HEADER HYDROLASE/HYDROLASE INHIBITOR 27-SEP-95 1BIM
TITLE CRYSTALLOGRAPHIC STUDIES ON THE BINDING MODES OF P2-P3 BUTANEDIAMIDE
TITLE 2 RENIN INHIBITORS
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;
COMPND 7 OTHER_DETAILS: GLYCOSYLATED
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: CMV IE-HUMAN PREPRORENIN CDNA, REN;
SOURCE 6 EXPRESSION_SYSTEM: CANIS LUPUS FAMILIARIS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: DOG;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9615;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: FAMILIARIS;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMNC RETROVIRAL VECTOR;
SOURCE 11 EXPRESSION_SYSTEM_GENE: CMV IE-HUMAN PREPRORENIN CDNA;
SOURCE 12 OTHER_DETAILS: STABLY TRANSFERRED
KEYWDS ASPARTIC PROTEINASE, ASPARTYL PROTEASE, CLEAVAGE ON PAIR OF BASIC
KEYWDS 2 RESIDUES, DISEASE MUTATION, DISULFIDE BOND, GLYCOPROTEIN, HYDROLASE,
KEYWDS 3 MEMBRANE, PROTEASE, SECRETED, ZYMOGEN, HYDROLASE-HYDROLASE INHIBITOR
KEYWDS 4 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR L.TONG
REVDAT 7 09-MAR-22 1BIM 1 REMARK
REVDAT 6 14-AUG-19 1BIM 1 REMARK
REVDAT 5 17-JUL-19 1BIM 1 REMARK
REVDAT 4 18-JAN-12 1BIM 1 REMARK
REVDAT 3 13-JUL-11 1BIM 1 VERSN
REVDAT 2 24-FEB-09 1BIM 1 VERSN
REVDAT 1 29-JAN-96 1BIM 0
JRNL AUTH L.TONG,S.PAV,D.LAMARRE,B.SIMONEAU,P.LAVALLEE,G.JUNG
JRNL TITL CRYSTALLOGRAPHIC STUDIES ON THE BINDING MODES OF P2-P3
JRNL TITL 2 BUTANEDIAMIDE RENIN INHIBITORS.
JRNL REF J.BIOL.CHEM. V. 270 29520 1995
JRNL REFN ISSN 0021-9258
JRNL PMID 7493993
JRNL DOI 10.1074/JBC.270.49.29520
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : TNT
REMARK 3 AUTHORS : TRONRUD,TEN EYCK,MATTHEWS
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 6.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 17435
REMARK 3
REMARK 3 USING DATA ABOVE SIGMA CUTOFF.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : 0.178
REMARK 3 R VALUE (WORKING SET) : 0.178
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3
REMARK 3 USING ALL DATA, NO SIGMA CUTOFF.
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 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5125
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 96
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 WILSON B VALUE (FROM FCALC, A**2) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. RMS WEIGHT COUNT
REMARK 3 BOND LENGTHS (A) : NULL ; NULL ; NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 TRIGONAL CARBON PLANES (A) : NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES (A) : NULL ; NULL ; NULL
REMARK 3 ISOTROPIC THERMAL FACTORS (A**2) : NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS (A) : NULL ; NULL ; NULL
REMARK 3
REMARK 3 INCORRECT CHIRAL-CENTERS (COUNT) : 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 RESTRAINT LIBRARIES.
REMARK 3 STEREOCHEMISTRY : NULL
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1BIM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000171801.
