HEADER HYDROLASE 14-NOV-05 2F1G
TITLE CATHEPSIN S IN COMPLEX WITH NON-COVALENT 2-(BENZOXAZOL-2-YLAMINO)-
TITLE 2 ACETAMIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CATHEPSIN S;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: CATHEPSIN S;
COMPND 5 EC: 3.4.22.27;
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: CTSS;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS CATHEPSIN S, NONCOVALENT, INHIBITION, 2-(BENZOOXAZOL-2-YLAMINO)
KEYWDS 2 ACETAMIDES, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR G.SPRAGGON,M.HORNSBY,S.A.LESLEY,D.C.TULLY,J.L.HARRIS,D.S.KARENEWSKY,
AUTHOR 2 R.KULATHILA,K.CLARK
REVDAT 3 13-JUL-11 2F1G 1 VERSN
REVDAT 2 24-FEB-09 2F1G 1 VERSN
REVDAT 1 04-APR-06 2F1G 0
JRNL AUTH D.C.TULLY,H.LIU,P.B.ALPER,A.K.CHATTERJEE,R.EPPLE,
JRNL AUTH 2 M.J.ROBERTS,J.A.WILLIAMS,K.T.NGUYEN,D.H.WOODMANSEE,
JRNL AUTH 3 C.TUMANUT,J.LI,G.SPRAGGON,J.CHANG,T.TUNTLAND,J.L.HARRIS,
JRNL AUTH 4 D.S.KARANEWSKY
JRNL TITL SYNTHESIS AND EVALUATION OF ARYLAMINOETHYL AMIDES AS
JRNL TITL 2 NONCOVALENT INHIBITORS OF CATHEPSIN S. PART 3: HETEROCYCLIC
JRNL TITL 3 P3.
JRNL REF BIOORG.MED.CHEM.LETT. V. 16 1975 2006
JRNL REFN ISSN 0960-894X
JRNL PMID 16446091
JRNL DOI 10.1016/J.BMCL.2005.12.095
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 84.51
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.4
REMARK 3 NUMBER OF REFLECTIONS : 39331
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) : 0.191
REMARK 3 R VALUE (WORKING SET) : 0.189
REMARK 3 FREE R VALUE : 0.230
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2119
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) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2630
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 85.21
REMARK 3 BIN R VALUE (WORKING SET) : 0.2530
REMARK 3 BIN FREE R VALUE SET COUNT : 135
REMARK 3 BIN FREE R VALUE : 0.3130
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3396
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 70
REMARK 3 SOLVENT ATOMS : 326
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.79
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.06000
REMARK 3 B22 (A**2) : -0.06000
REMARK 3 B33 (A**2) : 0.12000
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): 0.149
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.142
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.093
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.189
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.948
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.926
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3585 ; 0.013 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 3062 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4853 ; 1.476 ; 1.964
REMARK 3 BOND ANGLES OTHERS (DEGREES): 7171 ; 0.760 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 443 ; 5.770 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 163 ;35.258 ;24.233
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 570 ;12.125 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;13.144 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 488 ; 0.077 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4053 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 765 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 788 ; 0.199 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 3425 ; 0.180 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1851 ; 0.189 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 1998 ; 0.087 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 303 ; 0.148 ; 0.200
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): 9 ; 0.284 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 52 ; 0.183 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 20 ; 0.216 ; 0.200
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): 2772 ; 1.373 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 930 ; 0.285 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3470 ; 1.700 ; 3.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1752 ; 3.408 ; 5.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1379 ; 4.614 ; 8.000
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 : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
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 ELECTRON DENSITY FOR THE METHOXYPHENYL AMINO GROUP, MODELED IN THE
REMARK 3 P' SITE IS LARGELY ABSENT.
REMARK 4
REMARK 4 2F1G COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-MAR-06.
