HEADER LIPID BINDING PROTEIN 08-JAN-09 3FR2
TITLE N-BENZYL-INDOLO CARBOXYLIC ACIDS: DESIGN AND SYNTHESIS OF POTENT AND
TITLE 2 SELECTIVE ADIPOCYTE FATTY-ACID BINDING PROTEIN (A-FABP) INHIBITORS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FATTY ACID-BINDING PROTEIN, ADIPOCYTE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: A-FABP, AFABP, FATTY ACID-BINDING PROTEIN 4, ADIPOCYTE
COMPND 5 LIPID-BINDING PROTEIN, ALBP;
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: FABP4;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS SELECTIVE ADIPOCYTE FATTY-ACID BINDING PROTEIN (A-FABP) INHIBITORS,
KEYWDS 2 CYTOPLASM, LIPID-BINDING, NUCLEUS, PHOSPHOPROTEIN, POLYMORPHISM,
KEYWDS 3 TRANSPORT, LIPID BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR T.BARF,K.HAMMER,F.LEHMANN,S.HAILE,E.AXEN,C.MEDINA,L.RONDAHL,
AUTHOR 2 J.UPPENBERG,S.SVENSSON,T.LUNDB CK
REVDAT 4 21-FEB-24 3FR2 1 REMARK
REVDAT 3 24-JAN-18 3FR2 1 AUTHOR
REVDAT 2 31-MAR-09 3FR2 1 JRNL
REVDAT 1 10-MAR-09 3FR2 0
JRNL AUTH T.BARF,F.LEHMANN,K.HAMMER,S.HAILE,E.AXEN,C.MEDINA,
JRNL AUTH 2 J.UPPENBERG,S.SVENSSON,L.RONDAHL,T.LUNDBACK
JRNL TITL N-BENZYL-INDOLO CARBOXYLIC ACIDS: DESIGN AND SYNTHESIS OF
JRNL TITL 2 POTENT AND SELECTIVE ADIPOCYTE FATTY-ACID BINDING PROTEIN
JRNL TITL 3 (A-FABP) INHIBITORS.
JRNL REF BIOORG.MED.CHEM.LETT. V. 19 1745 2009
JRNL REFN ISSN 0960-894X
JRNL PMID 19217286
JRNL DOI 10.1016/J.BMCL.2009.01.084
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.0
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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.1
REMARK 3 NUMBER OF REFLECTIONS : 5770
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) : 0.224
REMARK 3 R VALUE (WORKING SET) : 0.221
REMARK 3 FREE R VALUE : 0.297
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.600
REMARK 3 FREE R VALUE TEST SET COUNT : 279
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) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.26
REMARK 3 REFLECTION IN BIN (WORKING SET) : 260
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3390
REMARK 3 BIN FREE R VALUE SET COUNT : 7
REMARK 3 BIN FREE R VALUE : 0.5570
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1021
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 23
REMARK 3 SOLVENT ATOMS : 154
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.68
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.07000
REMARK 3 B22 (A**2) : -0.74000
REMARK 3 B33 (A**2) : 1.81000
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): 0.563
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.312
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.212
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.350
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.911
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.867
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1060 ; 0.020 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1427 ; 1.861 ; 1.973
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 130 ; 4.662 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 201 ;18.552 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 166 ; 0.112 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 766 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 504 ; 0.244 ; 0.300
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): 182 ; 0.282 ; 0.500
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): 32 ; 0.409 ; 0.300
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 15 ; 0.263 ; 0.500
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): 645 ; 0.994 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1049 ; 1.724 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 415 ; 2.773 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 378 ; 4.323 ; 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 : BABINET MODEL WITH 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: NULL
REMARK 4
REMARK 4 3FR2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-JAN-09.
