HEADER HYDROLASE/BLOOD CLOTTING 05-DEC-05 2F9B
TITLE DISCOVERY OF NOVEL HETEROCYCLIC FACTOR VIIA INHIBITORS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: COAGULATION FACTOR VII;
COMPND 3 CHAIN: L;
COMPND 4 FRAGMENT: LIGHT CHAIN, RESIDUES 61-212;
COMPND 5 EC: 3.4.21.21;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: COAGULATION FACTOR VII;
COMPND 9 CHAIN: H;
COMPND 10 FRAGMENT: HEAVY CHAIN, RESIDUES 213-466;
COMPND 11 EC: 3.4.21.21;
COMPND 12 ENGINEERED: YES;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: TISSUE FACTOR;
COMPND 15 CHAIN: T;
COMPND 16 FRAGMENT: RESIDUES 34-251;
COMPND 17 SYNONYM: TF, COAGULATION FACTOR III, THROMBOPLASTIN, CD142 ANTIGEN;
COMPND 18 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: F7;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: EMBRYONIC KIDNEY CELL LINE 293;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606;
SOURCE 14 GENE: F7;
SOURCE 15 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 16 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 18 EXPRESSION_SYSTEM_CELL_LINE: EMBRYONIC KIDNEY CELL LINE 293;
SOURCE 19 MOL_ID: 3;
SOURCE 20 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 21 ORGANISM_COMMON: HUMAN;
SOURCE 22 ORGANISM_TAXID: 9606;
SOURCE 23 GENE: F3;
SOURCE 24 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 25 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 26 EXPRESSION_SYSTEM_STRAIN: BL21-DES3;
SOURCE 27 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 28 EXPRESSION_SYSTEM_PLASMID: PET-21A(+)
KEYWDS SERINE PROTEASE, SHORT HYDROGEN BOND, ACTIVE SITE-DIRECTED INHIBITOR,
KEYWDS 2 HYDROLASE-BLOOD CLOTTING COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR R.RAI,A.KOLESNIKOV,P.A.SPRENGELER,S.TORKELSON,T.TON,B.A.KATZ,C.YU,
AUTHOR 2 J.HENDRIX,W.D.SHRADER,R.STEPHENS,R.CABUSLAY,E.SANFORD,W.B.YOUNG
REVDAT 5 30-AUG-23 2F9B 1 REMARK
REVDAT 4 18-OCT-17 2F9B 1 REMARK
REVDAT 3 24-FEB-09 2F9B 1 VERSN
REVDAT 2 21-MAR-06 2F9B 1 JRNL
REVDAT 1 28-FEB-06 2F9B 0
JRNL AUTH R.RAI,A.KOLESNIKOV,P.A.SPRENGELER,S.TORKELSON,T.TON,
JRNL AUTH 2 B.A.KATZ,C.YU,J.HENDRIX,W.D.SHRADER,R.STEPHENS,R.CABUSLAY,
JRNL AUTH 3 E.SANFORD,W.B.YOUNG
JRNL TITL DISCOVERY OF NOVEL HETEROCYCLIC FACTOR VIIA INHIBITORS.
JRNL REF BIOORG.MED.CHEM.LETT. V. 16 2270 2006
JRNL REFN ISSN 0960-894X
JRNL PMID 16460932
JRNL DOI 10.1016/J.BMCL.2006.01.017
REMARK 2
REMARK 2 RESOLUTION. 2.54 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.54
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 26404
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.226
REMARK 3 FREE R VALUE : 0.286
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 2673
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 : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
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 : 3874
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 30
REMARK 3 SOLVENT ATOMS : 153
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.018
REMARK 3 BOND ANGLES (DEGREES) : 3.980
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.90
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.470
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2F9B COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-DEC-05.
