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HEADER BLOOD CLOTTING, HYDROLASE 06-MAR-03 1O2G
TITLE ELABORATE MANIFOLD OF SHORT HYDROGEN BOND ARRAYS MEDIATING
TITLE 2 BINDING OF ACTIVE SITE-DIRECTED SERINE PROTEASE INHIBITORS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THROMBIN;
COMPND 3 CHAIN: L;
COMPND 4 FRAGMENT: LIGHT CHAIN, RESIDUES 328-363;
COMPND 5 SYNONYM: COAGULATION FACTOR II;
COMPND 6 EC: 3.4.21.5;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: THROMBIN;
COMPND 9 CHAIN: H;
COMPND 10 FRAGMENT: HEAVY CHAIN, RESIDUES 364-620;
COMPND 11 SYNONYM: COAGULATION FACTOR II;
COMPND 12 EC: 3.4.21.5;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: ACETYL HIRUDIN;
COMPND 15 CHAIN: I;
COMPND 16 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 MOL_ID: 2;
SOURCE 5 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 6 ORGANISM_COMMON: HUMAN;
SOURCE 7 MOL_ID: 3;
SOURCE 8 SYNTHETIC: YES
KEYWDS SERINE PROTEASE, SHORT HYDROGEN BOND, INHIBITION MECHANISM,
KEYWDS 2 SHIFT OF PKA, TRYPSIN, THROMBIN, UROKINASE, FACTOR XA
EXPDTA X-RAY DIFFRACTION
AUTHOR B.A.KATZ,K.ELROD,E.VERNER,R.L.MACKMAN,C.LUONG,W.SHRADER,
AUTHOR 2 M.SENDZIK,J.R.SPENCER,P.A.SPRENGELER,A.KOLESNIKOV,W.F.TAI,
AUTHOR 3 H.HUI,G.BREITENBUCHER,D.ALLEN,J.JANC
REVDAT 1 13-MAY-03 1O2G 0
JRNL AUTH B.A.KATZ,K.ELROD,E.VERNER,R.L.MACKMAN,C.LUONG,
JRNL AUTH 2 W.D.SHRADER,M.SENDZIK,J.R.SPENCER,P.A.SPRENGELER,
JRNL AUTH 3 A.KOLESNIKOV,V.W.-F.TAI,H.C.HUI,J.G.BREITENBUCHER,
JRNL AUTH 4 D.ALLEN,J.W.JANC
JRNL TITL ELABORATE MANIFOLD OF SHORT HYDROGEN BOND ARRAYS
JRNL TITL 2 MEDIATING BINDING OF ACTIVE SITE-DIRECTED SERINE
JRNL TITL 3 PROTEASE INHIBITORS
JRNL REF J.MOL.BIOL. V. 329 93 2003
JRNL REFN ASTM JMOBAK UK ISSN 0022-2836
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.58 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) : 1.58
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 7.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.700
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 87.3
REMARK 3 NUMBER OF REFLECTIONS : 42749
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.219
REMARK 3 FREE R VALUE : 0.250
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4349
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 : 4842
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 43
REMARK 3 SOLVENT ATOMS : 930
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) : 3.70
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
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: MET_H84, LEU_H130, VAL_H157, PRO_
REMARK 3 H166, AND ILE_H174 WERE SIMULTANEOUSLY REFINED IN TWO
REMARK 3 CONFORMATIONS. NO DENSITY WAS OBSERVED FOR THR147, TRP148,
REMARK 3 THR149, ALA149A, ASN149B, VAL149C, GLY149D, AND LYS149E IN THE
REMARK 3 AUTOLYSIS LOOP, AND THESE RESIDUES ARE NOT INCLUDED IN THE
REMARK 3 MODEL. IN THE NON-ACTIVE SITE PEPTIDE INHIBITOR
REMARK 3 (ACETYLHIRUDIN) THE TYROSINE HYDROXYL IS SULFONATED. HOH477,
REMARK 3 OGSER195 AND O6' OF THE INHIBITOR MAKE A 3-CENTERED SHORT
REMARK 3 HYDROGEN BOND ARRAY. DISORDERED WATERS INCLUDE: HOH395 IS
REMARK 3 CLOSE TO A SYMMETRY RELATED EQUIVALENT OF ITSELF. HOH396 IS
REMARK 3 CLOSE TO A SYMMETRY RELATED EQUIVALENT OF ITSELF. HOH397 IS
REMARK 3 CLOSE TO A SYMMETRY RELATED EQUIVALENT OF ITSELF. HIS_H57 IS
REMARK 3 DOUBLY PROTONATED. HIS_H91 AND HIS_H119 ARE MONOPROTONATED ON
REMARK 3 THE EPSILON NITROGEN
REMARK 4
REMARK 4 1O2G COMPLIES WITH FORMAT V. 3.0, 1-DEC-2006
REMARK 4
REMARK 4 THIS IS THE REMEDIATED VERSION OF THIS PDB ENTRY.