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) : NULL
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
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 : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
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) : 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: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.62
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.29
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 71.45000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 71.45000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 71.45000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 71.45000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 71.45000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 71.45000
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 71.45000
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 71.45000
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 71.45000
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 71.45000
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 71.45000
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 71.45000
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 71.45000
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 71.45000
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 71.45000
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 71.45000
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 71.45000
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 71.45000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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: DIMERIC
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 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 ASN A 160A
REMARK 465 SER A 160B
REMARK 465 GLN A 160C
REMARK 465 GLU B 159A
REMARK 465 ASN B 159B
REMARK 465 SER B 159C
REMARK 465 GLN B 159D
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG B 74 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 132 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 238 CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 17 CD GLU A 17 OE1 0.089
REMARK 500 GLU A 70 CD GLU A 70 OE2 0.084
REMARK 500 GLU A 106 CD GLU A 106 OE2 0.069
REMARK 500 GLU A 116 CD GLU A 116 OE2 0.073
REMARK 500 GLU A 148 CD GLU A 148 OE2 0.100
REMARK 500 GLU A 160 CD GLU A 160 OE1 0.092
REMARK 500 GLU A 207 CD GLU A 207 OE1 0.093
REMARK 500 GLU A 229 CD GLU A 229 OE1 0.084
REMARK 500 GLU A 233 CD GLU A 233 OE2 0.067
REMARK 500 GLU A 251 CD GLU A 251 OE2 0.097
REMARK 500 GLU A 266 CD GLU A 266 OE2 0.070
REMARK 500 GLU A 278 CD GLU A 278 OE1 0.074
REMARK 500 GLU B 17 CD GLU B 17 OE2 0.088
REMARK 500 GLU B 70 CD GLU B 70 OE2 0.095
REMARK 500 GLU B 103 CD GLU B 103 OE1 0.077
