HEADER HYDROLASE 15-FEB-06 2G1Y
TITLE KETOPIPERAZINE-BASED RENIN INHIBITORS: OPTIMIZATION OF THE "C" RING
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: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PROTEIN-LIGAND COMPLEXES, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.D.HOLSWORTH,M.JALAIEA,E.ZHANGA,P.MCCONNELLA
REVDAT 4 29-JUL-20 2G1Y 1 COMPND REMARK HETNAM LINK
REVDAT 4 2 1 SITE
REVDAT 3 13-JUL-11 2G1Y 1 VERSN
REVDAT 2 24-FEB-09 2G1Y 1 VERSN
REVDAT 1 13-JUN-06 2G1Y 0
JRNL AUTH D.D.HOLSWORTH,C.CAI,X.M.CHENG,W.L.CODY,D.M.DOWNING,N.ERASGA,
JRNL AUTH 2 C.LEE,N.A.POWELL,J.J.EDNUNDS,M.STIER,M.JALAIE,E.ZHANG,
JRNL AUTH 3 P.MCCONNELL,M.J.RYAN,J.BRYANT,T.LI,A.KASANI,E.HALL,R.SUBEDI,
JRNL AUTH 4 M.RAHIM,S.MAITI
JRNL TITL KETOPIPERAZINE-BASED RENIN INHIBITORS: OPTIMIZATION OF THE
JRNL TITL 2 "C" RING
JRNL REF BIOORG.MED.CHEM.LETT. V. 16 2500 2006
JRNL REFN ISSN 0960-894X
JRNL PMID 16480874
JRNL DOI 10.1016/J.BMCL.2006.01.084
REMARK 2
REMARK 2 RESOLUTION. 2.50 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 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 32307
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.197
REMARK 3 FREE R VALUE : 0.252
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 3231
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 : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
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 : 5144
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 84
REMARK 3 SOLVENT ATOMS : 322
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.500
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2G1Y COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-FEB-06.
REMARK 100 THE DEPOSITION ID IS D_1000036586.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 17-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
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 : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32307
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
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 (%) : 1.0
REMARK 200 DATA REDUNDANCY : NULL
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) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : 1.0
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: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.22
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 70.51900
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 70.51900
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 70.51900
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 70.51900
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 70.51900
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 70.51900
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 70.51900
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 70.51900
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 70.51900
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 70.51900
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 70.51900
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 70.51900
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 70.51900