REMARK 4 REMEDIATED DATA FILE REVISION 3.101 (2007-05-29)
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB.
REMARK 100 THE RCSB ID CODE IS RCSB001720.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-JUN-2002
REMARK 200 TEMPERATURE (KELVIN) : 285.0
REMARK 200 PH : 6.50
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 RUH3R
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CRYSTALCLEAR (MSC/RIGAKU)
REMARK 200 DATA SCALING SOFTWARE : CRYSTALCLEAR (MSC/RIGAKU)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 45048
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.580
REMARK 200 RESOLUTION RANGE LOW (A) : 32.190
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.9
REMARK 200 DATA REDUNDANCY : 2.000
REMARK 200 R MERGE (I) : 0.04600
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.58
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.65
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.36000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: QUANTA
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.59
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2-PROPANOL, PEG 4000, PH 6.5, VAPOR
REMARK 280 DIFFUSION AT 298 K, PH 6.50
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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 1/2+X,1/2+Y,Z
REMARK 290 4555 1/2-X,1/2+Y,-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 35.68000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.03000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 35.68000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 36.03000
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 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 3 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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 APPLY THE FOLLOWING TO CHAINS: L, H, I
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 H 146A
REMARK 465 TRP H 146B
REMARK 465 THR H 146C
REMARK 465 ALA H 146D
REMARK 465 ASN H 146E
REMARK 465 VAL H 146F
REMARK 465 GLY H 146G
REMARK 465 LYS H 146H
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
REMARK 500 OG SER H 195 O6' 696 246 2.14
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O ARG H 77A O HOH 395 2555 1.80
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: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 SER L 1E N - CA - C ANGL. DEV. =-35.2 DEGREES
REMARK 500 GLY L 1D N - CA - C ANGL. DEV. = 18.3 DEGREES
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 M RES CSSEQI PSI PHI
REMARK 500 SER L 1E -80.38 88.69
REMARK 500 ALA L 1B -59.50 127.40
REMARK 500 ASP L 14L 160.27 81.48
REMARK 525