REMARK 500 GLU B 106 CD GLU B 106 OE1 0.080
REMARK 500 GLU B 127 CD GLU B 127 OE1 0.085
REMARK 500 GLU B 148 CD GLU B 148 OE1 0.110
REMARK 500 GLU B 176 CD GLU B 176 OE1 0.082
REMARK 500 GLU B 207 CD GLU B 207 OE2 0.091
REMARK 500 GLU B 229 CD GLU B 229 OE1 0.100
REMARK 500 GLU B 233 CD GLU B 233 OE1 0.092
REMARK 500 GLU B 251 CD GLU B 251 OE1 0.079
REMARK 500 GLU B 266 CD GLU B 266 OE2 0.075
REMARK 500 GLU B 278 CD GLU B 278 OE2 0.099
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP A 11 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 ASP A 32 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 ASP A 57 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ASP A 60 CB - CG - OD1 ANGL. DEV. = 7.5 DEGREES
REMARK 500 ASP A 60 CB - CG - OD2 ANGL. DEV. = -8.7 DEGREES
REMARK 500 ARG A 74 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG A 74 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 GLN A 86 N - CA - CB ANGL. DEV. = 10.9 DEGREES
REMARK 500 THR A 90 N - CA - CB ANGL. DEV. = 13.5 DEGREES
REMARK 500 PRO A 108 C - N - CD ANGL. DEV. = -12.7 DEGREES
REMARK 500 ARG A 132 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 ARG A 132 NE - CZ - NH2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 ASP A 138 CB - CG - OD2 ANGL. DEV. = 7.4 DEGREES
REMARK 500 ASP A 149 CB - CG - OD1 ANGL. DEV. = 6.9 DEGREES
REMARK 500 ASP A 149 CB - CG - OD2 ANGL. DEV. = -7.6 DEGREES
REMARK 500 ASP A 158 CB - CG - OD2 ANGL. DEV. = -6.4 DEGREES
REMARK 500 ASP A 171 CB - CG - OD2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 HIS A 174 CA - CB - CG ANGL. DEV. = -11.5 DEGREES
REMARK 500 ASP A 208 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 ASP A 215 CB - CG - OD1 ANGL. DEV. = -5.5 DEGREES
REMARK 500 ARG A 240 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ASP A 273 CB - CG - OD1 ANGL. DEV. = -8.0 DEGREES
REMARK 500 ASP A 273 CB - CG - OD2 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ASP A 290 CB - CG - OD2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 ASP A 314 CB - CG - OD1 ANGL. DEV. = 10.3 DEGREES
REMARK 500 ASP A 314 CB - CG - OD2 ANGL. DEV. = -10.4 DEGREES
REMARK 500 ARG A 319 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 ARG A 319 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 TYR B 14 CB - CG - CD2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 TYR B 15 CB - CG - CD1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ASP B 32 CB - CG - OD1 ANGL. DEV. = 6.9 DEGREES
REMARK 500 ASP B 57 CB - CG - OD2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 ASP B 60 CB - CG - OD2 ANGL. DEV. = -8.0 DEGREES
REMARK 500 ASP B 87 CB - CG - OD1 ANGL. DEV. = 7.3 DEGREES
REMARK 500 ASP B 87 CB - CG - OD2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 ASP B 138 CB - CG - OD1 ANGL. DEV. = 6.5 DEGREES