REMARK 100 THE DEPOSITION ID IS D_1000035612.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-JAN-03
REMARK 200 TEMPERATURE (KELVIN) : 113
REMARK 200 PH : 7.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28367
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
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) : 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) : 2.54
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.65
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
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: XTALVIEW
REMARK 200 STARTING MODEL: PDB ENTRY 1DAN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.41
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.03
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M CITRATE, 16-18% PEG5000 MME, PH
REMARK 280 7.2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 290K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 34.47000
REMARK 290 SMTRY3 2 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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS CONTAINED IN THE ASYMMETIC UNIT
REMARK 300 (FACTOR VIIA LIGHT CHAIN, FACTOR VIIA HEAVY CHAIN, SOLUBLE TISSUE
REMARK 300 FACTOR, AND THE INHIBITOR)
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5490 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22100 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, H, T
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 ALA L 1
REMARK 465 ASN L 2
REMARK 465 ALA L 3
REMARK 465 PHE L 4
REMARK 465 LEU L 5
REMARK 465 GLU L 6
REMARK 465 GLU L 7
REMARK 465 LEU L 8
REMARK 465 ARG L 9
REMARK 465 PRO L 10
REMARK 465 GLY L 11
REMARK 465 SER L 12
REMARK 465 LEU L 13
REMARK 465 GLU L 14
REMARK 465 ARG L 15
REMARK 465 GLU L 16
REMARK 465 CYS L 17
REMARK 465 LYS L 18
REMARK 465 GLU L 19
REMARK 465 GLU L 20
REMARK 465 GLN L 21
REMARK 465 CYS L 22
REMARK 465 SER L 23
REMARK 465 PHE L 24
REMARK 465 GLU L 25
REMARK 465 GLU L 26
REMARK 465 ALA L 27
REMARK 465 ARG L 28
REMARK 465 GLU L 29
REMARK 465 ILE L 30
REMARK 465 PHE L 31
REMARK 465 LYS L 32
REMARK 465 ASP L 33
REMARK 465 ALA L 34
REMARK 465 GLU L 35
REMARK 465 ARG L 36
REMARK 465 THR L 37
REMARK 465 LYS L 38
REMARK 465 LEU L 39
REMARK 465 PHE L 40
REMARK 465 TRP L 41
REMARK 465 ILE L 42
REMARK 465 SER L 43
REMARK 465 TYR L 44
REMARK 465 SER L 45
REMARK 465 ASP L 46
REMARK 465 GLY L 47
REMARK 465 ASP L 48
REMARK 465 LYS L 143
REMARK 465 ARG L 144
REMARK 465 ASN L 145
REMARK 465 ALA L 146
REMARK 465 SER L 147
REMARK 465 LYS L 148
REMARK 465 PRO L 149
REMARK 465 GLN L 150
REMARK 465 GLY L 151
REMARK 465 ARG L 152
REMARK 465 GLY T 2
REMARK 465 THR T 3
REMARK 465 THR T 4
REMARK 465 ASN T 5
REMARK 465 GLN T 110
REMARK 465 PRO T 111
