HEADER HYDROLASE/HYDROLASE INHIBITOR 04-APR-14 4Q1N
TITLE STRUCTURE-BASED DESIGN OF 4-HYDROXY-3,5-SUBSTITUTED PIPERIDINES AS
TITLE 2 DIRECT 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
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_TAXID: 9606;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HEK
KEYWDS ASPARTIC PROTEASE, ANGIOTENSIN, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR N.SCHIERING,A.D'ARCY,O.IRIE,F.YOKOKAWA
REVDAT 3 29-JUL-20 4Q1N 1 COMPND REMARK HETNAM LINK
REVDAT 3 2 1 SITE
REVDAT 2 22-NOV-17 4Q1N 1 REMARK
REVDAT 1 06-AUG-14 4Q1N 0
JRNL AUTH T.EHARA,O.IRIE,T.KOSAKA,T.KANAZAWA,W.BREITENSTEIN,P.GROSCHE,
JRNL AUTH 2 N.OSTERMANN,M.SUZUKI,S.KAWAKAMI,K.KONISHI,Y.HITOMI,A.TOYAO,
JRNL AUTH 3 H.GUNJI,F.CUMIN,N.SCHIERING,T.WAGNER,D.F.RIGEL,R.L.WEBB,
JRNL AUTH 4 J.MAIBAUM,F.YOKOKAWA
JRNL TITL STRUCTURE-BASED DESIGN OF SUBSTITUTED PIPERIDINES AS A NEW
JRNL TITL 2 CLASS OF HIGHLY EFFICACIOUS ORAL DIRECT RENIN INHIBITORS.
JRNL REF ACS MED CHEM LETT V. 5 787 2014
JRNL REFN ISSN 1948-5875
JRNL PMID 25050166
JRNL DOI 10.1021/ML500137B
REMARK 2
REMARK 2 RESOLUTION. 2.09 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.4
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.09
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 62.99
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 55184
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) : 0.170
REMARK 3 R VALUE (WORKING SET) : 0.169
REMARK 3 FREE R VALUE : 0.189
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2759
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 : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.09
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.14
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.93
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 4055
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.1883
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3852
REMARK 3 BIN R VALUE (WORKING SET) : 0.1879
REMARK 3 BIN FREE R VALUE : 0.1943
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.01
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 203
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 : 5184
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 113
REMARK 3 SOLVENT ATOMS : 415
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 34.77
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.42
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) : 0.224
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.149
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.955
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.949
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 5469 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 7434 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1833 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 113 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 802 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 5469 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 732 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 6597 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.011
REMARK 3 BOND ANGLES (DEGREES) : 1.16
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 4.07
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 17.22
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 66.5947 11.6126 41.0916
REMARK 3 T TENSOR
REMARK 3 T11: -0.0210 T22: -0.0815
REMARK 3 T33: -0.0347 T12: 0.0017
REMARK 3 T13: -0.0394 T23: -0.0129
REMARK 3 L TENSOR
REMARK 3 L11: 0.6594 L22: 0.6197
REMARK 3 L33: 1.1896 L12: 0.2926
REMARK 3 L13: -0.4380 L23: -0.4687
REMARK 3 S TENSOR
REMARK 3 S11: -0.0908 S12: 0.0724 S13: -0.0153
REMARK 3 S21: -0.1492 S22: 0.0295 S23: 0.0333
REMARK 3 S31: 0.1361 S32: -0.0913 S33: 0.0612
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { B|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 83.1262 35.0445 17.3247
REMARK 3 T TENSOR
REMARK 3 T11: -0.0212 T22: -0.0999
REMARK 3 T33: -0.0977 T12: 0.0307
REMARK 3 T13: 0.0254 T23: -0.0041
REMARK 3 L TENSOR
REMARK 3 L11: 1.3197 L22: 1.1266
REMARK 3 L33: 0.9512 L12: 0.1546
REMARK 3 L13: 0.1396 L23: -0.2455
REMARK 3 S TENSOR
REMARK 3 S11: -0.0924 S12: 0.1229 S13: -0.0731
REMARK 3 S21: -0.1813 S22: 0.0003 S23: -0.1483
REMARK 3 S31: 0.0562 S32: 0.0792 S33: 0.0921
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4Q1N COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-APR-14.
