HEADER HYDROLASE/HYDROLASE INHIBITOR 11-MAY-12 3VSX
TITLE HUMAN RENIN IN COMPLEX WITH COMPOUND 18
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 RAS, HYPERTENSION, INHIBITOR, ASPARTYL PROTEASE, HYDROLASE-HYDROLASE
KEYWDS 2 INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR M.TAKAHASHI,H.HANZAWA
REVDAT 4 08-NOV-23 3VSX 1 HETSYN
REVDAT 3 29-JUL-20 3VSX 1 COMPND REMARK HETNAM LINK
REVDAT 3 2 1 SITE
REVDAT 2 22-NOV-17 3VSX 1 REMARK
REVDAT 1 25-JUL-12 3VSX 0
JRNL AUTH Y.NAKAMURA,C.SUGITA,M.MEGURO,S.MIYAZAKI,K.TAMAKI,
JRNL AUTH 2 M.TAKAHASHI,Y.NAGAI,T.NAGAYAMA,M.KATO,H.SUEMUNE,T.NISHI
JRNL TITL DESIGN AND OPTIMIZATION OF NOVEL
JRNL TITL 2 (2S,4S,5S)-5-AMINO-6-(2,
JRNL TITL 3 2-DIMETHYL-5-OXO-4-PHENYLPIPERAZIN-1-YL)
JRNL TITL 4 -4-HYDROXY-2-ISOPROPYLHEXANAMIDES AS RENIN INHIBITORS
JRNL REF BIOORG.MED.CHEM.LETT. V. 22 4561 2012
JRNL REFN ISSN 0960-894X
JRNL PMID 22726934
JRNL DOI 10.1016/J.BMCL.2012.05.092
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
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 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.74
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1545152.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 21665
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : OTHER
REMARK 3 R VALUE (WORKING + TEST SET) : 0.237
REMARK 3 R VALUE (WORKING SET) : 0.237
REMARK 3 FREE R VALUE : 0.301
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2165
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL
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) (%) : 100.0
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3243
REMARK 3 BIN R VALUE (WORKING SET) : 0.3360
REMARK 3 BIN FREE R VALUE : 0.4380
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.80
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 354
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.023
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5240
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 100
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.56
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) : 0.37
REMARK 3 ESD FROM SIGMAA (A) : 0.40
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) : 0.49
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.59
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.500
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 26.60
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.870
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) : 1.090 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.890 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.500 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.340 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.28
REMARK 3 BSOL : 10.00
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 : CARBOHYDRATE.PARAM
REMARK 3 PARAMETER FILE 4 : R32.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 : CARBOHYDRATE.TOP
REMARK 3 TOPOLOGY FILE 4 : R32.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED
REMARK 4
REMARK 4 3VSX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 30-MAY-12.
REMARK 100 THE DEPOSITION ID IS D_1000095460.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-APR-06
REMARK 200 TEMPERATURE (KELVIN) : 93
REMARK 200 PH : 3.0
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 DW
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
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 : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21771
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 (%) : 98.9
REMARK 200 DATA REDUNDANCY : 6.200
REMARK 200 R MERGE (I) : 0.12500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 25.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.50
REMARK 200 R MERGE FOR SHELL (I) : 0.24100
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: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 1RNE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.31
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.95
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 5-12% PEG3 350, 0.6M NACL, 0.1M
REMARK 280 CITRATE (PH 3.0-4.5), VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 295K
