HEADER HYDROLASE/HYDROLASE INHIBITOR 28-DEC-10 3Q5H
TITLE CLINICALLY USEFUL ALKYL AMINE RENIN INHIBITORS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RENIN;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 67-406;
COMPND 5 SYNONYM: ANGIOTENSINOGENASE;
COMPND 6 EC: 3.4.23.15;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: REN, RENIN;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: HEK 293;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PCDNA3.1
KEYWDS ASPARTATE PROTEASE, HYPERTENSION, RENIN EXPRESSION, RENIN INHIBITOR,
KEYWDS 2 ASPARTYL PROTEASE, CLEAVAGE ON PAIR OF BASIC RESIDUES, DISEASE
KEYWDS 3 MUTATION, GLYCOPROTEIN, MEMBRANE, PROTEASE, SECRETED, HYDROLASE-
KEYWDS 4 HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR Z.WU,B.M.MCKEEVER
REVDAT 5 13-SEP-23 3Q5H 1 HETSYN
REVDAT 4 29-JUL-20 3Q5H 1 COMPND REMARK HETNAM LINK
REVDAT 4 2 1 SITE ATOM
REVDAT 3 17-JUL-19 3Q5H 1 REMARK LINK
REVDAT 2 24-SEP-14 3Q5H 1 JRNL
REVDAT 1 30-NOV-11 3Q5H 0
JRNL AUTH L.JIA,R.D.SIMPSON,J.YUAN,Z.XU,W.ZHAO,S.CACATIAN,C.M.TICE,
JRNL AUTH 2 J.GUO,A.ISHCHENKO,S.B.SINGH,Z.WU,B.M.MCKEEVER,Y.BUKHTIYAROV,
JRNL AUTH 3 J.A.JOHNSON,C.P.DOE,R.K.HARRISON,G.M.MCGEEHAN,L.W.DILLARD,
JRNL AUTH 4 J.J.BALDWIN,D.A.CLAREMON
JRNL TITL DISCOVERY OF VTP-27999, AN ALKYL AMINE RENIN INHIBITOR WITH
JRNL TITL 2 POTENTIAL FOR CLINICAL UTILITY.
JRNL REF ACS MED CHEM LETT V. 2 747 2011
JRNL REFN ISSN 1948-5875
JRNL PMID 24900262
JRNL DOI 10.1021/ML200137X
REMARK 2
REMARK 2 RESOLUTION. 2.16 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0102
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.16
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.92
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.8
REMARK 3 NUMBER OF REFLECTIONS : 39698
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.226
REMARK 3 R VALUE (WORKING SET) : 0.224
REMARK 3 FREE R VALUE : 0.268
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2099
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.16
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.22
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2179
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 72.13
REMARK 3 BIN R VALUE (WORKING SET) : 0.3560
REMARK 3 BIN FREE R VALUE SET COUNT : 106
REMARK 3 BIN FREE R VALUE : 0.4700
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5204
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 106
REMARK 3 SOLVENT ATOMS : 168
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 42.46
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.03000
REMARK 3 B22 (A**2) : 0.01000
REMARK 3 B33 (A**2) : 0.02000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.279
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.223
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.188
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.626
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.944
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.928
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5469 ; 0.020 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7419 ; 1.953 ; 1.982
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 669 ; 7.966 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 224 ;37.049 ;24.196
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 864 ;18.887 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 20 ;18.433 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 839 ; 0.129 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4079 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 3329 ; 1.099 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5376 ; 2.019 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2140 ; 3.002 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2043 ; 4.780 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
REMARK 3 U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 3Q5H COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-FEB-11.