REMARK 100 THE DEPOSITION ID IS D_1000085491.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-NOV-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9999
REMARK 200 MONOCHROMATOR : DOUBLE-CRYSTAL SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 55186
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.090
REMARK 200 RESOLUTION RANGE LOW (A) : 62.990
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.09
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.16
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.52000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.63
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.12
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 4000, 0.6 M NACL, 0.05M SODIUM
REMARK 280 CITRATE, PH 4.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
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 70.42700
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 70.42700
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 70.42700
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 70.42700
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 70.42700
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 70.42700
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 70.42700
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 70.42700
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 70.42700
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 70.42700
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 70.42700
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 70.42700
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 70.42700
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 70.42700
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 70.42700
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 70.42700
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 70.42700
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 70.42700
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: 17800 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 72880 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.0 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 140.85400
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 -70.42700
REMARK 350 BIOMT3 2 0.000000 -1.000000 0.000000 70.42700
REMARK 350 BIOMT1 3 0.000000 1.000000 0.000000 70.42700
REMARK 350 BIOMT2 3 0.000000 0.000000 -1.000000 70.42700
REMARK 350 BIOMT3 3 -1.000000 0.000000 0.000000 140.85400
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 SER A 158A
REMARK 465 GLU A 158B
REMARK 465 ASN A 158C
REMARK 465 SER A 158D
REMARK 465 SER B 158A
REMARK 465 GLU B 158B
REMARK 465 ASN B 158C
REMARK 465 SER B 158D
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 GLN B 160C CA - C - N ANGL. DEV. = -13.9 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 67 -65.33 -136.41
REMARK 500 ALA A 285 33.21 -86.22
REMARK 500 ASN B 67 -64.89 -137.01
REMARK 500 ARG B 240 -88.69 -67.11
REMARK 500 LEU B 241 -59.52 -127.52
REMARK 500 ALA B 285 32.51 -86.79
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4PYV RELATED DB: PDB
DBREF 4Q1N A -5 326 UNP P00797 RENI_HUMAN 67 406
DBREF 4Q1N 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 4Q1N ASN B 67 ASN GLYCOSYLATION SITE
MODRES 4Q1N ASN A 67 ASN GLYCOSYLATION SITE
HET DMS A 401 4
HET NAG A 402 14
HET PO4 A 403 5
HET 2Y9 A 404 34
HET DMS B 401 4
HET DMS B 402 4
HET NAG B 403 14
HET 2Y9 B 404 34
HETNAM DMS DIMETHYL SULFOXIDE
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM PO4 PHOSPHATE ION
HETNAM 2Y9 (3S,4R,5R)-N-CYCLOPROPYL-N'-[(2R)-1-ETHOXY-4-
HETNAM 2 2Y9 METHYLPENTAN-2-YL]-4-HYDROXY-N-[5-(PROPAN-2-YL)
HETNAM 3 2Y9 PYRIDIN-2-YL]PIPERIDINE-3,5-DICARBOXAMIDE
FORMUL 3 DMS 3(C2 H6 O S)
FORMUL 4 NAG 2(C8 H15 N O6)
FORMUL 5 PO4 O4 P 3-
FORMUL 6 2Y9 2(C26 H42 N4 O4)
FORMUL 11 HOH *415(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 GLN A 143 1 9
HELIX 6 6 ASP A 171 GLN A 173 5 3
HELIX 7 7 SER A 224 GLY A 236 1 13
HELIX 8 8 ASN A 250 LEU A 255 5 6
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 THR B 48 HIS B 53 1 6
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 GLN B 143 1 9
HELIX 16 16 ASP B 171 GLN B 173 5 3