REMARK 465 THR T 112
REMARK 465 ILE T 113
REMARK 465 GLN T 114
REMARK 465 SER T 115
REMARK 465 PHE T 116
REMARK 465 GLU T 117
REMARK 465 GLN T 118
REMARK 465 VAL T 119
REMARK 465 GLY T 120
REMARK 465 THR T 121
REMARK 465 LYS T 122
REMARK 465 VAL T 123
REMARK 465 ASN T 124
REMARK 465 VAL T 125
REMARK 465 THR T 126
REMARK 465 VAL T 127
REMARK 465 GLU T 128
REMARK 465 TYR T 156
REMARK 465 TYR T 157
REMARK 465 TRP T 158
REMARK 465 LYS T 159
REMARK 465 SER T 160
REMARK 465 SER T 161
REMARK 465 SER T 162
REMARK 465 SER T 163
REMARK 465 GLY T 164
REMARK 465 LYS T 165
REMARK 465 LYS T 166
REMARK 465 THR T 167
REMARK 465 ALA T 168
REMARK 465 LYS T 169
REMARK 465 THR T 170
REMARK 465 ASN T 171
REMARK 465 THR T 172
REMARK 465 ASN T 173
REMARK 465 GLU T 174
REMARK 465 PHE T 175
REMARK 465 LEU T 176
REMARK 465 ILE T 177
REMARK 465 ASP T 178
REMARK 465 VAL T 179
REMARK 465 ASP T 180
REMARK 465 LYS T 181
REMARK 465 GLY T 182
REMARK 465 GLU T 183
REMARK 465 ASN T 184
REMARK 465 TYR T 185
REMARK 465 CYS T 186
REMARK 465 PHE T 187
REMARK 465 PRO T 206
REMARK 465 VAL T 207
REMARK 465 GLU T 208
REMARK 465 CYS T 209
REMARK 465 MET T 210
REMARK 465 GLY T 211
REMARK 465 GLN T 212
REMARK 465 GLU T 213
REMARK 465 LYS T 214
REMARK 465 GLY T 215
REMARK 465 GLU T 216
REMARK 465 PHE T 217
REMARK 465 ARG T 218
REMARK 465 GLU T 219
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 OG SER H 195 O HOH H 332 1.98
REMARK 500 O6' N1H H 258 O HOH H 332 2.02
REMARK 500
REMARK 500 REMARK: NULL
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 CYS H 58 CA CYS H 58 CB -0.109
REMARK 500 HIS H 71 NE2 HIS H 71 CD2 -0.083
REMARK 500 TRP H 215 CG TRP H 215 CD2 -0.105
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 L 113 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 TYR L 118 CB - CG - CD2 ANGL. DEV. = -4.7 DEGREES
REMARK 500 TYR L 118 CB - CG - CD1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 TRP H 29 CG - CD1 - NE1 ANGL. DEV. = -8.2 DEGREES
REMARK 500 TRP H 29 CD1 - NE1 - CE2 ANGL. DEV. = 9.4 DEGREES
REMARK 500 TRP H 29 NE1 - CE2 - CZ2 ANGL. DEV. = 8.6 DEGREES
REMARK 500 TRP H 29 NE1 - CE2 - CD2 ANGL. DEV. = -6.6 DEGREES
REMARK 500 TRP H 51 CG - CD1 - NE1 ANGL. DEV. = -6.6 DEGREES
REMARK 500 TRP H 51 CD1 - NE1 - CE2 ANGL. DEV. = 8.1 DEGREES
REMARK 500 TRP H 61 CG - CD1 - NE1 ANGL. DEV. = -7.8 DEGREES
REMARK 500 TRP H 61 CD1 - NE1 - CE2 ANGL. DEV. = 9.1 DEGREES
REMARK 500 TRP H 61 NE1 - CE2 - CZ2 ANGL. DEV. = 8.0 DEGREES
REMARK 500 TRP H 61 NE1 - CE2 - CD2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 THR H 115 OG1 - CB - CG2 ANGL. DEV. = -15.7 DEGREES
REMARK 500 ARG H 129B NE - CZ - NH2 ANGL. DEV. = -4.7 DEGREES
REMARK 500 VAL H 129G N - CA - C ANGL. DEV. = -22.7 DEGREES