REMARK 100 THE DEPOSITION ID IS D_1000063218.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-AUG-06
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.0-8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X8C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.100
REMARK 200 MONOCHROMATOR : SI (111) DOUBLE-CRYSTAL
REMARK 200 MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 41821
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.160
REMARK 200 RESOLUTION RANGE LOW (A) : 48.930
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.6
REMARK 200 DATA REDUNDANCY : 5.000
REMARK 200 R MERGE (I) : 0.08600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.3100
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: PDB ENTRY 3GW5
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.98
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.67
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS-HCL, 0.2 M AMMONIUM
REMARK 280 SULFATE, 18-26% PEG3550, 5 MG/ML RENIN, 1 MM INHIBITOR, PH 7.0-
REMARK 280 8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 278K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 27.32500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 74.50300
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 48.92500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 74.50300
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.32500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 48.92500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 LEU A -5
REMARK 465 THR A -4
REMARK 465 LEU A -3
REMARK 465 LEU B -5
REMARK 465 THR B -4
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O7 NAG C 1 O HOH A 1017 1.75
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 ARG A 157 NE - CZ - NH1 ANGL. DEV. = -3.1 DEGREES
REMARK 500 LEU A 205 CA - CB - CG ANGL. DEV. = 14.0 DEGREES
REMARK 500 ARG A 307 NE - CZ - NH1 ANGL. DEV. = -3.5 DEGREES
REMARK 500 LEU B 161 CA - C - N ANGL. DEV. = -18.9 DEGREES
REMARK 500 ARG B 315 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG B 316 NE - CZ - NH1 ANGL. DEV. = -4.3 DEGREES
REMARK 500 ARG B 316 NE - CZ - NH2 ANGL. DEV. = 4.0 DEGREES
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 ASN A -1 19.57 -140.09
REMARK 500 ASN A 67 -52.51 -141.60
REMARK 500 SER A 160D 111.05 90.56
REMARK 500 PRO A 172 0.55 -69.04
REMARK 500 ARG A 240 -165.81 -112.50
REMARK 500 ALA A 285 46.84 -87.71
REMARK 500 ARG B 47 -33.79 -37.68
REMARK 500 LEU B 47A 25.35 -64.23
REMARK 500 ASP B 60 9.43 -151.70
REMARK 500 ASN B 67 -53.04 -138.68
REMARK 500 ARG B 132 15.41 47.98
