIOMT3 3 1.000000 0.000000 0.000000 -70.71350
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 167
REMARK 465 ASN A 168
REMARK 465 SER A 169
REMARK 465 GLN A 170
REMARK 465 SER B 166
REMARK 465 GLU B 167
REMARK 465 ASN B 168
REMARK 465 SER B 169
REMARK 465 GLN B 170
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 16 22.66 48.32
REMARK 500 ASN A 75 -65.11 -152.94
REMARK 500 LYS A 197 148.14 -176.59
REMARK 500 ALA A 299 45.46 -84.58
REMARK 500 ASN B 75 -55.75 -140.61
REMARK 500 PHE B 119 -4.08 -50.57
REMARK 500 ARG B 164 -33.81 -133.65
REMARK 500 LYS B 197 144.36 -178.39
REMARK 500 ARG B 251 -98.32 -65.08
REMARK 500 LEU B 252 -52.75 -120.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3VYD RELATED DB: PDB
REMARK 900 RELATED ID: 3VYE RELATED DB: PDB
DBREF 3VYF A 1 340 UNP P00797 RENI_HUMAN 67 406
DBREF 3VYF B 1 340 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 3VYF ASN B 75 ASN GLYCOSYLATION SITE
MODRES 3VYF ASN A 75 ASN GLYCOSYLATION SITE
HET NAG A 401 14
HET VYF A 402 68
HET NAG B 401 14
HET VYF B 402 68
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM VYF (3S,5R)-5-[4-(2-CHLOROPHENYL)-2,2-DIMETHYL-5-
HETNAM 2 VYF OXOPIPERAZIN-1-YL]-N-(2,6-DIMETHYLHEPTAN-4-YL)
HETNAM 3 VYF PIPERIDINE-3-CARBOXAMIDE
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 VYF 2(C27 H43 CL N4 O2)
FORMUL 7 HOH *97(H2 O)
HELIX 1 1 TYR A 55 TYR A 60 1 6
HELIX 2 2 ASP A 65 SER A 69 5 5
HELIX 3 3 PRO A 115 MET A 120 1 6
HELIX 4 4 PHE A 132 VAL A 140 5 9
HELIX 5 5 PRO A 142 SER A 149 1 8
HELIX 6 6 ASP A 182 GLN A 184 5 3
HELIX 7 7 SER A 235 GLY A 247 1 13
HELIX 8 8 ASN A 260 LEU A 265 5 6
HELIX 9 9 THR A 280 VAL A 285 1 6
HELIX 10 10 GLY A 316 ARG A 321 1 6
HELIX 11 11 TYR B 55 HIS B 61 1 7
HELIX 12 12 ASP B 65 SER B 69 5 5
HELIX 13 13 PRO B 115 MET B 120 1 6
HELIX 14 14 PHE B 132 VAL B 140 5 9
HELIX 15 15 PRO B 142 GLN B 150 1 9
HELIX 16 16 ASP B 182 GLN B 184 5 3
HELIX 17 17 SER B 235 GLY B 247 1 13
HELIX 18 18 ASN B 260 LEU B 265 5 6
HELIX 19 19 THR B 280 VAL B 285 1 6
HELIX 20 20 GLY B 316 ARG B 321 1 6
SHEET 1 A 9 GLU A 78 TYR A 83 0
SHEET 2 A 9 GLY A 86 VAL A 99 -1 O GLY A 90 N LEU A 79
SHEET 3 A 9 GLN A 19 ILE A 26 -1 N GLY A 25 O THR A 98
SHEET 4 A 9 SER A 8 TYR A 15 -1 N THR A 13 O TYR A 21
SHEET 5 A 9 GLY A 174 LEU A 178 -1 O LEU A 178 N SER A 8
SHEET 6 A 9 VAL A 157 TYR A 162 -1 N SER A 159 O VAL A 177
SHEET 7 A 9 PHE A 323 ASP A 328 -1 O PHE A 327 N PHE A 158
SHEET 8 A 9 ARG A 333 ALA A 339 -1 O GLY A 335 N GLU A 326
SHEET 9 A 9 TYR A 186 ASN A 194 -1 N HIS A 191 O PHE A 336
SHEET 1 B13 GLU A 78 TYR A 83 0
SHEET 2 B13 GLY A 86 VAL A 99 -1 O GLY A 90 N LEU A 79
SHEET 3 B13 ILE A 102 GLU A 113 -1 O GLU A 110 N PHE A 91
SHEET 4 B13 VAL A 44 PRO A 47 1 N VAL A 44 O GLY A 109
SHEET 5 B13 GLY A 126 GLY A 129 -1 O VAL A 127 N TRP A 45
SHEET 6 B13 GLN A 31 ASP A 38 1 N VAL A 36 O VAL A 128
SHEET 7 B13 GLN A 19 ILE A 26 -1 N GLY A 22 O VAL A 35
SHEET 8 B13 SER A 8 TYR A 15 -1 N THR A 13 O TYR A 21
SHEET 9 B13 GLY A 174 LEU A 178 -1 O LEU A 178 N SER A 8
SHEET 10 B13 VAL A 157 TYR A 162 -1 N SER A 159 O VAL A 177
SHEET 11 B13 PHE A 323 ASP A 328 -1 O PHE A 327 N PHE A 158
SHEET 12 B13 ARG A 333 ALA A 339 -1 O GLY A 335 N GLU A 326