REMARK 500 ASP B 149 CB - CG - OD1 ANGL. DEV. = -8.6 DEGREES
REMARK 500 ASP B 149 CB - CG - OD2 ANGL. DEV. = 8.2 DEGREES
REMARK 500 ARG B 157 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ASP B 171 CB - CG - OD2 ANGL. DEV. = -7.8 DEGREES
REMARK 500 ASP B 208 CB - CG - OD1 ANGL. DEV. = -7.8 DEGREES
REMARK 500 ASP B 208 CB - CG - OD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ARG B 240 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG B 240 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 CYS B 249 N - CA - CB ANGL. DEV. = 10.9 DEGREES
REMARK 500 ASP B 273 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ASP B 273 CB - CG - OD2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 ASP B 290 CB - CG - OD1 ANGL. DEV. = 6.3 DEGREES
REMARK 500 ARG B 307 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 ASP B 314 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 51 ANGLE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
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 ASP A 11 -5.04 68.17
REMARK 500 THR A 33 23.59 -77.20
REMARK 500 TRP A 39 142.51 -179.44
REMARK 500 PRO A 41 141.50 -37.37
REMARK 500 LYS A 44 -4.64 -54.37
REMARK 500 ASN A 67 -89.56 -121.16
REMARK 500 PHE A 101 -167.09 -129.89
REMARK 500 PHE A 112 -36.74 -39.15
REMARK 500 LEU A 146 130.03 -35.22
REMARK 500 GLN A 164 134.75 -171.79
REMARK 500 PRO A 172 1.57 -55.05
REMARK 500 ILE A 185 -96.45 -60.76
REMARK 500 SER A 201 -40.82 -141.16
REMARK 500 THR A 203 89.48 -68.73
REMARK 500 CYS A 206 12.04 54.29
REMARK 500 ASP A 208 31.29 72.88
REMARK 500 CYS A 210 -175.56 -174.59
REMARK 500 ARG A 240 -147.46 -114.24
REMARK 500 LEU A 242 -70.72 -68.61
REMARK 500 PRO A 253 15.88 -60.23
REMARK 500 GLN A 277 99.84 -63.36
REMARK 500 SER A 279 168.29 167.55
REMARK 500 LEU A 284 -174.11 -62.95
REMARK 500 MET A 289 108.36 -176.25
REMARK 500 ARG A 316 -85.72 -41.53
REMARK 500 ASN A 317 0.96 -67.47
REMARK 500 ASN B -1 10.21 -152.81
REMARK 500 THR B 1 122.71 -172.04
REMARK 500 LYS B 44 -6.54 -59.88
REMARK 500 TYR B 64 135.67 -38.22
REMARK 500 ASN B 67 -37.11 -146.58
REMARK 500 PHE B 112 -35.87 -14.11
REMARK 500 MET B 123 35.35 -90.44
REMARK 500 GLU B 127 -61.30 -26.64
REMARK 500 GLN B 128 39.87 -79.63
REMARK 500 LYS B 147 -49.96 -26.88
REMARK 500 PRO B 172 -3.27 -59.53
REMARK 500 ILE B 182 106.46 -163.60
REMARK 500 LYS B 186 145.46 -179.32
REMARK 500 TRP B 190 69.37 -104.02
REMARK 500 LEU B 204 -43.66 -131.73
REMARK 500 CYS B 206 35.08 70.96
REMARK 500 LEU B 242 -16.72 40.39
REMARK 500 PHE B 243 -87.82 -148.29
REMARK 500 ASN B 250 -25.28 -35.72
REMARK 500 PRO B 253 -19.42 -42.55
REMARK 500 PHE B 276 68.34 -105.17
REMARK 500 GLN B 277 83.90 -56.15
REMARK 500 ALA B 285 50.50 -99.01
REMARK 500 TYR B 310 122.51 -37.67
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 HET GROUPS DMF, PHC, HII, CHA AND IP4 FORM AN INHIBITOR AND
