HEADER HYDROLASE/HYDROLASE INHIBITOR 09-JAN-10 3LC5
TITLE SELECTIVE BENZOTHIOPHINE INHIBITORS OF FACTOR IXA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: COAGULATION FACTOR IX;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 227-461;
COMPND 5 SYNONYM: CHRISTMAS FACTOR, PLASMA THROMBOPLASTIN COMPONENT,
COMPND 6 PTC, COAGULATION FACTOR IXA LIGHT CHAIN, COAGULATION FACTOR
COMPND 7 IXA HEAVY CHAIN;
COMPND 8 EC: 3.4.21.22;
COMPND 9 ENGINEERED: YES;
COMPND 10 MOL_ID: 2;
COMPND 11 MOLECULE: COAGULATION FACTOR IX;
COMPND 12 CHAIN: B;
COMPND 13 FRAGMENT: RESIDUES 133-188;
COMPND 14 SYNONYM: CHRISTMAS FACTOR, PLASMA THROMBOPLASTIN COMPONENT,
COMPND 15 PTC, COAGULATION FACTOR IXA LIGHT CHAIN, COAGULATION FACTOR
COMPND 16 IXA HEAVY CHAIN;
COMPND 17 EC: 3.4.21.22;
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: F9;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 GENE: F9;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PROTEIN-INHIBITOR COMPLEX, PEPTIDASE S1, BLOOD COAGULATION,
KEYWDS 2 CALCIUM, CLEAVAGE ON PAIR OF BASIC RESIDUES, DISEASE
KEYWDS 3 MUTATION, DISULFIDE BOND, EGF-LIKE DOMAIN, GAMMA-
KEYWDS 4 CARBOXYGLUTAMIC ACID, GLYCOPROTEIN, HEMOPHILIA, HYDROLASE,
KEYWDS 5 HYDROXYLATION, PHARMACEUTICAL, PHOSPHOPROTEIN,
KEYWDS 6 POLYMORPHISM, PROTEASE, SECRETED, SERINE PROTEASE,
KEYWDS 7 SULFATION, ZYMOGEN, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR S.WANG,R.BECK
REVDAT 2 02-MAR-10 3LC5 1 JRNL
REVDAT 1 23-FEB-10 3LC5 0
JRNL AUTH S.WANG,R.BECK,A.BURD,T.BLENCH,F.MARLIN,T.AYELE,
JRNL AUTH 2 S.BUXTON,C.DAGOSTIN,M.MALIC,R.JOSHI,J.BARRY,
JRNL AUTH 3 M.SAJAD,C.CHEUNG,S.SHAIKH,S.CHAHWALA,C.CHANDER,
JRNL AUTH 4 C.BAUMGARTNER,H.P.HOLTHOFF,E.MURRAY,M.BLACKNEY,
JRNL AUTH 5 A.GIDDINGS
JRNL TITL STRUCTURE BASED DRUG DESIGN: DEVELOPMENT OF POTENT
JRNL TITL 2 AND SELECTIVE FACTOR IXA (FIXA) INHIBITORS.
JRNL REF J.MED.CHEM. V. 53 1473 2010
JRNL REFN ISSN 0022-2623
JRNL PMID 20121197
JRNL DOI 10.1021/JM901476X
REMARK 2
REMARK 2 RESOLUTION. 2.62 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) : 2.62
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 94.07
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.0
REMARK 3 NUMBER OF REFLECTIONS : 7348
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) : 0.213
REMARK 3 R VALUE (WORKING SET) : 0.206
REMARK 3 FREE R VALUE : 0.277
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 8.800
REMARK 3 FREE R VALUE TEST SET COUNT : 711
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) : 2.62
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.69
REMARK 3 REFLECTION IN BIN (WORKING SET) : 311
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 55.27
REMARK 3 BIN R VALUE (WORKING SET) : 0.2890
REMARK 3 BIN FREE R VALUE SET COUNT : 30
REMARK 3 BIN FREE R VALUE : 0.4290
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2251
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 32
REMARK 3 SOLVENT ATOMS : 13
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 19.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.93
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.51000
REMARK 3 B22 (A**2) : -0.93000
REMARK 3 B33 (A**2) : -0.58000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.421
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.311
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 24.884
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.920
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.858
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2283 ; 0.008 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 1985 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3103 ; 1.101 ; 1.948
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4608 ; 0.724 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 284 ; 6.087 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 99 ;37.451 ;24.444
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 358 ;15.570 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 10 ;12.212 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 339 ; 0.067 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2565 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 469 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 411 ; 0.189 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 1985 ; 0.172 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1096 ; 0.174 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 1259 ; 0.079 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 56 ; 0.116 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 4 ; 0.171 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 10 ; 0.106 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 38 ; 0.177 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 6 ; 0.242 ; 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): 1463 ; 1.231 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 594 ; 0.240 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2277 ; 2.002 ; 3.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 962 ; 2.570 ; 4.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 826 ; 3.828 ; 6.000
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: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 3LC5 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-JAN-10.