HELIX 17 17 SER B 224 GLY B 236 1 13
HELIX 18 18 ASN B 250 LEU B 255 5 6
HELIX 19 19 THR B 270 VAL B 275 1 6
HELIX 20 20 GLY B 302 LYS B 308 1 7
SHEET 1 A 9 LYS A 65 TYR A 75 0
SHEET 2 A 9 GLY A 78 VAL A 91 -1 O VAL A 80 N LEU A 73
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 LEU A 167 N SER A 2
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 ALA A 325 -1 O GLY A 321 N GLU A 312
SHEET 9 A 9 TYR A 175 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 VAL A 80 N LEU A 73
SHEET 3 B13 ILE A 94 GLU A 106 -1 O GLN A 99 N ASP A 87
SHEET 4 B13 VAL A 38 PRO A 41 1 N VAL A 38 O GLY A 102
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 GLY A 16 O VAL A 29
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 LEU A 167 N SER A 2
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 ALA A 325 -1 O GLY A 321 N GLU A 312
SHEET 13 B13 TYR A 175 ASN A 183 -1 N ILE A 182 O ILE A 320
SHEET 1 C 5 GLN A 191 MET A 194 0
SHEET 2 C 5 CYS A 210 VAL A 214 -1 O CYS A 210 N MET A 194
SHEET 3 C 5 TRP A 299 LEU A 301 1 O LEU A 301 N LEU A 213
SHEET 4 C 5 ILE A 221 GLY A 223 -1 N SER A 222 O ALA A 300
SHEET 5 C 5 ILE A 286 ALA A 288 1 O HIS A 287 N ILE A 221
SHEET 1 D 4 SER A 202 LEU A 205 0
SHEET 2 D 4 GLY A 196 VAL A 199 -1 N VAL A 197 O LEU A 205
SHEET 3 D 4 ILE A 258 LEU A 262 -1 O HIS A 261 N GLY A 196
SHEET 4 D 4 LYS A 265 LEU A 269 -1 O LEU A 269 N ILE A 258
SHEET 1 E 3 LYS A 238 LYS A 239 0
SHEET 2 E 3 TYR A 245 LYS A 248 -1 O VAL A 246 N LYS A 238
SHEET 3 E 3 LEU A 281D THR A 283 -1 O CYS A 282 N VAL A 247
SHEET 1 F 9 LYS B 65 TYR B 75 0
SHEET 2 F 9 GLY B 78 VAL B 91 -1 O VAL B 80 N LEU B 73
SHEET 3 F 9 GLN B 13 ILE B 20 -1 N GLY B 19 O THR B 90
SHEET 4 F 9 SER B 2 TYR B 9 -1 N TYR B 9 O GLN B 13
SHEET 5 F 9 GLY B 163 LEU B 167 -1 O LEU B 167 N SER B 2
SHEET 6 F 9 VAL B 150 TYR B 155 -1 N TYR B 154 O GLN B 164
SHEET 7 F 9 PHE B 309 ASP B 314 -1 O PHE B 313 N PHE B 151
SHEET 8 F 9 ARG B 319 ALA B 325 -1 O GLY B 321 N GLU B 312
SHEET 9 F 9 TYR B 175 ASN B 183 -1 N GLU B 176 O LEU B 324
SHEET 1 G13 LYS B 65 TYR B 75 0
SHEET 2 G13 GLY B 78 VAL B 91 -1 O VAL B 80 N LEU B 73
SHEET 3 G13 ILE B 94 GLU B 106 -1 O GLN B 99 N ASP B 87
SHEET 4 G13 VAL B 38 PRO B 41 1 N VAL B 38 O GLY B 102
SHEET 5 G13 GLY B 119 GLY B 122 -1 O VAL B 120 N TRP B 39
SHEET 6 G13 GLN B 25 ASP B 32 1 N VAL B 30 O VAL B 121
SHEET 7 G13 GLN B 13 ILE B 20 -1 N GLY B 16 O VAL B 29
SHEET 8 G13 SER B 2 TYR B 9 -1 N TYR B 9 O GLN B 13
SHEET 9 G13 GLY B 163 LEU B 167 -1 O LEU B 167 N SER B 2
SHEET 10 G13 VAL B 150 TYR B 155 -1 N TYR B 154 O GLN B 164
SHEET 11 G13 PHE B 309 ASP B 314 -1 O PHE B 313 N PHE B 151
SHEET 12 G13 ARG B 319 ALA B 325 -1 O GLY B 321 N GLU B 312
SHEET 13 G13 TYR B 175 ASN B 183 -1 N GLU B 176 O LEU B 324
SHEET 1 H 5 GLN B 191 MET B 194 0
SHEET 2 H 5 CYS B 210 VAL B 214 -1 O CYS B 210 N MET B 194
SHEET 3 H 5 TRP B 299 LEU B 301 1 O LEU B 301 N LEU B 213
SHEET 4 H 5 ILE B 221 GLY B 223 -1 N SER B 222 O ALA B 300
SHEET 5 H 5 ILE B 286 ALA B 288 1 O HIS B 287 N ILE B 221
SHEET 1 I 4 SER B 202 LEU B 205 0
SHEET 2 I 4 GLY B 196 VAL B 199 -1 N VAL B 197 O LEU B 205
SHEET 3 I 4 ILE B 258 LEU B 262 -1 O HIS B 261 N GLY B 196
SHEET 4 I 4 LYS B 265 LEU B 269 -1 O LEU B 269 N ILE B 258
SHEET 1 J 3 LYS B 238 LYS B 239 0
SHEET 2 J 3 TYR B 245 LYS B 248 -1 O VAL B 246 N LYS B 238
SHEET 3 J 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 2.01
SSBOND 2 CYS A 206 CYS A 210 1555 1555 2.04
SSBOND 3 CYS A 249 CYS A 282 1555 1555 2.05
SSBOND 4 CYS B 45 CYS B 50 1555 1555 2.02
SSBOND 5 CYS B 206 CYS B 210 1555 1555 2.56
SSBOND 6 CYS B 249 CYS B 282 1555 1555 2.06
LINK ND2 ASN A 67 C1 NAG A 402 1555 1555 1.43
LINK ND2 ASN B 67 C1 NAG B 403 1555 1555 1.43
CISPEP 1 THR A 22 PRO A 23 0 -4.04
CISPEP 2 LEU A 110 PRO A 111 0 11.49
CISPEP 3 PRO A 293 PRO A 294 0 4.02
CISPEP 4 GLY A 296 PRO A 297 0 -1.48
CISPEP 5 THR B 22 PRO B 23 0 -4.41
CISPEP 6 LEU B 110 PRO B 111 0 10.22
CISPEP 7 PRO B 293 PRO B 294 0 4.99
CISPEP 8 GLY B 296 PRO B 297 0 -2.42
CRYST1 140.854 140.854 140.854 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 0.007100 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007100 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007100 0.00000
(ATOM LINES ARE NOT SHOWN.)
END