REMARK 500 SER B 160B 5.51 -53.77
REMARK 500 GLN B 160C -96.41 -150.29
REMARK 500 SER B 160D 109.14 4.62
REMARK 500 ALA B 285 45.55 -92.39
REMARK 500 ASN B 318 62.66 36.68
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLY B 144 VAL B 145 -142.32
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 LEU B 161 23.92
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3GW5 RELATED DB: PDB
REMARK 900 RENIN COMPLEXED WITH A SIMILAR ALKYL AMINE INHIBITOR
REMARK 900 RELATED ID: 3KM4 RELATED DB: PDB
REMARK 900 RENIN COMPLEXED WITH A SIMILAR ALKYL AMINE INHIBITOR
REMARK 900 RELATED ID: 3Q3T RELATED DB: PDB
REMARK 900 RENIN COMPLEXED WITH A SIMILAR ALKYL AMINE INHIBITOR
REMARK 900 RELATED ID: 3Q4B RELATED DB: PDB
REMARK 900 RENIN COMPLEXED WITH A SIMILAR ALKYL AMINE INHIBITOR
DBREF 3Q5H A -5 326 UNP P00797 RENI_HUMAN 67 406
DBREF 3Q5H B -5 326 UNP P00797 RENI_HUMAN 67 406
SEQRES 1 A 340 LEU THR LEU GLY ASN THR THR SER SER VAL ILE LEU THR
SEQRES 2 A 340 ASN TYR MET ASP THR GLN TYR TYR GLY GLU ILE GLY ILE
SEQRES 3 A 340 GLY THR PRO PRO GLN THR PHE LYS VAL VAL PHE ASP THR
SEQRES 4 A 340 GLY SER SER ASN VAL TRP VAL PRO SER SER LYS CYS SER
SEQRES 5 A 340 ARG LEU TYR THR ALA CYS VAL TYR HIS LYS LEU PHE ASP
SEQRES 6 A 340 ALA SER ASP SER SER SER TYR LYS HIS ASN GLY THR GLU
SEQRES 7 A 340 LEU THR LEU ARG TYR SER THR GLY THR VAL SER GLY PHE
SEQRES 8 A 340 LEU SER GLN ASP ILE ILE THR VAL GLY GLY ILE THR VAL
SEQRES 9 A 340 THR GLN MET PHE GLY GLU VAL THR GLU MET PRO ALA LEU
SEQRES 10 A 340 PRO PHE MET LEU ALA GLU PHE ASP GLY VAL VAL GLY MET
SEQRES 11 A 340 GLY PHE ILE GLU GLN ALA ILE GLY ARG VAL THR PRO ILE
SEQRES 12 A 340 PHE ASP ASN ILE ILE SER GLN GLY VAL LEU LYS GLU ASP
SEQRES 13 A 340 VAL PHE SER PHE TYR TYR ASN ARG ASP SER GLU ASN SER
SEQRES 14 A 340 GLN SER LEU GLY GLY GLN ILE VAL LEU GLY GLY SER ASP
SEQRES 15 A 340 PRO GLN HIS TYR GLU GLY ASN PHE HIS TYR ILE ASN LEU
SEQRES 16 A 340 ILE LYS THR GLY VAL TRP GLN ILE GLN MET LYS GLY VAL
SEQRES 17 A 340 SER VAL GLY SER SER THR LEU LEU CYS GLU ASP GLY CYS
SEQRES 18 A 340 LEU ALA LEU VAL ASP THR GLY ALA SER TYR ILE SER GLY
SEQRES 19 A 340 SER THR SER SER ILE GLU LYS LEU MET GLU ALA LEU GLY
SEQRES 20 A 340 ALA LYS LYS ARG LEU PHE ASP TYR VAL VAL LYS CYS ASN
SEQRES 21 A 340 GLU GLY PRO THR LEU PRO ASP ILE SER PHE HIS LEU GLY
SEQRES 22 A 340 GLY LYS GLU TYR THR LEU THR SER ALA ASP TYR VAL PHE
SEQRES 23 A 340 GLN GLU SER TYR SER SER LYS LYS LEU CYS THR LEU ALA
SEQRES 24 A 340 ILE HIS ALA MET ASP ILE PRO PRO PRO THR GLY PRO THR
SEQRES 25 A 340 TRP ALA LEU GLY ALA THR PHE ILE ARG LYS PHE TYR THR