REMARK 500 TRP H 141 CG - CD1 - NE1 ANGL. DEV. = -7.1 DEGREES
REMARK 500 TRP H 141 CD1 - NE1 - CE2 ANGL. DEV. = 8.4 DEGREES
REMARK 500 TRP H 141 NE1 - CE2 - CZ2 ANGL. DEV. = 9.1 DEGREES
REMARK 500 TRP H 141 NE1 - CE2 - CD2 ANGL. DEV. = -6.3 DEGREES
REMARK 500 ARG H 147 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 GLY H 170F N - CA - C ANGL. DEV. = -15.2 DEGREES
REMARK 500 HIS H 199 N - CA - C ANGL. DEV. = -19.9 DEGREES
REMARK 500 TRP H 207 CG - CD1 - NE1 ANGL. DEV. = -7.0 DEGREES
REMARK 500 TRP H 207 CD1 - NE1 - CE2 ANGL. DEV. = 7.2 DEGREES
REMARK 500 TRP H 207 NE1 - CE2 - CZ2 ANGL. DEV. = 8.5 DEGREES
REMARK 500 TRP H 215 CG - CD1 - NE1 ANGL. DEV. = -6.2 DEGREES
REMARK 500 TRP H 215 CD1 - NE1 - CE2 ANGL. DEV. = 7.2 DEGREES
REMARK 500 TRP H 215 NE1 - CE2 - CZ2 ANGL. DEV. = 7.5 DEGREES
REMARK 500 TRP H 215 CG - CD2 - CE3 ANGL. DEV. = -5.8 DEGREES
REMARK 500 TRP H 237 CG - CD1 - NE1 ANGL. DEV. = -7.5 DEGREES
REMARK 500 TRP H 237 CD1 - NE1 - CE2 ANGL. DEV. = 8.9 DEGREES
REMARK 500 TRP H 237 NE1 - CE2 - CZ2 ANGL. DEV. = 9.9 DEGREES
REMARK 500 TRP H 237 NE1 - CE2 - CD2 ANGL. DEV. = -6.9 DEGREES
REMARK 500 ARG H 243 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 ARG H 253 NE - CZ - NH2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 TRP T 14 CG - CD1 - NE1 ANGL. DEV. = -7.1 DEGREES
REMARK 500 TRP T 14 CD1 - NE1 - CE2 ANGL. DEV. = 8.2 DEGREES
REMARK 500 TRP T 14 NE1 - CE2 - CZ2 ANGL. DEV. = 7.8 DEGREES
REMARK 500 TRP T 25 CG - CD1 - NE1 ANGL. DEV. = -7.3 DEGREES
REMARK 500 TRP T 25 CD1 - NE1 - CE2 ANGL. DEV. = 8.4 DEGREES
REMARK 500 TRP T 25 NE1 - CE2 - CZ2 ANGL. DEV. = 8.6 DEGREES
REMARK 500 TRP T 45 CG - CD1 - NE1 ANGL. DEV. = -8.0 DEGREES
REMARK 500 TRP T 45 CD1 - NE1 - CE2 ANGL. DEV. = 8.8 DEGREES
REMARK 500 TRP T 45 NE1 - CE2 - CZ2 ANGL. DEV. = 9.1 DEGREES
REMARK 500 TRP T 45 NE1 - CE2 - CD2 ANGL. DEV. = -6.3 DEGREES
REMARK 500 ARG T 74 NE - CZ - NH2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 TYR T 78 CB - CG - CD2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 TYR T 78 CB - CG - CD1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ARG T 135 NE - CZ - NH1 ANGL. DEV. = -3.9 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 SER L 52 44.62 -93.95
REMARK 500 SER L 53 71.14 1.35
REMARK 500 GLN L 56 -158.67 -103.08
REMARK 500 ASN L 57 44.28 23.35
REMARK 500 GLN L 64 -154.40 -136.95
REMARK 500 GLN L 66 -40.64 94.18
REMARK 500 PRO L 74 -37.16 -32.20
REMARK 500 CYS L 81 38.46 35.07
REMARK 500 GLN L 100 -82.49 -120.36
REMARK 500 LYS L 109 155.14 -49.19
REMARK 500 VAL L 125 -45.60 -130.07
REMARK 500 PRO H 23 100.82 -44.92
REMARK 500 LYS H 24 121.07 -22.76
REMARK 500 ASN H 37 15.19 48.60
REMARK 500 LEU H 41 -88.78 -115.04
REMARK 500 THR H 49 -31.30 -35.80
REMARK 500 ALA H 56 -40.33 -28.85