REMARK 100 THE RCSB ID CODE IS RCSB057095.
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) : 1.54179
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 8059
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.620
REMARK 200 RESOLUTION RANGE LOW (A) : 94.070
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
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 : 5.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.62
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 55.3
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 : 5.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
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 (%): 40.08
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.05
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 21.56000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 46.99250
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 32.86900
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 46.99250
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 21.56000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 32.86900
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1600 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13780 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 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 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 THR B 140
REMARK 465 SER B 141
REMARK 465 LYS B 142
REMARK 475
REMARK 475 ZERO OCCUPANCY RESIDUES
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)
REMARK 475 M RES C SSEQI
REMARK 475 LYS A 148
REMARK 475 GLY A 149
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 LYS A 98 CD CE NZ
REMARK 480 ARG A 150 CG CD NE CZ NH1 NH2
REMARK 480 TYR A 177 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 480 ASN A 178 CG OD1 ND2
REMARK 480 MET B 86 CG SD CE
REMARK 480 LYS B 91 CD CE NZ
REMARK 480 ARG B 94 CZ NH1 NH2
REMARK 480 LYS B 100 CG CD CE NZ
REMARK 480 SER B 102 OG
REMARK 480 ASP B 104 CG OD1 OD2
REMARK 480 LYS B 106 CG CD CE NZ
REMARK 480 VAL B 107 CG1 CG2
REMARK 480 VAL B 108 CG1 CG2
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 HIS A 71 -54.73 -132.05
REMARK 500 ALA A 124 -173.31 -69.61
REMARK 500 GLU A 186 32.62 -97.78
REMARK 500 SER A 214 -64.17 -127.95
REMARK 500 GLU A 219 -173.99 65.43
REMARK 500 ARG B 94 15.79 57.78
REMARK 500 GLN B 97 -86.78 -105.93
REMARK 500 ASP B 104 21.99 -78.86
REMARK 500 LYS B 122 -55.87 -145.00
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 HIS A 147 -10.97
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 500 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 77 OE1
REMARK 620 2 GLU A 70 OE1 104.4
REMARK 620 3 GLU A 80 OE2 109.2 103.4
REMARK 620 4 GLU A 75 O 116.7 129.4 90.2
REMARK 620 5 ASN A 72 O 87.0 67.8 163.4 85.5
REMARK 620 6 HOH A 246 O 168.3 65.9 80.4 68.9 83.1
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IZX A 1
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3LC3 RELATED DB: PDB
DBREF 3LC5 A 16 245 UNP P00740 FA9_HUMAN 227 461
DBREF 3LC5 B 87 142 UNP P00740 FA9_HUMAN 133 188
SEQADV 3LC5 MET B 86 UNP P00740 INITIATING METHIONINE
SEQRES 1 A 235 VAL VAL GLY GLY GLU ASP ALA LYS PRO GLY GLN PHE PRO
SEQRES 2 A 235 TRP GLN VAL VAL LEU ASN GLY LYS VAL ASP ALA PHE CYS
SEQRES 3 A 235 GLY GLY SER ILE VAL ASN GLU LYS TRP ILE VAL THR ALA
SEQRES 4 A 235 ALA HIS CYS VAL GLU THR GLY VAL LYS ILE THR VAL VAL
SEQRES 5 A 235 ALA GLY GLU HIS ASN ILE GLU GLU THR GLU HIS THR GLU
SEQRES 6 A 235 GLN LYS ARG ASN VAL ILE ARG ILE ILE PRO HIS HIS ASN
SEQRES 7 A 235 TYR ASN ALA ALA ILE ASN LYS TYR ASN HIS ASP ILE ALA