SEQRES 26 A 340 GLU PHE ASP ARG ARG ASN ASN ARG ILE GLY PHE ALA LEU
SEQRES 27 A 340 ALA ARG
SEQRES 1 B 340 LEU THR LEU GLY ASN THR THR SER SER VAL ILE LEU THR
SEQRES 2 B 340 ASN TYR MET ASP THR GLN TYR TYR GLY GLU ILE GLY ILE
SEQRES 3 B 340 GLY THR PRO PRO GLN THR PHE LYS VAL VAL PHE ASP THR
SEQRES 4 B 340 GLY SER SER ASN VAL TRP VAL PRO SER SER LYS CYS SER
SEQRES 5 B 340 ARG LEU TYR THR ALA CYS VAL TYR HIS LYS LEU PHE ASP
SEQRES 6 B 340 ALA SER ASP SER SER SER TYR LYS HIS ASN GLY THR GLU
SEQRES 7 B 340 LEU THR LEU ARG TYR SER THR GLY THR VAL SER GLY PHE
SEQRES 8 B 340 LEU SER GLN ASP ILE ILE THR VAL GLY GLY ILE THR VAL
SEQRES 9 B 340 THR GLN MET PHE GLY GLU VAL THR GLU MET PRO ALA LEU
SEQRES 10 B 340 PRO PHE MET LEU ALA GLU PHE ASP GLY VAL VAL GLY MET
SEQRES 11 B 340 GLY PHE ILE GLU GLN ALA ILE GLY ARG VAL THR PRO ILE
SEQRES 12 B 340 PHE ASP ASN ILE ILE SER GLN GLY VAL LEU LYS GLU ASP
SEQRES 13 B 340 VAL PHE SER PHE TYR TYR ASN ARG ASP SER GLU ASN SER
SEQRES 14 B 340 GLN SER LEU GLY GLY GLN ILE VAL LEU GLY GLY SER ASP
SEQRES 15 B 340 PRO GLN HIS TYR GLU GLY ASN PHE HIS TYR ILE ASN LEU
SEQRES 16 B 340 ILE LYS THR GLY VAL TRP GLN ILE GLN MET LYS GLY VAL
SEQRES 17 B 340 SER VAL GLY SER SER THR LEU LEU CYS GLU ASP GLY CYS
SEQRES 18 B 340 LEU ALA LEU VAL ASP THR GLY ALA SER TYR ILE SER GLY
SEQRES 19 B 340 SER THR SER SER ILE GLU LYS LEU MET GLU ALA LEU GLY
SEQRES 20 B 340 ALA LYS LYS ARG LEU PHE ASP TYR VAL VAL LYS CYS ASN
SEQRES 21 B 340 GLU GLY PRO THR LEU PRO ASP ILE SER PHE HIS LEU GLY
SEQRES 22 B 340 GLY LYS GLU TYR THR LEU THR SER ALA ASP TYR VAL PHE
SEQRES 23 B 340 GLN GLU SER TYR SER SER LYS LYS LEU CYS THR LEU ALA
SEQRES 24 B 340 ILE HIS ALA MET ASP ILE PRO PRO PRO THR GLY PRO THR
SEQRES 25 B 340 TRP ALA LEU GLY ALA THR PHE ILE ARG LYS PHE TYR THR
SEQRES 26 B 340 GLU PHE ASP ARG ARG ASN ASN ARG ILE GLY PHE ALA LEU
SEQRES 27 B 340 ALA ARG
MODRES 3Q5H ASN A 67 ASN GLYCOSYLATION SITE
HET NAG C 1 14
HET NAG C 2 14
HET CL A 500 1
HET RX6 A 335 36
HET CL A 336 1
HET CL A 337 1
HET CL A 338 1
HET CL B 500 1
HET RX6 B 335 36
HET CL B 336 1
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM CL CHLORIDE ION
HETNAM RX6 METHYL (2-{(R)-(3-CHLOROPHENYL)[(3R)-1-({(2S)-1-
HETNAM 2 RX6 (METHYLAMINO)-3-[(3R)-TETRAHYDRO-2H-PYRAN-3-YL]PROPAN-
HETNAM 3 RX6 2-YL}CARBAMOYL)PIPERIDIN-3-YL]METHOXY}ETHYL)CARBAMATE
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 CL 6(CL 1-)
FORMUL 5 RX6 2(C26 H41 CL N4 O5)
FORMUL 12 HOH *168(H2 O)
HELIX 1 1 TYR A 47B TYR A 52 1 6
HELIX 2 2 ASP A 57 SER A 61 5 5
HELIX 3 3 PRO A 108 MET A 113 1 6
HELIX 4 4 PHE A 125 VAL A 133 5 9