REMARK 500 TRP H 61 -12.46 -43.53
REMARK 500 ASN H 63 30.68 -87.98
REMARK 500 GLU H 70 150.15 -49.38
REMARK 500 HIS H 71 -68.61 -154.01
REMARK 500 ASP H 79 -43.05 -160.21
REMARK 500 PRO H 96 102.03 -45.71
REMARK 500 HIS H 101 42.50 70.62
REMARK 500 PRO H 111 170.98 -57.96
REMARK 500 ASP H 146 -46.08 -23.44
REMARK 500 SER H 195 136.54 -35.34
REMARK 500 GLN H 217 114.62 92.04
REMARK 500 CYS H 220 151.71 156.62
REMARK 500 ALA H 221A 67.33 9.96
REMARK 500 PRO H 255 136.70 -31.57
REMARK 500 ASN T 18 32.98 37.28
REMARK 500 PHE T 19 -10.65 82.27
REMARK 500 CYS T 49 58.65 32.24
REMARK 500 TYR T 51 46.29 37.45
REMARK 500 VAL T 67 -8.03 -55.82
REMARK 500 VAL T 83 36.85 -87.64
REMARK 500 SER T 85 129.25 -8.11
REMARK 500 SER T 88 -44.75 -14.77
REMARK 500 ASN T 137 66.91 20.07
REMARK 500 ASN T 138 -29.96 74.98
REMARK 500 SER T 195 48.24 -83.15
REMARK 500 ASN T 199 60.51 26.06
REMARK 500 SER T 202 -141.81 -100.04
REMARK 500 THR T 203 -164.88 -114.80
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 LYS T 28 PRO T 29 -149.18
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 N1H H 258
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1O5D RELATED DB: PDB
REMARK 900 DISSECTING AND DESIGNING INHIBITOR SELECTIVITY DETERMINANTS AT THE
REMARK 900 S1 SITE USING AN ARTIFICIAL ALA190 PROTEASE (ALA190 UPA)
DBREF 2F9B L 1 152 UNP P08709 FA7_HUMAN 61 212
DBREF 2F9B H 16 257 UNP P08709 FA7_HUMAN 213 466
DBREF 2F9B T 2 219 UNP P13726 TF_HUMAN 34 251
SEQRES 1 L 152 ALA ASN ALA PHE LEU GLU GLU LEU ARG PRO GLY SER LEU
SEQRES 2 L 152 GLU ARG GLU CYS LYS GLU GLU GLN CYS SER PHE GLU GLU
SEQRES 3 L 152 ALA ARG GLU ILE PHE LYS ASP ALA GLU ARG THR LYS LEU
SEQRES 4 L 152 PHE TRP ILE SER TYR SER ASP GLY ASP GLN CYS ALA SER
SEQRES 5 L 152 SER PRO CYS GLN ASN GLY GLY SER CYS LYS ASP GLN LEU
SEQRES 6 L 152 GLN SER TYR ILE CYS PHE CYS LEU PRO ALA PHE GLU GLY
SEQRES 7 L 152 ARG ASN CYS GLU THR HIS LYS ASP ASP GLN LEU ILE CYS
SEQRES 8 L 152 VAL ASN GLU ASN GLY GLY CYS GLU GLN TYR CYS SER ASP
SEQRES 9 L 152 HIS THR GLY THR LYS ARG SER CYS ARG CYS HIS GLU GLY
SEQRES 10 L 152 TYR SER LEU LEU ALA ASP GLY VAL SER CYS THR PRO THR
SEQRES 11 L 152 VAL GLU TYR PRO CYS GLY LYS ILE PRO ILE LEU GLU LYS
SEQRES 12 L 152 ARG ASN ALA SER LYS PRO GLN GLY ARG
SEQRES 1 H 254 ILE VAL GLY GLY LYS VAL CYS PRO LYS GLY GLU CYS PRO
SEQRES 2 H 254 TRP GLN VAL LEU LEU LEU VAL ASN GLY ALA GLN LEU CYS
SEQRES 3 H 254 GLY GLY THR LEU ILE ASN THR ILE TRP VAL VAL SER ALA
SEQRES 4 H 254 ALA HIS CYS PHE ASP LYS ILE LYS ASN TRP ARG ASN LEU
SEQRES 5 H 254 ILE ALA VAL LEU GLY GLU HIS ASP LEU SER GLU HIS ASP
SEQRES 6 H 254 GLY ASP GLU GLN SER ARG ARG VAL ALA GLN VAL ILE ILE
SEQRES 7 H 254 PRO SER THR TYR VAL PRO GLY THR THR ASN HIS ASP ILE