REMARK 600 REFERRED TO AS INHIBITOR NUMBER 3 IN THE MANUSCRIPT.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0QB A 391
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0QB B 391
DBREF 1BIM A -2 326 UNP P00797 RENI_HUMAN 70 406
DBREF 1BIM B -2 326 UNP P00797 RENI_HUMAN 70 406
SEQRES 1 A 337 GLY ASN THR THR SER SER VAL ILE LEU THR ASN TYR MET
SEQRES 2 A 337 ASP THR GLN TYR TYR GLY GLU ILE GLY ILE GLY THR PRO
SEQRES 3 A 337 PRO GLN THR PHE LYS VAL VAL PHE ASP THR GLY SER SER
SEQRES 4 A 337 ASN VAL TRP VAL PRO SER SER LYS CYS SER ARG LEU TYR
SEQRES 5 A 337 THR ALA CYS VAL TYR HIS LYS LEU PHE ASP ALA SER ASP
SEQRES 6 A 337 SER SER SER TYR LYS HIS ASN GLY THR GLU LEU THR LEU
SEQRES 7 A 337 ARG TYR SER THR GLY THR VAL SER GLY PHE LEU SER GLN
SEQRES 8 A 337 ASP ILE ILE THR VAL GLY GLY ILE THR VAL THR GLN MET
SEQRES 9 A 337 PHE GLY GLU VAL THR GLU MET PRO ALA LEU PRO PHE MET
SEQRES 10 A 337 LEU ALA GLU PHE ASP GLY VAL VAL GLY MET GLY PHE ILE
SEQRES 11 A 337 GLU GLN ALA ILE GLY ARG VAL THR PRO ILE PHE ASP ASN
SEQRES 12 A 337 ILE ILE SER GLN GLY VAL LEU LYS GLU ASP VAL PHE SER
SEQRES 13 A 337 PHE TYR TYR ASN ARG ASP SER GLU ASN SER GLN SER LEU
SEQRES 14 A 337 GLY GLY GLN ILE VAL LEU GLY GLY SER ASP PRO GLN HIS
SEQRES 15 A 337 TYR GLU GLY ASN PHE HIS TYR ILE ASN LEU ILE LYS THR
SEQRES 16 A 337 GLY VAL TRP GLN ILE GLN MET LYS GLY VAL SER VAL GLY
SEQRES 17 A 337 SER SER THR LEU LEU CYS GLU ASP GLY CYS LEU ALA LEU
SEQRES 18 A 337 VAL ASP THR GLY ALA SER TYR ILE SER GLY SER THR SER
SEQRES 19 A 337 SER ILE GLU LYS LEU MET GLU ALA LEU GLY ALA LYS LYS
SEQRES 20 A 337 ARG LEU PHE ASP TYR VAL VAL LYS CYS ASN GLU GLY PRO
SEQRES 21 A 337 THR LEU PRO ASP ILE SER PHE HIS LEU GLY GLY LYS GLU
SEQRES 22 A 337 TYR THR LEU THR SER ALA ASP TYR VAL PHE GLN GLU SER
SEQRES 23 A 337 TYR SER SER LYS LYS LEU CYS THR LEU ALA ILE HIS ALA
SEQRES 24 A 337 MET ASP ILE PRO PRO PRO THR GLY PRO THR TRP ALA LEU
SEQRES 25 A 337 GLY ALA THR PHE ILE ARG LYS PHE TYR THR GLU PHE ASP
SEQRES 26 A 337 ARG ARG ASN ASN ARG ILE GLY PHE ALA LEU ALA ARG
SEQRES 1 B 337 GLY ASN THR THR SER SER VAL ILE LEU THR ASN TYR MET
SEQRES 2 B 337 ASP THR GLN TYR TYR GLY GLU ILE GLY ILE GLY THR PRO
SEQRES 3 B 337 PRO GLN THR PHE LYS VAL VAL PHE ASP THR GLY SER SER
SEQRES 4 B 337 ASN VAL TRP VAL PRO SER SER LYS CYS SER ARG LEU TYR
SEQRES 5 B 337 THR ALA CYS VAL TYR HIS LYS LEU PHE ASP ALA SER ASP
SEQRES 6 B 337 SER SER SER TYR LYS HIS ASN GLY THR GLU LEU THR LEU
SEQRES 7 B 337 ARG TYR SER THR GLY THR VAL SER GLY PHE LEU SER GLN
SEQRES 8 B 337 ASP ILE ILE THR VAL GLY GLY ILE THR VAL THR GLN MET
SEQRES 9 B 337 PHE GLY GLU VAL THR GLU MET PRO ALA LEU PRO PHE MET
SEQRES 10 B 337 LEU ALA GLU PHE ASP GLY VAL VAL GLY MET GLY PHE ILE
SEQRES 11 B 337 GLU GLN ALA ILE GLY ARG VAL THR PRO ILE PHE ASP ASN