REMARK 100 THE RCSB ID CODE IS RCSB035333.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-MAR-03
REMARK 200 TEMPERATURE (KELVIN) : 190
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39331
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 84.510
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.4
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : 0.11000
REMARK 200 R SYM (I) : 0.11000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.3100
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 85.5
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : 0.73700
REMARK 200 R SYM FOR SHELL (I) : 0.73700
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.750
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
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 (%): 56.42
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.82
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG-8000, PH 6.5, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 278K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y,X,Z+1/4
REMARK 290 4555 Y,-X,Z+3/4
REMARK 290 5555 -X,Y,-Z
REMARK 290 6555 X,-Y,-Z+1/2
REMARK 290 7555 Y,X,-Z+3/4
REMARK 290 8555 -Y,-X,-Z+1/4
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 75.80650
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 37.90325
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 113.70975
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 75.80650
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 113.70975
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 37.90325
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 300 REMARK: THE BIOLOGICAL UNIT IS A MONOMER
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 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 B -2
REMARK 465 ARG B -1
REMARK 465 ILE B 0
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 ASN A -2 CG OD1
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 HIS A 205 ND1 CD2 CE1 NE2
REMARK 480 HIS B 205 ND1 CD2 CE1 NE2
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 O HOH A 1004 O HOH A 1147 2.06
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 SER A 21 42.50 -97.68
REMARK 500 THR A 58 -125.93 -115.28
REMARK 500 LYS A 202 54.00 -120.00
REMARK 500 CYS A 206 18.59 57.51
REMARK 500 THR B 58 -126.99 -112.48
REMARK 500 ARG B 141 44.47 -88.31
REMARK 500 ASN B 163 -1.59 -147.82
REMARK 500 LYS B 202 53.65 -115.88
REMARK 500 CYS B 206 15.47 58.38
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GNF B 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GNF A 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 1002
DBREF 2F1G A -2 217 UNP P25774 CATS_HUMAN 112 331