SEQRES 8 A 235 LEU LEU GLU LEU ASP GLU PRO LEU VAL LEU ASN SER TYR
SEQRES 9 A 235 VAL THR PRO ILE CYS ILE ALA ASP LYS GLU TYR THR ASN
SEQRES 10 A 235 ILE PHE LEU LYS PHE GLY SER GLY TYR VAL SER GLY TRP
SEQRES 11 A 235 GLY ARG VAL PHE HIS LYS GLY ARG SER ALA LEU VAL LEU
SEQRES 12 A 235 GLN TYR LEU ARG VAL PRO LEU VAL ASP ARG ALA THR CYS
SEQRES 13 A 235 LEU ARG SER THR LYS PHE THR ILE TYR ASN ASN MET PHE
SEQRES 14 A 235 CYS ALA GLY PHE HIS GLU GLY GLY ARG ASP SER CYS GLN
SEQRES 15 A 235 GLY ASP SER GLY GLY PRO HIS VAL THR GLU VAL GLU GLY
SEQRES 16 A 235 THR SER PHE LEU THR GLY ILE ILE SER TRP GLY GLU GLU
SEQRES 17 A 235 CYS ALA MET LYS GLY LYS TYR GLY ILE TYR THR LYS VAL
SEQRES 18 A 235 SER ARG TYR VAL ASN TRP ILE LYS GLU LYS THR LYS LEU
SEQRES 19 A 235 THR
SEQRES 1 B 57 MET THR CYS ASN ILE LYS ASN GLY ARG CYS GLU GLN PHE
SEQRES 2 B 57 CYS LYS ASN SER ALA ASP ASN LYS VAL VAL CYS SER CYS
SEQRES 3 B 57 THR GLU GLY TYR ARG LEU ALA GLU ASN GLN LYS SER CYS
SEQRES 4 B 57 GLU PRO ALA VAL PRO PHE PRO CYS GLY ARG VAL SER VAL
SEQRES 5 B 57 SER GLN THR SER LYS
HET CA A 500 1
HET IZX A 1 31
HETNAM CA CALCIUM ION
HETNAM IZX 1-{4-[(R)-PHENYL(3-PHENYL-1,2,4-OXADIAZOL-5-YL)
HETNAM 2 IZX METHOXY]-1-BENZOTHIOPHEN-2-YL}METHANEDIAMINE
FORMUL 3 CA CA 2+
FORMUL 4 IZX C24 H20 N4 O2 S
FORMUL 5 HOH *13(H2 O)
HELIX 1 1 ALA A 55 VAL A 59 5 5
HELIX 2 2 ASP A 125 PHE A 133 1 11
HELIX 3 3 ASP A 164 THR A 172 1 9
HELIX 4 4 TYR A 234 THR A 242 1 9
HELIX 5 5 ILE B 90 CYS B 95 5 6
SHEET 1 A 8 GLU A 20 ASP A 21 0
SHEET 2 A 8 GLN A 156 VAL A 163 -1 O TYR A 157 N GLU A 20
SHEET 3 A 8 MET A 180 ALA A 183 -1 O CYS A 182 N VAL A 163
SHEET 4 A 8 GLY A 226 LYS A 230 -1 O TYR A 228 N PHE A 181
SHEET 5 A 8 THR A 206 TRP A 215 -1 N TRP A 215 O ILE A 227
SHEET 6 A 8 PRO A 198 VAL A 203 -1 N THR A 201 O PHE A 208
SHEET 7 A 8 SER A 135 GLY A 140 -1 N TYR A 137 O VAL A 200
SHEET 8 A 8 GLN A 156 VAL A 163 -1 O LEU A 158 N VAL A 138
SHEET 1 B 7 GLN A 30 ASN A 34 0
SHEET 2 B 7 CYS A 42 ILE A 46 -1 O CYS A 42 N LEU A 33
SHEET 3 B 7 TRP A 51 THR A 54 -1 O VAL A 53 N SER A 45
SHEET 4 B 7 ALA A 104 LEU A 108 -1 O LEU A 106 N ILE A 52
SHEET 5 B 7 GLN A 81 PRO A 90 -1 N ARG A 87 O GLU A 107
SHEET 6 B 7 THR A 65 ALA A 68 -1 N ALA A 68 O GLN A 81
SHEET 7 B 7 GLN A 30 ASN A 34 -1 N ASN A 34 O THR A 65
SHEET 1 C 2 PHE B 98 ASN B 101 0
SHEET 2 C 2 VAL B 107 SER B 110 -1 O SER B 110 N PHE B 98
SHEET 1 D 2 TYR B 115 LEU B 117 0
SHEET 2 D 2 CYS B 124 PRO B 126 -1 O GLU B 125 N ARG B 116
SSBOND 1 CYS A 42 CYS A 58 1555 1555 2.04
SSBOND 2 CYS A 122 CYS B 132 1555 1555 2.02
SSBOND 3 CYS A 168 CYS A 182 1555 1555 2.01
SSBOND 4 CYS A 191 CYS A 220 1555 1555 2.05
SSBOND 5 CYS B 88 CYS B 99 1555 1555 2.05
SSBOND 6 CYS B 95 CYS B 109 1555 1555 2.04
SSBOND 7 CYS B 111 CYS B 124 1555 1555 2.03
LINK OE1 GLU A 77 CA CA A 500 1555 1555 2.14
LINK OE1 GLU A 70 CA CA A 500 1555 1555 2.34
LINK OE2 GLU A 80 CA CA A 500 1555 1555 2.37
LINK O GLU A 75 CA CA A 500 1555 1555 2.44
LINK O ASN A 72 CA CA A 500 1555 1555 2.55
LINK CA CA A 500 O HOH A 246 1555 1555 2.25
SITE 1 AC1 6 GLU A 70 ASN A 72 GLU A 75 GLU A 77
SITE 2 AC1 6 GLU A 80 HOH A 246
SITE 1 AC2 12 ARG A 143 HIS A 147 PHE A 174 ASP A 189
SITE 2 AC2 12 SER A 190 GLN A 192 SER A 195 GLY A 216
SITE 3 AC2 12 GLU A 219 GLY A 226 ARG B 116 GLU B 119
CRYST1 43.120 65.738 93.985 90.00 90.00 90.00 P 21 21 21 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 0.023191 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015212 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010640 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