SEQRES 8 H 254 ALA LEU LEU ARG LEU HIS GLN PRO VAL VAL LEU THR ASP
SEQRES 9 H 254 HIS VAL VAL PRO LEU CYS LEU PRO GLU ARG THR PHE SER
SEQRES 10 H 254 GLU ARG THR LEU ALA PHE VAL ARG PHE SER LEU VAL SER
SEQRES 11 H 254 GLY TRP GLY GLN LEU LEU ASP ARG GLY ALA THR ALA LEU
SEQRES 12 H 254 GLU LEU MET VAL LEU ASN VAL PRO ARG LEU MET THR GLN
SEQRES 13 H 254 ASP CYS LEU GLN GLN SER ARG LYS VAL GLY ASP SER PRO
SEQRES 14 H 254 ASN ILE THR GLU TYR MET PHE CYS ALA GLY TYR SER ASP
SEQRES 15 H 254 GLY SER LYS ASP SER CYS LYS GLY ASP SER GLY GLY PRO
SEQRES 16 H 254 HIS ALA THR HIS TYR ARG GLY THR TRP TYR LEU THR GLY
SEQRES 17 H 254 ILE VAL SER TRP GLY GLN GLY CYS ALA THR VAL GLY HIS
SEQRES 18 H 254 PHE GLY VAL TYR THR ARG VAL SER GLN TYR ILE GLU TRP
SEQRES 19 H 254 LEU GLN LYS LEU MET ARG SER GLU PRO ARG PRO GLY VAL
SEQRES 20 H 254 LEU LEU ARG ALA PRO PHE PRO
SEQRES 1 T 218 GLY THR THR ASN THR VAL ALA ALA TYR ASN LEU THR TRP
SEQRES 2 T 218 LYS SER THR ASN PHE LYS THR ILE LEU GLU TRP GLU PRO
SEQRES 3 T 218 LYS PRO VAL ASN GLN VAL TYR THR VAL GLN ILE SER THR
SEQRES 4 T 218 LYS SER GLY ASP TRP LYS SER LYS CYS PHE TYR THR THR
SEQRES 5 T 218 ASP THR GLU CYS ASP LEU THR ASP GLU ILE VAL LYS ASP
SEQRES 6 T 218 VAL LYS GLN THR TYR LEU ALA ARG VAL PHE SER TYR PRO
SEQRES 7 T 218 ALA GLY ASN VAL GLU SER THR GLY SER ALA GLY GLU PRO
SEQRES 8 T 218 LEU TYR GLU ASN SER PRO GLU PHE THR PRO TYR LEU GLU
SEQRES 9 T 218 THR ASN LEU GLY GLN PRO THR ILE GLN SER PHE GLU GLN
SEQRES 10 T 218 VAL GLY THR LYS VAL ASN VAL THR VAL GLU ASP GLU ARG
SEQRES 11 T 218 THR LEU VAL ARG ARG ASN ASN THR PHE LEU SER LEU ARG
SEQRES 12 T 218 ASP VAL PHE GLY LYS ASP LEU ILE TYR THR LEU TYR TYR
SEQRES 13 T 218 TRP LYS SER SER SER SER GLY LYS LYS THR ALA LYS THR
SEQRES 14 T 218 ASN THR ASN GLU PHE LEU ILE ASP VAL ASP LYS GLY GLU
SEQRES 15 T 218 ASN TYR CYS PHE SER VAL GLN ALA VAL ILE PRO SER ARG
SEQRES 16 T 218 THR VAL ASN ARG LYS SER THR ASP SER PRO VAL GLU CYS
SEQRES 17 T 218 MET GLY GLN GLU LYS GLY GLU PHE ARG GLU
HET N1H H 258 30
HETNAM N1H {5-(5-AMINO-1H-PYRROLO[3,2-B]PYRIDIN-2-YL)-6-HYDROXY-
HETNAM 2 N1H 3'-NITRO-BIPHENYL-3-YL]-ACETIC ACID
FORMUL 4 N1H C21 H16 N4 O5
FORMUL 5 HOH *153(H2 O)
HELIX 1 1 GLN L 49 SER L 53 5 5
HELIX 2 2 ASP L 86 GLN L 88 5 3
HELIX 3 3 ASN L 93 CYS L 98 5 6
HELIX 4 4 ILE L 138 GLU L 142 5 5
HELIX 5 5 ALA H 55 ASP H 60 5 6
HELIX 6 6 GLU H 125 THR H 129C 1 8
HELIX 7 7 LEU H 129D VAL H 129G 5 4
HELIX 8 8 MET H 164 SER H 170B 1 9
HELIX 9 9 TYR H 234 ARG H 243 1 10
HELIX 10 10 LEU T 59 VAL T 64 1 6
HELIX 11 11 THR T 101 THR T 106 1 6
HELIX 12 12 LEU T 143 GLY T 148 1 6
HELIX 13 13 LYS T 149 LEU T 151 5 3
SHEET 1 A 2 SER L 60 ASP L 63 0
SHEET 2 A 2 TYR L 68 PHE L 71 -1 O PHE L 71 N SER L 60
SHEET 1 B 2 PHE L 76 GLU L 77 0