HELIX 5 5 PRO A 135 SER A 142 1 8
HELIX 6 6 ASP A 171 TYR A 175 5 5
HELIX 7 7 SER A 224 GLY A 236 1 13
HELIX 8 8 GLU A 251 LEU A 255 5 5
HELIX 9 9 THR A 270 VAL A 275 1 6
HELIX 10 10 GLY A 302 LYS A 308 1 7
HELIX 11 11 TYR B 47B HIS B 53 1 7
HELIX 12 12 ASP B 57 SER B 61 5 5
HELIX 13 13 PRO B 108 MET B 113 1 6
HELIX 14 14 PHE B 125 VAL B 133 5 9
HELIX 15 15 PRO B 135 SER B 142 1 8
HELIX 16 16 SER B 224 LEU B 235 1 12
HELIX 17 17 ASN B 250 LEU B 255 5 6
HELIX 18 18 THR B 270 VAL B 275 1 6
HELIX 19 19 GLY B 302 ARG B 307 1 6
SHEET 1 A 9 LYS A 65 TYR A 75 0
SHEET 2 A 9 GLY A 78 VAL A 91 -1 O GLY A 78 N TYR A 75
SHEET 3 A 9 GLN A 13 ILE A 20 -1 N GLY A 19 O THR A 90
SHEET 4 A 9 SER A 2 TYR A 9 -1 N TYR A 9 O GLN A 13
SHEET 5 A 9 GLY A 163 LEU A 167 -1 O GLY A 163 N LEU A 6
SHEET 6 A 9 VAL A 150 TYR A 155 -1 N TYR A 154 O GLN A 164
SHEET 7 A 9 PHE A 309 ASP A 314 -1 O PHE A 313 N PHE A 151
SHEET 8 A 9 ARG A 319 LEU A 324 -1 O GLY A 321 N GLU A 312
SHEET 9 A 9 HIS A 180 ASN A 183 -1 N ILE A 182 O ILE A 320
SHEET 1 B13 LYS A 65 TYR A 75 0
SHEET 2 B13 GLY A 78 VAL A 91 -1 O GLY A 78 N TYR A 75
SHEET 3 B13 ILE A 94 GLU A 106 -1 O VAL A 96 N ILE A 89
SHEET 4 B13 VAL A 38 PRO A 41 1 N VAL A 40 O VAL A 104
SHEET 5 B13 GLY A 119 GLY A 122 -1 O VAL A 120 N TRP A 39
SHEET 6 B13 GLN A 25 ASP A 32 1 N VAL A 30 O VAL A 121
SHEET 7 B13 GLN A 13 ILE A 20 -1 N ILE A 20 O GLN A 25
SHEET 8 B13 SER A 2 TYR A 9 -1 N TYR A 9 O GLN A 13
SHEET 9 B13 GLY A 163 LEU A 167 -1 O GLY A 163 N LEU A 6
SHEET 10 B13 VAL A 150 TYR A 155 -1 N TYR A 154 O GLN A 164
SHEET 11 B13 PHE A 309 ASP A 314 -1 O PHE A 313 N PHE A 151
SHEET 12 B13 ARG A 319 LEU A 324 -1 O GLY A 321 N GLU A 312
SHEET 13 B13 HIS A 180 ASN A 183 -1 N ILE A 182 O ILE A 320
SHEET 1 C 3 GLN A 191 MET A 194 0
SHEET 2 C 3 CYS A 210 VAL A 214 -1 O CYS A 210 N MET A 194
SHEET 3 C 3 TRP A 299 LEU A 301 1 O LEU A 301 N LEU A 213
SHEET 1 D 3 GLY A 196 VAL A 199 0
SHEET 2 D 3 ILE A 258 LEU A 262 -1 O SER A 259 N SER A 198
SHEET 3 D 3 LYS A 265 LEU A 269 -1 O TYR A 267 N PHE A 260
SHEET 1 E 2 ILE A 221 GLY A 223 0
SHEET 2 E 2 ILE A 286 ALA A 288 1 O HIS A 287 N ILE A 221
SHEET 1 F 3 LYS A 238 LYS A 239 0
SHEET 2 F 3 TYR A 245 LYS A 248 -1 O VAL A 246 N LYS A 238
SHEET 3 F 3 LEU A 281D THR A 283 -1 O CYS A 282 N VAL A 247
SHEET 1 G 9 GLU B 70 ARG B 74 0
SHEET 2 G 9 THR B 79 VAL B 91 -1 O GLY B 82 N LEU B 71
SHEET 3 G 9 GLN B 13 ILE B 20 -1 N GLY B 19 O THR B 90
SHEET 4 G 9 SER B 2 TYR B 9 -1 N TYR B 9 O GLN B 13
SHEET 5 G 9 GLY B 163 LEU B 167 -1 O GLY B 163 N LEU B 6