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 69.09400
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 69.09400
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 69.09400
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 69.09400
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 69.09400
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 69.09400
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 69.09400
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 69.09400
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 69.09400
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 69.09400
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 69.09400
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 69.09400
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 69.09400
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 69.09400
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 69.09400
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 69.09400
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 69.09400
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 69.09400
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: 16180 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 71630 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -51.0 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 69.09400
REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 -207.28200
REMARK 350 BIOMT3 2 0.000000 -1.000000 0.000000 -276.37600
REMARK 350 BIOMT1 3 0.000000 -1.000000 0.000000 -207.28200
REMARK 350 BIOMT2 3 0.000000 0.000000 -1.000000 -276.37600
REMARK 350 BIOMT3 3 1.000000 0.000000 0.000000 -69.09400
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 27.59 49.03
REMARK 500 ASP A 17 16.35 58.72
REMARK 500 ASN A 75 -65.11 -142.33
REMARK 500 ARG A 139 18.31 48.55
REMARK 500 ARG A 164 -72.20 -73.87
REMARK 500 ASN A 168 -31.98 176.25
REMARK 500 SER A 169 -51.79 64.33
REMARK 500 LYS A 206 36.81 -75.73
REMARK 500 SER A 212 -86.84 -52.70
REMARK 500 THR A 214 46.22 -95.76
REMARK 500 LEU A 215 7.05 -54.30
REMARK 500 THR A 227 3.25 -66.04
REMARK 500 ARG A 251 -168.29 -125.45
REMARK 500 ASP A 254 -177.98 176.67
REMARK 500 GLN A 287 -85.78 -50.27
REMARK 500 GLU A 288 71.67 48.49
REMARK 500 SER A 289 163.78 110.85
REMARK 500 ALA A 299 35.17 -80.92
REMARK 500 MET A 303 115.84 -166.78
REMARK 500 ASN A 332 52.31 39.71
REMARK 500 ASN B 75 -65.24 -142.54
REMARK 500 ARG B 139 22.55 44.89
REMARK 500 ARG B 164 -81.23 -78.07
REMARK 500 ASP B 165 103.34 -12.39
REMARK 500 ASN B 168 25.74 -179.06
REMARK 500 SER B 169 -88.90 37.73
REMARK 500 GLN B 170 -84.52 -6.22
REMARK 500 SER B 171 136.43 -30.63
REMARK 500 PRO B 183 8.32 -56.51
REMARK 500 SER B 212 54.37 -116.34
REMARK 500 SER B 213 132.72 178.14
REMARK 500 ASP B 219 41.17 -90.75
REMARK 500 CYS B 221 176.54 176.75
REMARK 500 LEU B 252 -149.86 -155.53
REMARK 500 PHE B 253 -8.13 -44.52
REMARK 500 PHE B 286 79.57 -66.59
REMARK 500 SER B 289 158.30 165.55
REMARK 500 ALA B 299 21.19 -76.32
REMARK 500 MET B 303 91.81 175.12
REMARK 500 THR B 312 149.98 178.89
REMARK 500 ASN B 332 60.95 39.74
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3VSW RELATED DB: PDB
DBREF 3VSX A 1 340 UNP P00797 RENI_HUMAN 67 406
DBREF 3VSX 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 3VSX ASN B 75 ASN GLYCOSYLATION SITE
MODRES 3VSX ASN A 75 ASN GLYCOSYLATION SITE
HET NAG A 401 14
HET R32 A 402 36
HET NAG B 401 14
HET R32 B 402 36
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM R32 (2S,4S,5S)-5-AMINO-N-(3-AMINO-2,2-DIMETHYL-3-
HETNAM 2 R32 OXOPROPYL)-6-[4-(2-CHLOROPHENYL)-2,2-DIMETHYL-5-
HETNAM 3 R32 OXOPIPERAZIN-1-YL]-4-HYDROXY-2-(PROPAN-2-YL)HEXANAMIDE
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 R32 2(C26 H42 CL N5 O4)
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 ALA A 136 5 5
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 THR A 280 VAL A 285 1 6
HELIX 9 9 GLY A 316 ARG A 321 1 6
HELIX 10 10 TYR B 55 TYR B 60 1 6
HELIX 11 11 ASP B 65 SER B 69 5 5
HELIX 12 12 PRO B 115 MET B 120 1 6
HELIX 13 13 PHE B 132 ALA B 136 5 5
HELIX 14 14 PRO B 142 SER B 149 1 8
HELIX 15 15 SER B 235 GLY B 247 1 13
HELIX 16 16 ASN B 260 LEU B 265 5 6