SHEET 2 B 2 THR L 83 HIS L 84 -1 O THR L 83 N GLU L 77
SHEET 1 C 2 TYR L 101 HIS L 105 0
SHEET 2 C 2 THR L 108 ARG L 113 -1 O ARG L 113 N TYR L 101
SHEET 1 D 2 TYR L 118 LEU L 120 0
SHEET 2 D 2 CYS L 127 PRO L 129 -1 O THR L 128 N SER L 119
SHEET 1 E 8 LYS H 20 VAL H 21 0
SHEET 2 E 8 MET H 156 LEU H 163 -1 O VAL H 157 N LYS H 20
SHEET 3 E 8 MET H 180 ALA H 183 -1 O CYS H 182 N LEU H 163
SHEET 4 E 8 GLY H 226 ARG H 230 -1 O GLY H 226 N ALA H 183
SHEET 5 E 8 THR H 206 VAL H 213 -1 N ILE H 212 O THR H 229
SHEET 6 E 8 PRO H 198 TYR H 203 -1 N TYR H 203 O THR H 206
SHEET 7 E 8 PHE H 135 GLY H 140 -1 N LEU H 137 O ALA H 200
SHEET 8 E 8 MET H 156 LEU H 163 -1 O LEU H 158 N VAL H 138
SHEET 1 F 8 LEU H 251 ALA H 254 0
SHEET 2 F 8 GLN H 81 PRO H 91 1 N VAL H 88 O LEU H 252
SHEET 3 F 8 ALA H 104 LEU H 108 -1 O LEU H 105 N ILE H 89
SHEET 4 F 8 TRP H 51 SER H 54 -1 N VAL H 52 O LEU H 106
SHEET 5 F 8 ALA H 39 ASN H 48 -1 N THR H 45 O VAL H 53
SHEET 6 F 8 GLN H 30 VAL H 35 -1 N VAL H 35 O ALA H 39
SHEET 7 F 8 LEU H 64 LEU H 68 -1 O ILE H 65 N LEU H 34
SHEET 8 F 8 GLN H 81 PRO H 91 -1 O ARG H 83 N ALA H 66
SHEET 1 G 3 TYR T 10 THR T 17 0
SHEET 2 G 3 LYS T 20 GLU T 26 -1 O ILE T 22 N LYS T 15
SHEET 3 G 3 GLU T 56 ASP T 58 -1 O CYS T 57 N LEU T 23
SHEET 1 H 4 LYS T 46 THR T 52 0
SHEET 2 H 4 GLN T 32 THR T 40 -1 N VAL T 36 O LYS T 48
SHEET 3 H 4 TYR T 71 PRO T 79 -1 O PHE T 76 N THR T 35
SHEET 4 H 4 TYR T 94 ASN T 96 -1 O GLU T 95 N VAL T 75
SHEET 1 I 2 ARG T 131 ARG T 136 0
SHEET 2 I 2 THR T 139 SER T 142 -1 O LEU T 141 N VAL T 134
SHEET 1 J 2 ILE T 152 TYR T 153 0
SHEET 2 J 2 ALA T 191 VAL T 192 -1 O VAL T 192 N ILE T 152
SSBOND 1 CYS L 50 CYS L 61 1555 1555 2.03
SSBOND 2 CYS L 55 CYS L 70 1555 1555 2.02
SSBOND 3 CYS L 72 CYS L 81 1555 1555 2.03
SSBOND 4 CYS L 91 CYS L 102 1555 1555 2.03
SSBOND 5 CYS L 98 CYS L 112 1555 1555 2.03
SSBOND 6 CYS L 114 CYS L 127 1555 1555 2.02
SSBOND 7 CYS L 135 CYS H 122 1555 1555 2.04
SSBOND 8 CYS H 22 CYS H 27 1555 1555 2.03
SSBOND 9 CYS H 42 CYS H 58 1555 1555 2.01
SSBOND 10 CYS H 168 CYS H 182 1555 1555 2.03
SSBOND 11 CYS H 191 CYS H 220 1555 1555 2.01
SSBOND 12 CYS T 49 CYS T 57 1555 1555 2.05
CISPEP 1 PHE H 256 PRO H 257 0 9.06
CISPEP 2 GLU T 26 PRO T 27 0 -16.05
SITE 1 AC1 16 CYS H 42 HIS H 57 CYS H 58 ASP H 60
SITE 2 AC1 16 LYS H 60A ASP H 189 SER H 190 CYS H 191
SITE 3 AC1 16 LYS H 192 SER H 195 VAL H 213 SER H 214
SITE 4 AC1 16 TRP H 215 GLN H 217 GLY H 219 HOH H 332
CRYST1 78.070 68.940 78.730 90.00 90.17 90.00 P 1 21 1 2
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 0.012809 0.000000 0.000038 0.00000
SCALE2 0.000000 0.014505 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012702 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