REMARK 525 SOLVENT
REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED
REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE
REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL
REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH 467 DISTANCE = 5.01 ANGSTROMS
REMARK 525 HOH 479 DISTANCE = 5.63 ANGSTROMS
REMARK 525 HOH 495 DISTANCE = 5.63 ANGSTROMS
REMARK 525 HOH 529 DISTANCE = 8.02 ANGSTROMS
REMARK 525 HOH 697 DISTANCE = 6.29 ANGSTROMS
REMARK 525 HOH 727 DISTANCE = 5.05 ANGSTROMS
REMARK 525 HOH 785 DISTANCE = 6.95 ANGSTROMS
REMARK 525 HOH 793 DISTANCE = 6.44 ANGSTROMS
REMARK 525 HOH 800 DISTANCE = 6.80 ANGSTROMS
REMARK 525 HOH 802 DISTANCE = 5.97 ANGSTROMS
REMARK 525 HOH 834 DISTANCE = 5.23 ANGSTROMS
REMARK 525 HOH 858 DISTANCE = 5.77 ANGSTROMS
REMARK 525 HOH 865 DISTANCE = 6.26 ANGSTROMS
REMARK 525 HOH 873 DISTANCE = 9.95 ANGSTROMS
REMARK 525 HOH 879 DISTANCE = 5.51 ANGSTROMS
REMARK 525 HOH 888 DISTANCE = 6.01 ANGSTROMS
REMARK 525 HOH 910 DISTANCE = 11.76 ANGSTROMS
REMARK 525 HOH 1034 DISTANCE = 5.78 ANGSTROMS
REMARK 525 HOH 1137 DISTANCE = 7.39 ANGSTROMS
REMARK 525 HOH 1147 DISTANCE = 5.47 ANGSTROMS
REMARK 525 HOH 1166 DISTANCE = 5.90 ANGSTROMS
REMARK 525 HOH 1200 DISTANCE = 6.68 ANGSTROMS
REMARK 525 HOH 1205 DISTANCE = 5.07 ANGSTROMS
REMARK 525 HOH 1247 DISTANCE = 9.43 ANGSTROMS
REMARK 525 HOH 1263 DISTANCE = 7.02 ANGSTROMS
REMARK 525 HOH 1284 DISTANCE = 6.25 ANGSTROMS
REMARK 525 HOH 1293 DISTANCE = 5.24 ANGSTROMS
REMARK 525 HOH 1303 DISTANCE = 5.52 ANGSTROMS
REMARK 525 HOH 1309 DISTANCE = 6.48 ANGSTROMS
REMARK 525 HOH 1388 DISTANCE = 9.16 ANGSTROMS
REMARK 525 HOH 1389 DISTANCE = 7.79 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1C5N RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH A DIFFERENT INHIBITOR
DBREF 1O2G L 1H 15 UNP P00734 THRB_HUMAN 328 363
DBREF 1O2G H 16 247 UNP P00734 THRB_HUMAN 364 622
SEQRES 1 L 36 THR PHE GLY SER GLY GLU ALA ASP CYS GLY LEU ARG PRO
SEQRES 2 L 36 LEU PHE GLU LYS LYS SER LEU GLU ASP LYS THR GLU ARG
SEQRES 3 L 36 GLU LEU LEU GLU SER TYR ILE ASP GLY ARG
SEQRES 1 H 259 ILE VAL GLU GLY SER ASP ALA GLU ILE GLY MET SER PRO
SEQRES 2 H 259 TRP GLN VAL MET LEU PHE ARG LYS SER PRO GLN GLU LEU
SEQRES 3 H 259 LEU CYS GLY ALA SER LEU ILE SER ASP ARG TRP VAL LEU
SEQRES 4 H 259 THR ALA ALA HIS CYS LEU LEU TYR PRO PRO TRP ASP LYS
SEQRES 5 H 259 ASN PHE THR GLU ASN ASP LEU LEU VAL ARG ILE GLY LYS
SEQRES 6 H 259 HIS SER ARG THR ARG TYR GLU ARG ASN ILE GLU LYS ILE
SEQRES 7 H 259 SER MET LEU GLU LYS ILE TYR ILE HIS PRO ARG TYR ASN
SEQRES 8 H 259 TRP ARG GLU ASN LEU ASP ARG ASP ILE ALA LEU MET LYS
SEQRES 9 H 259 LEU LYS LYS PRO VAL ALA PHE SER ASP TYR ILE HIS PRO