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 70.51900
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 70.51900
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 70.51900
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 70.51900
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 70.51900
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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: 22730 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 71620 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 2.0 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 141.03800
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 70.51900
REMARK 350 BIOMT3 2 0.000000 -1.000000 0.000000 211.55700
REMARK 350 BIOMT1 3 0.000000 1.000000 0.000000 -70.51900
REMARK 350 BIOMT2 3 0.000000 0.000000 -1.000000 211.55700
REMARK 350 BIOMT3 3 -1.000000 0.000000 0.000000 141.03800
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7640 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 39570 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 2.0 KCAL/MOL
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 BIOMT1 2 0.000000 0.000000 -1.000000 141.03800
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 70.51900
REMARK 350 BIOMT3 2 0.000000 -1.000000 0.000000 211.55700
REMARK 350 BIOMT1 3 0.000000 1.000000 0.000000 -70.51900
REMARK 350 BIOMT2 3 0.000000 0.000000 -1.000000 211.55700
REMARK 350 BIOMT3 3 -1.000000 0.000000 0.000000 141.03800
REMARK 350
REMARK 350 BIOMOLECULE: 5
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7030 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 40100 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 3.0 KCAL/MOL
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 BIOMT1 2 0.000000 0.000000 -1.000000 141.03800
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 70.51900
REMARK 350 BIOMT3 2 0.000000 -1.000000 0.000000 211.55700
REMARK 350 BIOMT1 3 0.000000 1.000000 0.000000 -70.51900
REMARK 350 BIOMT2 3 0.000000 0.000000 -1.000000 211.55700
REMARK 350 BIOMT3 3 -1.000000 0.000000 0.000000 141.03800
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 70 -54.08 -156.23
REMARK 500 ASP A 160 161.76 -47.08
REMARK 500 SER A 164 105.97 -49.65
REMARK 500 GLN A 165 -16.39 179.59
REMARK 500 SER A 208 106.84 166.35
REMARK 500 THR A 209 80.23 -67.41
REMARK 500 CYS A 212 46.89 37.94
REMARK 500 ASP A 214 -4.40 61.64
REMARK 500 TYR A 226 -165.53 -127.38
REMARK 500 SER A 230 153.72 -46.91
REMARK 500 ARG A 246 -161.36 -101.65
REMARK 500 GLN A 282 85.92 -66.56
REMARK 500 ALA A 294 24.36 -79.69
REMARK 500 ASP B 12 -1.05 66.91
REMARK 500 TYR B 50 96.59 -65.78
REMARK 500 SER B 62 5.69 -69.80
REMARK 500 HIS B 69 152.26 -49.86
REMARK 500 ASN B 70 71.40 174.90
REMARK 500 THR B 80 -84.76 -103.74
REMARK 500 SER B 207 12.36 -141.21
REMARK 500 THR B 209 77.68 -68.61
REMARK 500 ARG B 246 -87.33 -60.62
REMARK 500 LEU B 247 -49.25 -133.72
REMARK 500 ALA B 294 32.40 -96.62
REMARK 500 MET B 298 99.84 -163.81
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2G1N RELATED DB: PDB
REMARK 900 RELATED ID: 2G1R RELATED DB: PDB
REMARK 900 RELATED ID: 2G1O RELATED DB: PDB