SHEET 6 G 9 VAL B 150 TYR B 155 -1 N TYR B 154 O GLN B 164
SHEET 7 G 9 PHE B 309 ASP B 314 -1 O PHE B 313 N PHE B 151
SHEET 8 G 9 ARG B 319 ALA B 325 -1 O GLY B 321 N GLU B 312
SHEET 9 G 9 TYR B 175 ASN B 183 -1 N GLU B 176 O LEU B 324
SHEET 1 H13 GLU B 70 ARG B 74 0
SHEET 2 H13 THR B 79 VAL B 91 -1 O GLY B 82 N LEU B 71
SHEET 3 H13 ILE B 94 GLU B 106 -1 O VAL B 96 N ILE B 89
SHEET 4 H13 VAL B 38 PRO B 41 1 N VAL B 40 O VAL B 104
SHEET 5 H13 GLY B 119 GLY B 122 -1 O VAL B 120 N TRP B 39
SHEET 6 H13 GLN B 25 ASP B 32 1 N VAL B 30 O VAL B 121
SHEET 7 H13 GLN B 13 ILE B 20 -1 N ILE B 20 O GLN B 25
SHEET 8 H13 SER B 2 TYR B 9 -1 N TYR B 9 O GLN B 13
SHEET 9 H13 GLY B 163 LEU B 167 -1 O GLY B 163 N LEU B 6
SHEET 10 H13 VAL B 150 TYR B 155 -1 N TYR B 154 O GLN B 164
SHEET 11 H13 PHE B 309 ASP B 314 -1 O PHE B 313 N PHE B 151
SHEET 12 H13 ARG B 319 ALA B 325 -1 O GLY B 321 N GLU B 312
SHEET 13 H13 TYR B 175 ASN B 183 -1 N GLU B 176 O LEU B 324
SHEET 1 I 4 SER B 202 LEU B 205 0
SHEET 2 I 4 GLN B 191 VAL B 199 -1 N VAL B 197 O LEU B 204
SHEET 3 I 4 ILE B 258 LEU B 262 -1 O SER B 259 N SER B 198
SHEET 4 I 4 LYS B 265 LEU B 269 -1 O LEU B 269 N ILE B 258
SHEET 1 J 6 SER B 202 LEU B 205 0
SHEET 2 J 6 GLN B 191 VAL B 199 -1 N VAL B 197 O LEU B 204
SHEET 3 J 6 CYS B 210 VAL B 214 -1 O CYS B 210 N MET B 194
SHEET 4 J 6 TRP B 299 LEU B 301 1 O LEU B 301 N LEU B 213
SHEET 5 J 6 ILE B 221 GLY B 223 -1 N SER B 222 O ALA B 300
SHEET 6 J 6 ILE B 286 ALA B 288 1 O HIS B 287 N ILE B 221
SHEET 1 K 3 LYS B 238 LYS B 239 0
SHEET 2 K 3 TYR B 245 LYS B 248 -1 O VAL B 246 N LYS B 238
SHEET 3 K 3 LEU B 281D THR B 283 -1 O CYS B 282 N VAL B 247
SSBOND 1 CYS A 45 CYS A 50 1555 1555 2.00
SSBOND 2 CYS A 206 CYS A 210 1555 1555 2.04
SSBOND 3 CYS A 249 CYS A 282 1555 1555 2.04
SSBOND 4 CYS B 45 CYS B 50 1555 1555 2.02
SSBOND 5 CYS B 206 CYS B 210 1555 1555 2.08
SSBOND 6 CYS B 249 CYS B 282 1555 1555 2.11
LINK ND2 ASN A 67 C1 NAG C 1 1555 1555 1.49
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.44
CISPEP 1 THR A 22 PRO A 23 0 -1.62
CISPEP 2 GLY A 92 GLY A 93 0 21.91
CISPEP 3 LEU A 110 PRO A 111 0 2.64
CISPEP 4 PRO A 293 PRO A 294 0 -0.37
CISPEP 5 GLY A 296 PRO A 297 0 0.65
CISPEP 6 THR B 22 PRO B 23 0 -5.11
CISPEP 7 LEU B 110 PRO B 111 0 13.69
CISPEP 8 PRO B 293 PRO B 294 0 1.70
CISPEP 9 GLY B 296 PRO B 297 0 -8.63
CRYST1 54.650 97.850 149.006 90.00 90.00 90.00 P 21 21 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.018298 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010220 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006711 0.00000
(ATOM LINES ARE NOT SHOWN.)
END