DBREF 2F1G B -2 217 UNP P25774 CATS_HUMAN 112 331
SEQRES 1 A 220 ASN ARG ILE LEU PRO ASP SER VAL ASP TRP ARG GLU LYS
SEQRES 2 A 220 GLY CYS VAL THR GLU VAL LYS TYR GLN GLY SER CYS GLY
SEQRES 3 A 220 ALA CYS TRP ALA PHE SER ALA VAL GLY ALA LEU GLU ALA
SEQRES 4 A 220 GLN LEU LYS LEU LYS THR GLY LYS LEU VAL SER LEU SER
SEQRES 5 A 220 ALA GLN ASN LEU VAL ASP CYS SER THR GLU LYS TYR GLY
SEQRES 6 A 220 ASN LYS GLY CYS ASN GLY GLY PHE MET THR THR ALA PHE
SEQRES 7 A 220 GLN TYR ILE ILE ASP ASN LYS GLY ILE ASP SER ASP ALA
SEQRES 8 A 220 SER TYR PRO TYR LYS ALA MET ASP GLN LYS CYS GLN TYR
SEQRES 9 A 220 ASP SER LYS TYR ARG ALA ALA THR CYS SER LYS TYR THR
SEQRES 10 A 220 GLU LEU PRO TYR GLY ARG GLU ASP VAL LEU LYS GLU ALA
SEQRES 11 A 220 VAL ALA ASN LYS GLY PRO VAL SER VAL GLY VAL ASP ALA
SEQRES 12 A 220 ARG HIS PRO SER PHE PHE LEU TYR ARG SER GLY VAL TYR
SEQRES 13 A 220 TYR GLU PRO SER CYS THR GLN ASN VAL ASN HIS GLY VAL
SEQRES 14 A 220 LEU VAL VAL GLY TYR GLY ASP LEU ASN GLY LYS GLU TYR
SEQRES 15 A 220 TRP LEU VAL LYS ASN SER TRP GLY HIS ASN PHE GLY GLU
SEQRES 16 A 220 GLU GLY TYR ILE ARG MET ALA ARG ASN LYS GLY ASN HIS
SEQRES 17 A 220 CYS GLY ILE ALA SER PHE PRO SER TYR PRO GLU ILE
SEQRES 1 B 220 ASN ARG ILE LEU PRO ASP SER VAL ASP TRP ARG GLU LYS
SEQRES 2 B 220 GLY CYS VAL THR GLU VAL LYS TYR GLN GLY SER CYS GLY
SEQRES 3 B 220 ALA CYS TRP ALA PHE SER ALA VAL GLY ALA LEU GLU ALA
SEQRES 4 B 220 GLN LEU LYS LEU LYS THR GLY LYS LEU VAL SER LEU SER
SEQRES 5 B 220 ALA GLN ASN LEU VAL ASP CYS SER THR GLU LYS TYR GLY
SEQRES 6 B 220 ASN LYS GLY CYS ASN GLY GLY PHE MET THR THR ALA PHE
SEQRES 7 B 220 GLN TYR ILE ILE ASP ASN LYS GLY ILE ASP SER ASP ALA
SEQRES 8 B 220 SER TYR PRO TYR LYS ALA MET ASP GLN LYS CYS GLN TYR
SEQRES 9 B 220 ASP SER LYS TYR ARG ALA ALA THR CYS SER LYS TYR THR
SEQRES 10 B 220 GLU LEU PRO TYR GLY ARG GLU ASP VAL LEU LYS GLU ALA
SEQRES 11 B 220 VAL ALA ASN LYS GLY PRO VAL SER VAL GLY VAL ASP ALA
SEQRES 12 B 220 ARG HIS PRO SER PHE PHE LEU TYR ARG SER GLY VAL TYR
SEQRES 13 B 220 TYR GLU PRO SER CYS THR GLN ASN VAL ASN HIS GLY VAL
SEQRES 14 B 220 LEU VAL VAL GLY TYR GLY ASP LEU ASN GLY LYS GLU TYR
SEQRES 15 B 220 TRP LEU VAL LYS ASN SER TRP GLY HIS ASN PHE GLY GLU
SEQRES 16 B 220 GLU GLY TYR ILE ARG MET ALA ARG ASN LYS GLY ASN HIS
SEQRES 17 B 220 CYS GLY ILE ALA SER PHE PRO SER TYR PRO GLU ILE
HET GNF B1001 32
HET GNF A1002 32
HET GOL B1002 6
HETNAM GNF N~2~-1,3-BENZOXAZOL-2-YL-3-CYCLOHEXYL-N-{2-[(4-
HETNAM 2 GNF METHOXYPHENYL)AMINO]ETHYL}-L-ALANINAMIDE
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 GNF 2(C25 H32 N4 O3)
FORMUL 5 GOL C3 H8 O3
FORMUL 6 HOH *326(H2 O)
HELIX 1 1 ARG A 8 GLY A 11 5 4
HELIX 2 2 ALA A 24 GLY A 43 1 20
HELIX 3 3 SER A 49 SER A 57 1 9