REMARK 900 RELATED ID: 2G1S RELATED DB: PDB
REMARK 900 RELATED ID: 2G20 RELATED DB: PDB
REMARK 900 RELATED ID: 2G21 RELATED DB: PDB
REMARK 900 RELATED ID: 2G22 RELATED DB: PDB
REMARK 900 RELATED ID: 2G24 RELATED DB: PDB
REMARK 900 RELATED ID: 2G26 RELATED DB: PDB
REMARK 900 RELATED ID: 2G27 RELATED DB: PDB
DBREF 2G1Y A 3 335 UNP P00797 RENI_HUMAN 74 406
DBREF 2G1Y B 3 335 UNP P00797 RENI_HUMAN 74 406
SEQRES 1 A 333 SER SER VAL ILE LEU THR ASN TYR MET ASP THR GLN TYR
SEQRES 2 A 333 TYR GLY GLU ILE GLY ILE GLY THR PRO PRO GLN THR PHE
SEQRES 3 A 333 LYS VAL VAL PHE ASP THR GLY SER SER ASN VAL TRP VAL
SEQRES 4 A 333 PRO SER SER LYS CYS SER ARG LEU TYR THR ALA CYS VAL
SEQRES 5 A 333 TYR HIS LYS LEU PHE ASP ALA SER ASP SER SER SER TYR
SEQRES 6 A 333 LYS HIS ASN GLY THR GLU LEU THR LEU ARG TYR SER THR
SEQRES 7 A 333 GLY THR VAL SER GLY PHE LEU SER GLN ASP ILE ILE THR
SEQRES 8 A 333 VAL GLY GLY ILE THR VAL THR GLN MET PHE GLY GLU VAL
SEQRES 9 A 333 THR GLU MET PRO ALA LEU PRO PHE MET LEU ALA GLU PHE
SEQRES 10 A 333 ASP GLY VAL VAL GLY MET GLY PHE ILE GLU GLN ALA ILE
SEQRES 11 A 333 GLY ARG VAL THR PRO ILE PHE ASP ASN ILE ILE SER GLN
SEQRES 12 A 333 GLY VAL LEU LYS GLU ASP VAL PHE SER PHE TYR TYR ASN
SEQRES 13 A 333 ARG ASP SER GLU ASN SER GLN SER LEU GLY GLY GLN ILE
SEQRES 14 A 333 VAL LEU GLY GLY SER ASP PRO GLN HIS TYR GLU GLY ASN
SEQRES 15 A 333 PHE HIS TYR ILE ASN LEU ILE LYS THR GLY VAL TRP GLN
SEQRES 16 A 333 ILE GLN MET LYS GLY VAL SER VAL GLY SER SER THR LEU
SEQRES 17 A 333 LEU CYS GLU ASP GLY CYS LEU ALA LEU VAL ASP THR GLY
SEQRES 18 A 333 ALA SER TYR ILE SER GLY SER THR SER SER ILE GLU LYS
SEQRES 19 A 333 LEU MET GLU ALA LEU GLY ALA LYS LYS ARG LEU PHE ASP
SEQRES 20 A 333 TYR VAL VAL LYS CYS ASN GLU GLY PRO THR LEU PRO ASP
SEQRES 21 A 333 ILE SER PHE HIS LEU GLY GLY LYS GLU TYR THR LEU THR
SEQRES 22 A 333 SER ALA ASP TYR VAL PHE GLN GLU SER TYR SER SER LYS
SEQRES 23 A 333 LYS LEU CYS THR LEU ALA ILE HIS ALA MET ASP ILE PRO
SEQRES 24 A 333 PRO PRO THR GLY PRO THR TRP ALA LEU GLY ALA THR PHE
SEQRES 25 A 333 ILE ARG LYS PHE TYR THR GLU PHE ASP ARG ARG ASN ASN
SEQRES 26 A 333 ARG ILE GLY PHE ALA LEU ALA ARG
SEQRES 1 B 333 SER SER VAL ILE LEU THR ASN TYR MET ASP THR GLN TYR
SEQRES 2 B 333 TYR GLY GLU ILE GLY ILE GLY THR PRO PRO GLN THR PHE
SEQRES 3 B 333 LYS VAL VAL PHE ASP THR GLY SER SER ASN VAL TRP VAL
SEQRES 4 B 333 PRO SER SER LYS CYS SER ARG LEU TYR THR ALA CYS VAL
SEQRES 5 B 333 TYR HIS LYS LEU PHE ASP ALA SER ASP SER SER SER TYR
SEQRES 6 B 333 LYS HIS ASN GLY THR GLU LEU THR LEU ARG TYR SER THR
SEQRES 7 B 333 GLY THR VAL SER GLY PHE LEU SER GLN ASP ILE ILE THR
SEQRES 8 B 333 VAL GLY GLY ILE THR VAL THR GLN MET PHE GLY GLU VAL
SEQRES 9 B 333 THR GLU MET PRO ALA LEU PRO PHE MET LEU ALA GLU PHE
SEQRES 10 B 333 ASP GLY VAL VAL GLY MET GLY PHE ILE GLU GLN ALA ILE
SEQRES 11 B 333 GLY ARG VAL THR PRO ILE PHE ASP ASN ILE ILE SER GLN
SEQRES 12 B 333 GLY VAL LEU LYS GLU ASP VAL PHE SER PHE TYR TYR ASN
SEQRES 13 B 333 ARG ASP SER GLU ASN SER GLN SER LEU GLY GLY GLN ILE
SEQRES 14 B 333 VAL LEU GLY GLY SER ASP PRO GLN HIS TYR GLU GLY ASN
SEQRES 15 B 333 PHE HIS TYR ILE ASN LEU ILE LYS THR GLY VAL TRP GLN