REMARK 100 THE DEPOSITION ID IS D_1000050936.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : OSMIC MIRRORS
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 8439
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 89.4
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.07400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.7000
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: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.52
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 35.98000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 26.68750
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 35.98000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 26.68750
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 N CYS A 1 O HOH A 188 1.49
REMARK 500 OE1 GLU A 129 O HOH A 191 1.88
REMARK 500 NH2 ARG A 106 O HOH A 253 1.89
REMARK 500 O LEU A 86 O HOH A 214 1.90
REMARK 500 O ALA A 131 O HOH A 180 1.91
REMARK 500 OE1 GLU A 54 O HOH A 223 1.93
REMARK 500 O HOH A 152 O HOH A 163 1.95
REMARK 500 O HOH A 207 O HOH A 208 2.03
REMARK 500 O HOH A 202 O HOH A 212 2.03
REMARK 500 NZ LYS A 21 O HOH A 167 2.15
REMARK 500 O HOH A 264 O HOH A 273 2.15
REMARK 500 OE2 GLU A 72 O HOH A 269 2.16
REMARK 500 OE1 GLU A 69 O HOH A 275 2.17
REMARK 500 OD1 ASP A 18 O HOH A 153 2.17
REMARK 500 O HOH A 149 O HOH A 157 2.18
REMARK 500 O HOH A 250 O HOH A 260 2.19
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 17 CB - CG - OD2 ANGL. DEV. = 7.3 DEGREES
REMARK 500 ASP A 47 CB - CG - OD2 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ASP A 77 CB - CG - OD2 ANGL. DEV. = 6.6 DEGREES
REMARK 500 ASP A 98 CB - CG - OD2 ANGL. DEV. = 6.3 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 ASP A 2 -19.55 -140.58
REMARK 500 ALA A 3 -8.90 -59.34
REMARK 500 LYS A 37 76.35 -119.72
REMARK 500 ASP A 110 -112.88 51.72
REMARK 500 LYS A 120 -121.00 57.03
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 8CA A 501
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3FR4 RELATED DB: PDB
REMARK 900 RELATED ID: 3FR5 RELATED DB: PDB
DBREF 3FR2 A 1 131 UNP P15090 FABP4_HUMAN 2 132
SEQRES 1 A 131 CYS ASP ALA PHE VAL GLY THR TRP LYS LEU VAL SER SER
SEQRES 2 A 131 GLU ASN PHE ASP ASP TYR MET LYS GLU VAL GLY VAL GLY
SEQRES 3 A 131 PHE ALA THR ARG LYS VAL ALA GLY MET ALA LYS PRO ASN
SEQRES 4 A 131 MET ILE ILE SER VAL ASN GLY ASP VAL ILE THR ILE LYS
SEQRES 5 A 131 SER GLU SER THR PHE LYS ASN THR GLU ILE SER PHE ILE
SEQRES 6 A 131 LEU GLY GLN GLU PHE ASP GLU VAL THR ALA ASP ASP ARG
SEQRES 7 A 131 LYS VAL LYS SER THR ILE THR LEU ASP GLY GLY VAL LEU
SEQRES 8 A 131 VAL HIS VAL GLN LYS TRP ASP GLY LYS SER THR THR ILE
SEQRES 9 A 131 LYS ARG LYS ARG GLU ASP ASP LYS LEU VAL VAL GLU CYS
SEQRES 10 A 131 VAL MET LYS GLY VAL THR SER THR ARG VAL TYR GLU ARG
SEQRES 11 A 131 ALA
HET 8CA A 501 23
HETNAM 8CA 9-BENZYL-2,3,4,9-TETRAHYDRO-1H-CARBAZOLE-8-CARBOXYLIC
HETNAM 2 8CA ACID
FORMUL 2 8CA C20 H19 N O2
FORMUL 3 HOH *154(H2 O)
HELIX 1 1 ASN A 15 GLY A 24 1 10
HELIX 2 2 GLY A 26 ALA A 36 1 11
SHEET 1 A10 THR A 60 ILE A 65 0
SHEET 2 A10 VAL A 48 GLU A 54 -1 N SER A 53 O THR A 60
SHEET 3 A10 ASN A 39 ASN A 45 -1 N ILE A 41 O LYS A 52
SHEET 4 A10 GLY A 6 GLU A 14 -1 N TRP A 8 O MET A 40
SHEET 5 A10 VAL A 122 ARG A 130 -1 O VAL A 127 N VAL A 11
SHEET 6 A10 LYS A 112 MET A 119 -1 N CYS A 117 O SER A 124
SHEET 7 A10 LYS A 100 GLU A 109 -1 N LYS A 107 O VAL A 114
SHEET 8 A10 VAL A 90 TRP A 97 -1 N HIS A 93 O ILE A 104
SHEET 9 A10 LYS A 79 ASP A 87 -1 N LYS A 81 O LYS A 96
SHEET 10 A10 PHE A 70 VAL A 73 -1 N PHE A 70 O SER A 82
SITE 1 AC1 12 PHE A 16 PRO A 38 SER A 55 LYS A 58
SITE 2 AC1 12 ASP A 76 ARG A 78 CYS A 117 ARG A 126
SITE 3 AC1 12 TYR A 128 HOH A 244 HOH A 263 HOH A 264
CRYST1 71.960 53.375 32.000 90.00 90.00 90.00 P 21 21 2 4
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 0.013897 0.000000 0.000000 0.00000
SCALE2 0.000000 0.018735 0.000000 0.00000
SCALE3 0.000000 0.000000 0.031250 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