HELIX 17 17 THR B 280 TYR B 284 1 5
HELIX 18 18 GLY B 316 ARG B 321 1 6
SHEET 1 A 9 LYS A 73 ARG A 82 0
SHEET 2 A 9 THR A 87 VAL A 99 -1 O GLN A 94 N LYS A 73
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 TYR A 15 O GLN A 19
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 TYR A 161 O GLN A 175
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 ALA A 337 N TYR A 324
SHEET 9 A 9 TYR A 186 ASN A 194 -1 N GLU A 187 O LEU A 338
SHEET 1 B13 LYS A 73 ARG A 82 0
SHEET 2 B13 THR A 87 VAL A 99 -1 O GLN A 94 N LYS A 73
SHEET 3 B13 ILE A 102 GLU A 113 -1 O PHE A 108 N SER A 93
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 O LYS A 34 N GLY A 126
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 TYR A 15 O GLN A 19
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 TYR A 161 O GLN A 175
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 ALA A 337 N TYR A 324
SHEET 13 B13 TYR A 186 ASN A 194 -1 N GLU A 187 O LEU A 338
SHEET 1 C 5 LYS A 275 LEU A 279 0
SHEET 2 C 5 ILE A 268 LEU A 272 -1 N LEU A 272 O LYS A 275
SHEET 3 C 5 GLN A 202 SER A 209 -1 N GLY A 207 O HIS A 271
SHEET 4 C 5 CYS A 221 VAL A 225 -1 O CYS A 221 N MET A 205
SHEET 5 C 5 TRP A 313 LEU A 315 1 O TRP A 313 N LEU A 224
SHEET 1 D 2 ILE A 232 GLY A 234 0
SHEET 2 D 2 ILE A 300 ALA A 302 1 O HIS A 301 N ILE A 232
SHEET 1 E 3 LYS A 249 LYS A 250 0
SHEET 2 E 3 TYR A 255 LYS A 258 -1 O VAL A 256 N LYS A 249
SHEET 3 E 3 LEU A 295 THR A 297 -1 O CYS A 296 N VAL A 257
SHEET 1 F 9 LYS B 73 TYR B 83 0
SHEET 2 F 9 GLY B 86 VAL B 99 -1 O GLY B 90 N LEU B 79
SHEET 3 F 9 GLN B 19 ILE B 26 -1 N GLY B 25 O THR B 98
SHEET 4 F 9 SER B 8 TYR B 15 -1 N TYR B 15 O GLN B 19
SHEET 5 F 9 GLY B 174 LEU B 178 -1 O LEU B 178 N SER B 8
SHEET 6 F 9 VAL B 157 TYR B 162 -1 N TYR B 161 O GLN B 175
SHEET 7 F 9 PHE B 323 ASP B 328 -1 O THR B 325 N PHE B 160
SHEET 8 F 9 ARG B 333 LEU B 338 -1 O ARG B 333 N ASP B 328
SHEET 9 F 9 HIS B 191 ASN B 194 -1 N ILE B 193 O ILE B 334
SHEET 1 G13 LYS B 73 TYR B 83 0
SHEET 2 G13 GLY B 86 VAL B 99 -1 O GLY B 90 N LEU B 79
SHEET 3 G13 ILE B 102 GLU B 113 -1 O PHE B 108 N SER B 93
SHEET 4 G13 VAL B 44 PRO B 47 1 N VAL B 44 O GLY B 109
SHEET 5 G13 GLY B 126 GLY B 129 -1 O VAL B 127 N TRP B 45
SHEET 6 G13 GLN B 31 ASP B 38 1 O LYS B 34 N GLY B 126
SHEET 7 G13 GLN B 19 ILE B 26 -1 N GLY B 22 O VAL B 35
SHEET 8 G13 SER B 8 TYR B 15 -1 N TYR B 15 O GLN B 19
SHEET 9 G13 GLY B 174 LEU B 178 -1 O LEU B 178 N SER B 8
SHEET 10 G13 VAL B 157 TYR B 162 -1 N TYR B 161 O GLN B 175
SHEET 11 G13 PHE B 323 ASP B 328 -1 O THR B 325 N PHE B 160
SHEET 12 G13 ARG B 333 LEU B 338 -1 O ARG B 333 N ASP B 328
SHEET 13 G13 HIS B 191 ASN B 194 -1 N ILE B 193 O ILE B 334
SHEET 1 H 7 LYS B 275 LEU B 279 0
SHEET 2 H 7 ILE B 268 LEU B 272 -1 N PHE B 270 O TYR B 277
SHEET 3 H 7 GLN B 202 VAL B 210 -1 N GLY B 207 O HIS B 271
SHEET 4 H 7 CYS B 221 LEU B 224 -1 O CYS B 221 N MET B 205
SHEET 5 H 7 TRP B 313 LEU B 315 1 O LEU B 315 N LEU B 224
SHEET 6 H 7 ILE B 232 GLY B 234 -1 N SER B 233 O ALA B 314
SHEET 7 H 7 ILE B 300 ALA B 302 1 O HIS B 301 N ILE B 232
SHEET 1 I 4 LYS B 249 LYS B 250 0
SHEET 2 I 4 TYR B 255 LYS B 258 -1 O VAL B 256 N LYS B 249
SHEET 3 I 4 LEU B 295 LEU B 298 -1 O CYS B 296 N VAL B 257
SHEET 4 I 4 VAL B 285 PHE B 286 -1 N PHE B 286 O THR B 297
SSBOND 1 CYS A 51 CYS A 58 1555 1555 2.51
SSBOND 2 CYS A 217 CYS A 221 1555 1555 2.90
SSBOND 3 CYS A 259 CYS A 296 1555 1555 2.68
SSBOND 4 CYS B 51 CYS B 58 1555 1555 2.53
SSBOND 5 CYS B 217 CYS B 221 1555 1555 2.75
SSBOND 6 CYS B 259 CYS B 296 1555 1555 2.55
LINK ND2 ASN A 75 C1 NAG A 401 1555 1555 1.46
LINK ND2 ASN B 75 C1 NAG B 401 1555 1555 1.45
CISPEP 1 THR A 28 PRO A 29 0 -0.20
CISPEP 2 LEU A 117 PRO A 118 0 0.43
CISPEP 3 PRO A 307 PRO A 308 0 0.15
CISPEP 4 GLY A 310 PRO A 311 0 0.03
CISPEP 5 THR B 28 PRO B 29 0 -0.27
CISPEP 6 LEU B 117 PRO B 118 0 0.33
CISPEP 7 PRO B 307 PRO B 308 0 0.45
CISPEP 8 GLY B 310 PRO B 311 0 -0.21
CRYST1 138.188 138.188 138.188 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 0.007237 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007237 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007237 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