SEQRES 16 B 333 ILE GLN MET LYS GLY VAL SER VAL GLY SER SER THR LEU
SEQRES 17 B 333 LEU CYS GLU ASP GLY CYS LEU ALA LEU VAL ASP THR GLY
SEQRES 18 B 333 ALA SER TYR ILE SER GLY SER THR SER SER ILE GLU LYS
SEQRES 19 B 333 LEU MET GLU ALA LEU GLY ALA LYS LYS ARG LEU PHE ASP
SEQRES 20 B 333 TYR VAL VAL LYS CYS ASN GLU GLY PRO THR LEU PRO ASP
SEQRES 21 B 333 ILE SER PHE HIS LEU GLY GLY LYS GLU TYR THR LEU THR
SEQRES 22 B 333 SER ALA ASP TYR VAL PHE GLN GLU SER TYR SER SER LYS
SEQRES 23 B 333 LYS LEU CYS THR LEU ALA ILE HIS ALA MET ASP ILE PRO
SEQRES 24 B 333 PRO PRO THR GLY PRO THR TRP ALA LEU GLY ALA THR PHE
SEQRES 25 B 333 ILE ARG LYS PHE TYR THR GLU PHE ASP ARG ARG ASN ASN
SEQRES 26 B 333 ARG ILE GLY PHE ALA LEU ALA ARG
MODRES 2G1Y ASN A 70 ASN GLYCOSYLATION SITE
MODRES 2G1Y ASN B 70 ASN GLYCOSYLATION SITE
HET NAG A 985 14
HET 5IG A 885 28
HET NAG B 986 14
HET 5IG B 886 28
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM 5IG 6-(2,4-DIAMINO-6-ETHYLPYRIMIDIN-5-YL)-4-(3-
HETNAM 2 5IG METHOXYPROPYL)-2,2-DIMETHYL-2H-1,4-BENZOXAZIN-3(4H)-
HETNAM 3 5IG ONE
FORMUL 3 NAG 2(C8 H15 N O6)
FORMUL 4 5IG 2(C20 H27 N5 O3)
FORMUL 7 HOH *322(H2 O)
HELIX 1 1 TYR A 50 TYR A 55 1 6
HELIX 2 2 ASP A 60 SER A 64 5 5
HELIX 3 3 PRO A 110 MET A 115 1 6
HELIX 4 4 PHE A 127 VAL A 135 5 9
HELIX 5 5 PRO A 137 GLN A 145 1 9
HELIX 6 6 ASP A 177 GLN A 179 5 3
HELIX 7 7 SER A 230 GLY A 242 1 13
HELIX 8 8 ASN A 255 LEU A 260 5 6
HELIX 9 9 THR A 275 VAL A 280 1 6
HELIX 10 10 GLY A 311 ARG A 316 1 6
HELIX 11 11 TYR B 50 TYR B 55 1 6
HELIX 12 12 ASP B 60 SER B 64 5 5
HELIX 13 13 PRO B 110 MET B 115 1 6
HELIX 14 14 PRO B 137 GLN B 145 1 9
HELIX 15 15 ASP B 177 GLN B 179 5 3
HELIX 16 16 SER B 230 GLY B 242 1 13
HELIX 17 17 ASN B 255 LEU B 260 5 6
HELIX 18 18 THR B 275 VAL B 280 1 6
HELIX 19 19 GLY B 311 LYS B 317 1 7
SHEET 1 A 9 LYS A 68 TYR A 78 0
SHEET 2 A 9 GLY A 81 VAL A 94 -1 O VAL A 83 N LEU A 76
SHEET 3 A 9 GLN A 14 ILE A 21 -1 N GLY A 20 O THR A 93
SHEET 4 A 9 SER A 4 TYR A 10 -1 N TYR A 10 O GLN A 14
SHEET 5 A 9 GLY A 169 LEU A 173 -1 O GLY A 169 N LEU A 7
SHEET 6 A 9 VAL A 152 TYR A 157 -1 N TYR A 156 O GLN A 170
SHEET 7 A 9 PHE A 318 ASP A 323 -1 O THR A 320 N PHE A 155
SHEET 8 A 9 ARG A 328 ALA A 334 -1 O GLY A 330 N GLU A 321
SHEET 9 A 9 TYR A 181 ASN A 189 -1 N ILE A 188 O ILE A 329
SHEET 1 B13 LYS A 68 TYR A 78 0
SHEET 2 B13 GLY A 81 VAL A 94 -1 O VAL A 83 N LEU A 76
SHEET 3 B13 ILE A 97 GLU A 108 -1 O VAL A 99 N ILE A 92
SHEET 4 B13 VAL A 39 PRO A 42 1 N VAL A 39 O GLY A 104
SHEET 5 B13 GLY A 121 GLY A 124 -1 O VAL A 122 N TRP A 40
SHEET 6 B13 GLN A 26 ASP A 33 1 N VAL A 31 O VAL A 123
SHEET 7 B13 GLN A 14 ILE A 21 -1 N GLY A 17 O VAL A 30
SHEET 8 B13 SER A 4 TYR A 10 -1 N TYR A 10 O GLN A 14
SHEET 9 B13 GLY A 169 LEU A 173 -1 O GLY A 169 N LEU A 7
SHEET 10 B13 VAL A 152 TYR A 157 -1 N TYR A 156 O GLN A 170
SHEET 11 B13 PHE A 318 ASP A 323 -1 O THR A 320 N PHE A 155
SHEET 12 B13 ARG A 328 ALA A 334 -1 O GLY A 330 N GLU A 321
SHEET 13 B13 TYR A 181 ASN A 189 -1 N ILE A 188 O ILE A 329
SHEET 1 C 7 LYS A 270 LEU A 274 0
SHEET 2 C 7 ILE A 263 LEU A 267 -1 N ILE A 263 O LEU A 274