SHEET 13 B13 TYR A 186 ASN A 194 -1 N HIS A 191 O PHE A 336
SHEET 1 C 3 GLN A 202 MET A 205 0
SHEET 2 C 3 CYS A 221 VAL A 225 -1 O CYS A 221 N MET A 205
SHEET 3 C 3 TRP A 313 LEU A 315 1 O LEU A 315 N LEU A 224
SHEET 1 D 4 THR A 214 LEU A 216 0
SHEET 2 D 4 GLY A 207 VAL A 210 -1 N VAL A 208 O LEU A 216
SHEET 3 D 4 ILE A 268 HIS A 271 -1 O HIS A 271 N GLY A 207
SHEET 4 D 4 GLU A 276 LEU A 279 -1 O LEU A 279 N ILE A 268
SHEET 1 E 2 ILE A 232 GLY A 234 0
SHEET 2 E 2 ILE A 300 ALA A 302 1 O HIS A 301 N ILE A 232
SHEET 1 F 3 LYS A 249 LYS A 250 0
SHEET 2 F 3 TYR A 255 LYS A 258 -1 O VAL A 256 N LYS A 249
SHEET 3 F 3 LEU A 295 THR A 297 -1 O CYS A 296 N VAL A 257
SHEET 1 G 6 SER B 8 ILE B 11 0
SHEET 2 G 6 GLY B 174 LEU B 178 -1 O LEU B 178 N SER B 8
SHEET 3 G 6 VAL B 157 TYR B 162 -1 N SER B 159 O VAL B 177
SHEET 4 G 6 PHE B 323 ASP B 328 -1 O PHE B 327 N PHE B 158
SHEET 5 G 6 ARG B 333 ALA B 339 -1 O GLY B 335 N GLU B 326
SHEET 6 G 6 TYR B 186 ASN B 194 -1 N GLU B 187 O LEU B 338
SHEET 1 H 8 THR B 13 TYR B 15 0
SHEET 2 H 8 GLN B 19 ILE B 26 -1 O GLN B 19 N TYR B 15
SHEET 3 H 8 GLN B 31 ASP B 38 -1 O VAL B 35 N GLY B 22
SHEET 4 H 8 GLY B 126 GLY B 129 1 O VAL B 128 N VAL B 36
SHEET 5 H 8 VAL B 44 PRO B 47 -1 N TRP B 45 O VAL B 127
SHEET 6 H 8 ILE B 102 GLU B 113 1 O GLY B 109 N VAL B 44
SHEET 7 H 8 GLY B 86 VAL B 99 -1 N PHE B 91 O GLU B 110
SHEET 8 H 8 LYS B 73 TYR B 83 -1 N LEU B 79 O GLY B 90
SHEET 1 I 4 THR B 13 TYR B 15 0
SHEET 2 I 4 GLN B 19 ILE B 26 -1 O GLN B 19 N TYR B 15
SHEET 3 I 4 GLY B 86 VAL B 99 -1 O THR B 98 N GLY B 25
SHEET 4 I 4 LYS B 73 TYR B 83 -1 N LEU B 79 O GLY B 90
SHEET 1 J 5 GLN B 202 MET B 205 0
SHEET 2 J 5 CYS B 221 VAL B 225 -1 O CYS B 221 N MET B 205
SHEET 3 J 5 TRP B 313 LEU B 315 1 O TRP B 313 N LEU B 224
SHEET 4 J 5 ILE B 232 GLY B 234 -1 N SER B 233 O ALA B 314
SHEET 5 J 5 ILE B 300 ALA B 302 1 O HIS B 301 N ILE B 232
SHEET 1 K 4 SER B 213 LEU B 216 0
SHEET 2 K 4 VAL B 208 VAL B 210 -1 N VAL B 208 O LEU B 216
SHEET 3 K 4 ILE B 268 LEU B 272 -1 O SER B 269 N SER B 209
SHEET 4 K 4 LYS B 275 LEU B 279 -1 O TYR B 277 N PHE B 270
SHEET 1 L 3 LYS B 249 LYS B 250 0
SHEET 2 L 3 TYR B 255 LYS B 258 -1 O VAL B 256 N LYS B 249
SHEET 3 L 3 LEU B 295 THR B 297 -1 O CYS B 296 N VAL B 257
SSBOND 1 CYS A 51 CYS A 58 1555 1555 2.03
SSBOND 2 CYS A 217 CYS A 221 1555 1555 2.04
SSBOND 3 CYS A 259 CYS A 296 1555 1555 2.04
SSBOND 4 CYS B 51 CYS B 58 1555 1555 2.03
SSBOND 5 CYS B 217 CYS B 221 1555 1555 2.04
SSBOND 6 CYS B 259 CYS B 296 1555 1555 2.03
LINK ND2 ASN A 75 C1 NAG A 401 1555 1555 1.46
LINK ND2 ASN B 75 C1 NAG B 401 1555 1555 1.46
CISPEP 1 THR A 28 PRO A 29 0 -0.15
CISPEP 2 LEU A 117 PRO A 118 0 0.28
CISPEP 3 PRO A 307 PRO A 308 0 0.00
CISPEP 4 GLY A 310 PRO A 311 0 0.04
CISPEP 5 THR B 28 PRO B 29 0 -0.05
CISPEP 6 LEU B 117 PRO B 118 0 0.21
CISPEP 7 PRO B 307 PRO B 308 0 -0.04
CISPEP 8 GLY B 310 PRO B 311 0 -0.06
CRYST1 141.427 141.427 141.427 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 0.007071 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007071 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007071 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