HELIX 4 4 THR A 58 GLY A 62 5 5
HELIX 5 5 LYS A 64 GLY A 68 5 5
HELIX 6 6 PHE A 70 LYS A 82 1 13
HELIX 7 7 ASP A 102 LYS A 104 5 3
HELIX 8 8 ARG A 120 LYS A 131 1 12
HELIX 9 9 HIS A 142 LEU A 147 1 6
HELIX 10 10 ASN A 204 ILE A 208 5 5
HELIX 11 11 ALA B 24 GLY B 43 1 20
HELIX 12 12 SER B 49 SER B 57 1 9
HELIX 13 13 THR B 58 GLY B 62 5 5
HELIX 14 14 LYS B 64 GLY B 68 5 5
HELIX 15 15 PHE B 70 LYS B 82 1 13
HELIX 16 16 ASP B 102 LYS B 104 5 3
HELIX 17 17 ARG B 120 LYS B 131 1 12
HELIX 18 18 HIS B 142 TYR B 148 1 7
HELIX 19 19 ASN B 204 ILE B 208 5 5
SHEET 1 A 3 VAL A 5 ASP A 6 0
SHEET 2 A 3 HIS A 164 LEU A 174 -1 O TYR A 171 N VAL A 5
SHEET 3 A 3 VAL A 134 VAL A 138 -1 N VAL A 136 O VAL A 166
SHEET 1 B 4 VAL A 5 ASP A 6 0
SHEET 2 B 4 HIS A 164 LEU A 174 -1 O TYR A 171 N VAL A 5
SHEET 3 B 4 LYS A 177 LYS A 183 -1 O LYS A 183 N LEU A 167
SHEET 4 B 4 TYR A 195 ALA A 199 -1 O MET A 198 N TRP A 180
SHEET 1 C 2 ILE A 84 ASP A 85 0
SHEET 2 C 2 ARG A 106 ALA A 108 -1 O ALA A 107 N ILE A 84
SHEET 1 D 2 LYS A 112 GLU A 115 0
SHEET 2 D 2 SER A 213 GLU A 216 -1 O GLU A 216 N LYS A 112
SHEET 1 E 3 VAL B 5 ASP B 6 0
SHEET 2 E 3 HIS B 164 LEU B 174 -1 O TYR B 171 N VAL B 5
SHEET 3 E 3 VAL B 134 VAL B 138 -1 N VAL B 134 O VAL B 168
SHEET 1 F 5 VAL B 5 ASP B 6 0
SHEET 2 F 5 HIS B 164 LEU B 174 -1 O TYR B 171 N VAL B 5
SHEET 3 F 5 LYS B 177 LYS B 183 -1 O LYS B 177 N LEU B 174
SHEET 4 F 5 TYR B 195 ALA B 199 -1 O MET B 198 N TRP B 180
SHEET 5 F 5 VAL B 152 TYR B 153 1 N TYR B 153 O ARG B 197
SHEET 1 G 2 ILE B 84 ASP B 85 0
SHEET 2 G 2 ARG B 106 ALA B 108 -1 O ALA B 107 N ILE B 84
SHEET 1 H 2 LYS B 112 GLU B 115 0
SHEET 2 H 2 SER B 213 GLU B 216 -1 O GLU B 216 N LYS B 112
SSBOND 1 CYS A 22 CYS A 66 1555 1555 2.10
SSBOND 2 CYS A 56 CYS A 99 1555 1555 2.12
SSBOND 3 CYS A 158 CYS A 206 1555 1555 2.04
SSBOND 4 CYS B 22 CYS B 66 1555 1555 2.08
SSBOND 5 CYS B 56 CYS B 99 1555 1555 2.12
SSBOND 6 CYS B 158 CYS B 206 1555 1555 2.03
SITE 1 AC1 16 GLY B 23 CYS B 25 TRP B 26 GLY B 62
SITE 2 AC1 16 LYS B 64 ASN B 67 GLY B 68 GLY B 69
SITE 3 AC1 16 PHE B 70 MET B 71 GLY B 137 ALA B 140
SITE 4 AC1 16 PHE B 146 VAL B 162 ASN B 163 TRP B 186
SITE 1 AC2 16 GLN A 19 GLY A 23 CYS A 25 TRP A 26
SITE 2 AC2 16 GLY A 62 LYS A 64 GLY A 68 GLY A 69
SITE 3 AC2 16 PHE A 70 MET A 71 GLY A 137 ASN A 163
SITE 4 AC2 16 HIS A 164 GLY A 165 TRP A 186 GLU B 9
SITE 1 AC3 4 TYR A 105 SER B 103 ARG B 106 HOH B1019
CRYST1 85.250 85.250 151.613 90.00 90.00 90.00 P 41 2 2 16
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 0.011730 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011730 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006596 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