SHEET 3 C 7 GLN A 197 VAL A 205 -1 N GLY A 202 O HIS A 266
SHEET 4 C 7 CYS A 216 VAL A 220 -1 O CYS A 216 N MET A 200
SHEET 5 C 7 TRP A 308 LEU A 310 1 O LEU A 310 N LEU A 219
SHEET 6 C 7 ILE A 227 GLY A 229 -1 N SER A 228 O ALA A 309
SHEET 7 C 7 ILE A 295 ALA A 297 1 O HIS A 296 N ILE A 227
SHEET 1 D 3 LYS A 244 LYS A 245 0
SHEET 2 D 3 TYR A 250 LYS A 253 -1 O VAL A 251 N LYS A 244
SHEET 3 D 3 LEU A 290 THR A 292 -1 O CYS A 291 N VAL A 252
SHEET 1 E 9 LYS B 68 ARG B 77 0
SHEET 2 E 9 THR B 82 VAL B 94 -1 O LEU B 87 N THR B 72
SHEET 3 E 9 GLN B 14 ILE B 21 -1 N GLY B 20 O THR B 93
SHEET 4 E 9 SER B 4 TYR B 10 -1 N THR B 8 O TYR B 16
SHEET 5 E 9 GLY B 169 LEU B 173 -1 O GLY B 169 N LEU B 7
SHEET 6 E 9 VAL B 152 TYR B 157 -1 N SER B 154 O VAL B 172
SHEET 7 E 9 PHE B 318 ASP B 323 -1 O PHE B 322 N PHE B 153
SHEET 8 E 9 ARG B 328 ALA B 334 -1 O GLY B 330 N GLU B 321
SHEET 9 E 9 TYR B 181 ASN B 189 -1 N GLU B 182 O LEU B 333
SHEET 1 F13 LYS B 68 ARG B 77 0
SHEET 2 F13 THR B 82 VAL B 94 -1 O LEU B 87 N THR B 72
SHEET 3 F13 ILE B 97 GLU B 108 -1 O ILE B 97 N VAL B 94
SHEET 4 F13 VAL B 39 PRO B 42 1 N VAL B 41 O VAL B 106
SHEET 5 F13 GLY B 121 GLY B 124 -1 O VAL B 122 N TRP B 40
SHEET 6 F13 GLN B 26 ASP B 33 1 N VAL B 31 O VAL B 123
SHEET 7 F13 GLN B 14 ILE B 21 -1 N GLY B 17 O VAL B 30
SHEET 8 F13 SER B 4 TYR B 10 -1 N THR B 8 O TYR B 16
SHEET 9 F13 GLY B 169 LEU B 173 -1 O GLY B 169 N LEU B 7
SHEET 10 F13 VAL B 152 TYR B 157 -1 N SER B 154 O VAL B 172
SHEET 11 F13 PHE B 318 ASP B 323 -1 O PHE B 322 N PHE B 153
SHEET 12 F13 ARG B 328 ALA B 334 -1 O GLY B 330 N GLU B 321
SHEET 13 F13 TYR B 181 ASN B 189 -1 N GLU B 182 O LEU B 333
SHEET 1 G 5 GLN B 197 MET B 200 0
SHEET 2 G 5 CYS B 216 VAL B 220 -1 O ALA B 218 N ILE B 198
SHEET 3 G 5 TRP B 308 LEU B 310 1 O LEU B 310 N LEU B 219
SHEET 4 G 5 ILE B 227 GLY B 229 -1 N SER B 228 O ALA B 309
SHEET 5 G 5 ILE B 295 ALA B 297 1 O HIS B 296 N ILE B 227
SHEET 1 H 4 SER B 208 LEU B 211 0
SHEET 2 H 4 VAL B 203 VAL B 205 -1 N VAL B 203 O LEU B 211
SHEET 3 H 4 ILE B 263 LEU B 267 -1 O SER B 264 N SER B 204
SHEET 4 H 4 LYS B 270 LEU B 274 -1 O TYR B 272 N PHE B 265
SHEET 1 I 3 LYS B 244 LYS B 245 0
SHEET 2 I 3 TYR B 250 LYS B 253 -1 O VAL B 251 N LYS B 244
SHEET 3 I 3 LEU B 290 THR B 292 -1 O CYS B 291 N VAL B 252
SSBOND 1 CYS A 46 CYS A 53 1555 1555 2.03
SSBOND 2 CYS A 212 CYS A 216 1555 1555 2.03
SSBOND 3 CYS A 254 CYS A 291 1555 1555 2.03
SSBOND 4 CYS B 46 CYS B 53 1555 1555 2.03
SSBOND 5 CYS B 212 CYS B 216 1555 1555 2.03
SSBOND 6 CYS B 254 CYS B 291 1555 1555 2.03
LINK ND2 ASN A 70 C1 NAG A 985 1555 1555 1.45
LINK ND2 ASN B 70 C1 NAG B 986 1555 1555 1.45
CISPEP 1 THR A 23 PRO A 24 0 -0.24
CISPEP 2 LEU A 112 PRO A 113 0 0.60
CISPEP 3 PRO A 302 PRO A 303 0 0.01
CISPEP 4 GLY A 305 PRO A 306 0 0.05
CISPEP 5 THR B 23 PRO B 24 0 -0.08
CISPEP 6 LEU B 112 PRO B 113 0 0.08
CISPEP 7 PRO B 302 PRO B 303 0 0.17
CISPEP 8 GLY B 305 PRO B 306 0 -0.23
CRYST1 141.038 141.038 141.038 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 0.007046 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007046 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007046 0.00000
(ATOM LINES ARE NOT SHOWN.)
END