SEQRES 12 B 337 ILE ILE SER GLN GLY VAL LEU LYS GLU ASP VAL PHE SER
SEQRES 13 B 337 PHE TYR TYR ASN ARG ASP SER GLU ASN SER GLN SER LEU
SEQRES 14 B 337 GLY GLY GLN ILE VAL LEU GLY GLY SER ASP PRO GLN HIS
SEQRES 15 B 337 TYR GLU GLY ASN PHE HIS TYR ILE ASN LEU ILE LYS THR
SEQRES 16 B 337 GLY VAL TRP GLN ILE GLN MET LYS GLY VAL SER VAL GLY
SEQRES 17 B 337 SER SER THR LEU LEU CYS GLU ASP GLY CYS LEU ALA LEU
SEQRES 18 B 337 VAL ASP THR GLY ALA SER TYR ILE SER GLY SER THR SER
SEQRES 19 B 337 SER ILE GLU LYS LEU MET GLU ALA LEU GLY ALA LYS LYS
SEQRES 20 B 337 ARG LEU PHE ASP TYR VAL VAL LYS CYS ASN GLU GLY PRO
SEQRES 21 B 337 THR LEU PRO ASP ILE SER PHE HIS LEU GLY GLY LYS GLU
SEQRES 22 B 337 TYR THR LEU THR SER ALA ASP TYR VAL PHE GLN GLU SER
SEQRES 23 B 337 TYR SER SER LYS LYS LEU CYS THR LEU ALA ILE HIS ALA
SEQRES 24 B 337 MET ASP ILE PRO PRO PRO THR GLY PRO THR TRP ALA LEU
SEQRES 25 B 337 GLY ALA THR PHE ILE ARG LYS PHE TYR THR GLU PHE ASP
SEQRES 26 B 337 ARG ARG ASN ASN ARG ILE GLY PHE ALA LEU ALA ARG
HET 0QB A 391 48
HET 0QB B 391 48
HETNAM 0QB (2S)-2-[(2-AMINO-1,3-THIAZOL-4-YL)METHYL]-N~1~-{(1S,
HETNAM 2 0QB 2S)-1-(CYCLOHEXYLMETHYL)-2-HYDROXY-2-[(3R)-1,5,5-
HETNAM 3 0QB TRIMETHYL-2-OXOPYRROLIDIN-3-YL]ETHYL}-N~4~-[2-
HETNAM 4 0QB (DIMETHYLAMINO)-2-OXOETHYL]-N~4~-[(1S)-1-
HETNAM 5 0QB PHENYLETHYL]BUTANEDIAMIDE
HETSYN 0QB P2-P3 BUTANEDIAMIDE RENIN INHIBITOR (3)
FORMUL 3 0QB 2(C36 H54 N6 O5 S)
HELIX 1 1 THR A 48 VAL A 51 1 4
HELIX 2 2 ALA A 58 ASP A 60 5 3
HELIX 3 3 PHE A 112 LEU A 114 5 3
HELIX 4 4 ILE A 130 ARG A 132 5 3
HELIX 5 5 ILE A 136 ILE A 141 1 6
HELIX 6 6 THR A 225 LEU A 235 1 11
HELIX 7 7 CYS A 249 THR A 254 5 6
HELIX 8 8 ALA A 303 ILE A 306 1 4
HELIX 9 9 THR B 48 TYR B 52 1 5
HELIX 10 10 ALA B 58 ASP B 60 5 3
HELIX 11 11 ALA B 109 PHE B 112 1 4
HELIX 12 12 ILE B 136 GLN B 143 1 8
HELIX 13 13 THR B 225 LEU B 235 1 11
HELIX 14 14 CYS B 249 THR B 254 5 6
HELIX 15 15 SER B 271 TYR B 274 1 4
HELIX 16 16 ALA B 303 LYS B 308 1 6
SHEET 1 A 6 SER A 2 LEU A 6 0
SHEET 2 A 6 GLY A 163 LEU A 167 -1 N LEU A 167 O SER A 2
SHEET 3 A 6 VAL A 150 TYR A 155 -1 N TYR A 154 O GLN A 164
SHEET 4 A 6 PHE A 309 ASP A 314 -1 N PHE A 313 O PHE A 151
SHEET 5 A 6 ARG A 319 LEU A 324 -1 N ALA A 323 O TYR A 310
SHEET 6 A 6 HIS A 180 ILE A 182 -1 N ILE A 182 O ILE A 320
SHEET 1 B 4 THR A 7 TYR A 9 0
SHEET 2 B 4 GLN A 13 ILE A 20 -1 N TYR A 15 O THR A 7
SHEET 3 B 4 GLN A 25 ASP A 32 -1 N VAL A 29 O GLY A 16
SHEET 4 B 4 GLY A 119 GLY A 122 1 N GLY A 119 O VAL A 30
SHEET 1 C 3 ILE A 18 ILE A 20 0
SHEET 2 C 3 LEU A 84 VAL A 91 -1 N THR A 90 O GLY A 19
SHEET 3 C 3 ILE A 94 GLY A 102 -1 N PHE A 101 O SER A 85
SHEET 1 D 2 GLU A 70 TYR A 75 0
SHEET 2 D 2 GLY A 78 PHE A 83 -1 N GLY A 82 O LEU A 71
SHEET 1 E 5 TRP A 299 LEU A 301 0
SHEET 2 E 5 CYS A 210 VAL A 214 1 N LEU A 213 O TRP A 299