SEQRES 10 H 259 VAL CYS LEU PRO ASP ARG GLU THR ALA ALA SER LEU LEU
SEQRES 11 H 259 GLN ALA GLY TYR LYS GLY ARG VAL THR GLY TRP GLY ASN
SEQRES 12 H 259 LEU LYS GLU THR TRP THR ALA ASN VAL GLY LYS GLY GLN
SEQRES 13 H 259 PRO SER VAL LEU GLN VAL VAL ASN LEU PRO ILE VAL GLU
SEQRES 14 H 259 ARG PRO VAL CYS LYS ASP SER THR ARG ILE ARG ILE THR
SEQRES 15 H 259 ASP ASN MET PHE CYS ALA GLY TYR LYS PRO ASP GLU GLY
SEQRES 16 H 259 LYS ARG GLY ASP ALA CYS GLU GLY ASP SER GLY GLY PRO
SEQRES 17 H 259 PHE VAL MET LYS SER PRO PHE ASN ASN ARG TRP TYR GLN
SEQRES 18 H 259 MET GLY ILE VAL SER TRP GLY GLU GLY CYS ASP ARG ASP
SEQRES 19 H 259 GLY LYS TYR GLY PHE TYR THR HIS VAL PHE ARG LEU LYS
SEQRES 20 H 259 LYS TRP ILE GLN LYS VAL ILE ASP GLN PHE GLY GLU
SEQRES 1 I 11 ASP PHE GLU GLU ILE PRO GLU GLU TYS LEU GLN
MODRES 1O2G TYS I 63 TYR SULFONATED TYROSINE
HET TYS I 63 24
HET NA 409 1
HET 696 246 42
HETNAM TYS SULFONATED TYROSINE
HETNAM NA SODIUM ION
HETNAM 696 3-{5-[AMINO(IMINIO)METHYL]-1H-INDOL-2-YL}-1,1'-
HETNAM 2 696 BIPHENYL-2-OLATE
HETSYN 696 CRA_8696
FORMUL 3 TYS C9 H11 N O6 S
FORMUL 4 NA NA 1+
FORMUL 5 696 C21 H17 N3 O
FORMUL 6 HOH *308(H2 O)
HELIX 1 1 PHE L 7 SER L 11 5 5
HELIX 2 2 THR L 14B TYR L 14J 1 9
HELIX 3 3 ALA H 55 CYS H 58 5 4
HELIX 4 4 PRO H 60B ASP H 60E 5 4
HELIX 5 5 THR H 60I ASN H 62 5 3
HELIX 6 6 ASP H 125 LEU H 130 1 9
HELIX 7 7 GLU H 164 ASP H 170 1 7
HELIX 8 8 LYS H 185 GLY H 186C 5 5
HELIX 9 9 VAL H 231 GLY H 246 1 16
HELIX 10 10 PRO I 60 LEU I 64 5 5
SHEET 1 A 7 SER H 20 ASP H 21 0
SHEET 2 A 7 GLN H 156 PRO H 161 -1 O VAL H 157 N SER H 20
SHEET 3 A 7 LYS H 135 GLY H 140 -1 N GLY H 136 O LEU H 160
SHEET 4 A 7 PRO H 198 LYS H 202 -1 O VAL H 200 N ARG H 137
SHEET 5 A 7 TRP H 207 TRP H 215 -1 O TYR H 208 N MET H 201
SHEET 6 A 7 GLY H 226 HIS H 230 -1 O PHE H 227 N TRP H 215
SHEET 7 A 7 MET H 180 ALA H 183 -1 N PHE H 181 O TYR H 228
SHEET 1 B 7 LYS H 81 SER H 83 0
SHEET 2 B 7 LEU H 64 ILE H 68 -1 N ILE H 68 O LYS H 81
SHEET 3 B 7 GLN H 30 ARG H 35 -1 N PHE H 34 O LEU H 65
SHEET 4 B 7 GLU H 39 LEU H 46 -1 O LEU H 41 N LEU H 33
SHEET 5 B 7 TRP H 51 THR H 54 -1 O LEU H 53 N SER H 45
SHEET 6 B 7 ALA H 104 LEU H 108 -1 O MET H 106 N VAL H 52
SHEET 7 B 7 LEU H 85 ILE H 90 -1 N LYS H 87 O LYS H 107
SSBOND 1 CYS L 1 CYS H 122
SSBOND 2 CYS H 42 CYS H 58
SSBOND 3 CYS H 168 CYS H 182
SSBOND 4 CYS H 191 CYS H 220
CISPEP 1 SER H 36A PRO H 37 0 -16.89
CRYST1 71.360 72.060 72.960 90.00 101.77 90.00 C 1 2 1 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 0.014013 0.000000 0.002920 0.00000
SCALE2 0.000000 0.013877 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014001 0.00000