SHEET 3 E 5 GLN A 191 VAL A 199 -1 N MET A 194 O CYS A 210
SHEET 4 E 5 ILE A 258 LEU A 262 -1 N HIS A 261 O LYS A 195
SHEET 5 E 5 LYS A 265 LEU A 269 -1 N LEU A 269 O ILE A 258
SHEET 1 F 2 VAL A 246 LYS A 248 0
SHEET 2 F 2 LEU A 281 THR A 283 -1 N CYS A 282 O VAL A 247
SHEET 1 G 5 SER B 2 ILE B 5 0
SHEET 2 G 5 GLY B 163 LEU B 167 -1 N LEU B 167 O SER B 2
SHEET 3 G 5 VAL B 150 TYR B 155 -1 N TYR B 154 O GLN B 164
SHEET 4 G 5 PHE B 309 ASP B 314 -1 N PHE B 313 O PHE B 151
SHEET 5 G 5 ARG B 319 LEU B 324 -1 N ALA B 323 O TYR B 310
SHEET 1 H 4 LEU B 6 TYR B 9 0
SHEET 2 H 4 GLN B 13 GLY B 19 -1 N TYR B 15 O THR B 7
SHEET 3 H 4 THR B 26 ASP B 32 -1 N VAL B 29 O GLY B 16
SHEET 4 H 4 GLY B 119 GLY B 122 1 N GLY B 119 O VAL B 30
SHEET 1 I 4 VAL B 38 PRO B 41 0
SHEET 2 I 4 PHE B 101 MET B 107 1 N GLY B 102 O VAL B 38
SHEET 3 I 4 THR B 79 LEU B 84 -1 N PHE B 83 O GLU B 103
SHEET 4 I 4 GLU B 70 ARG B 74 -1 N LEU B 73 O VAL B 80
SHEET 1 J 2 ASP B 87 VAL B 91 0
SHEET 2 J 2 ILE B 94 GLN B 99 -1 N GLN B 99 O ASP B 87
SHEET 1 K 3 GLN B 191 MET B 194 0
SHEET 2 K 3 CYS B 210 VAL B 214 -1 N ALA B 212 O ILE B 192
SHEET 3 K 3 TRP B 299 LEU B 301 1 N TRP B 299 O LEU B 213
SHEET 1 L 4 LYS B 265 LEU B 269 0
SHEET 2 L 4 ILE B 258 LEU B 262 -1 N LEU B 262 O LYS B 265
SHEET 3 L 4 VAL B 197 VAL B 199 -1 N SER B 198 O SER B 259
SHEET 4 L 4 SER B 202 LEU B 205 -1 N LEU B 205 O VAL B 197
SHEET 1 M 2 ILE B 221 GLY B 223 0
SHEET 2 M 2 ILE B 286 ALA B 288 1 N HIS B 287 O ILE B 221
SHEET 1 N 2 VAL B 246 LYS B 248 0
SHEET 2 N 2 LEU B 281 THR B 283 -1 N CYS B 282 O VAL B 247
SSBOND 1 CYS A 45 CYS A 50 1555 1555 1.95
SSBOND 2 CYS A 206 CYS A 210 1555 1555 2.03
SSBOND 3 CYS A 249 CYS A 282 1555 1555 2.05
SSBOND 4 CYS B 45 CYS B 50 1555 1555 2.08
SSBOND 5 CYS B 206 CYS B 210 1555 1555 2.04
SSBOND 6 CYS B 249 CYS B 282 1555 1555 2.04
CISPEP 1 THR A 22 PRO A 23 0 -5.49
CISPEP 2 LEU A 110 PRO A 111 0 16.43
CISPEP 3 PRO A 293 PRO A 294 0 2.84
CISPEP 4 GLY A 296 PRO A 297 0 0.05
CISPEP 5 THR B 22 PRO B 23 0 4.03
CISPEP 6 LEU B 110 PRO B 111 0 9.53
CISPEP 7 PRO B 293 PRO B 294 0 24.38
CISPEP 8 GLY B 296 PRO B 297 0 -7.37
SITE 1 AC1 16 ASP A 32 GLY A 34 TYR A 75 SER A 76
SITE 2 AC1 16 THR A 77 PRO A 111 PHE A 117 ASP A 215
SITE 3 AC1 16 GLY A 217 ALA A 218 SER A 219 TYR A 220
SITE 4 AC1 16 SER A 222 MET A 289 ILE A 291 ALA A 300
SITE 1 AC2 16 THR B 12 GLN B 13 ASP B 32 TYR B 75
SITE 2 AC2 16 SER B 76 THR B 77 PHE B 112 LEU B 114
SITE 3 AC2 16 LEU B 213 ASP B 215 GLY B 217 ALA B 218
SITE 4 AC2 16 SER B 219 TYR B 220 SER B 222 ILE B 291
CRYST1 142.900 142.900 142.900 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 0.006998 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006998 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006998 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
