HEADER HYDROLASE/HYDROLASE INHIBITOR 01-JUL-04 1TWX
TITLE CRYSTAL STRUCTURE OF THE THROMBIN MUTANT D221A/D222K
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTHROMBIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: LIGHT CHAIN;
COMPND 5 SYNONYM: COAGULATION FACTOR II;
COMPND 6 EC: 3.4.21.5;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: PROTHROMBIN;
COMPND 10 CHAIN: B;
COMPND 11 FRAGMENT: HEAVY CHAIN;
COMPND 12 SYNONYM: COAGULATION FACTOR II;
COMPND 13 EC: 3.4.21.5;
COMPND 14 ENGINEERED: YES;
COMPND 15 MUTATION: YES;
COMPND 16 MOL_ID: 3;
COMPND 17 MOLECULE: HIRUDIN;
COMPND 18 CHAIN: C;
COMPND 19 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: F2;
SOURCE 6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE 9 EXPRESSION_SYSTEM_CELL: KIDNEY;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: HPC4-PNUT;
SOURCE 12 MOL_ID: 2;
SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 14 ORGANISM_COMMON: HUMAN;
SOURCE 15 ORGANISM_TAXID: 9606;
SOURCE 16 GENE: F2;
SOURCE 17 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 18 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE 19 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE 20 EXPRESSION_SYSTEM_CELL: KIDNEY;
SOURCE 21 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 22 EXPRESSION_SYSTEM_PLASMID: HPC4-PNUT;
SOURCE 23 MOL_ID: 3;
SOURCE 24 SYNTHETIC: YES
KEYWDS THROMBIN, HYDROLASE, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR A.O.PINEDA,E.ZHANG,E.R.GUINTO,S.N.SAVVIDES,A.TULINSKY,E.DI CERA
REVDAT 3 13-JUL-11 1TWX 1 VERSN
REVDAT 2 24-FEB-09 1TWX 1 VERSN
REVDAT 1 19-APR-05 1TWX 0
JRNL AUTH A.O.PINEDA,E.ZHANG,E.R.GUINTO,S.N.SAVVIDES,A.TULINSKY,
JRNL AUTH 2 E.DI CERA
JRNL TITL CRYSTAL STRUCTURE OF THE THROMBIN MUTANT D221A/D222K: THE
JRNL TITL 2 ASP222:ARG187 ION-PAIR STABILIZES THE FAST FORM
JRNL REF BIOPHYS.CHEM. V. 112 253 2004
JRNL REFN ISSN 0301-4622
JRNL PMID 15572256
JRNL DOI 10.1016/J.BPC.2004.07.027
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 622131.910
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 77.4
REMARK 3 NUMBER OF REFLECTIONS : 11514
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 SET) : 0.205
REMARK 3 FREE R VALUE : 0.268
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.300
REMARK 3 FREE R VALUE TEST SET COUNT : 839
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.009
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.55
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 55.30
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1257
REMARK 3 BIN R VALUE (WORKING SET) : 0.3620
REMARK 3 BIN FREE R VALUE : 0.3870
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 6.80
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 92
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.040
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2346
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 14
REMARK 3 SOLVENT ATOMS : 141
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 12.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.37000
REMARK 3 B22 (A**2) : -7.36000
REMARK 3 B33 (A**2) : 9.73000
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.32
REMARK 3 ESD FROM SIGMAA (A) : 0.56
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.43
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.59
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.026
REMARK 3 BOND ANGLES (DEGREES) : 1.70
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.80
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.66
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
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 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.39
REMARK 3 BSOL : 75.68
REMARK 3
REMARK 3 NCS MODEL : CONSTR
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : NAG.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : STY.PAR
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : NAG.TOPO
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : STY.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1TWX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-JUL-04.
REMARK 100 THE RCSB ID CODE IS RCSB022985.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-APR-00
REMARK 200 TEMPERATURE (KELVIN) : 148
REMARK 200 PH : 7.3
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 RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS II
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13866
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 72.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.06800
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) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.30
REMARK 200 COMPLETENESS FOR SHELL (%) : 48.0
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: CNS
REMARK 200 STARTING MODEL: 1PPB
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.41
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM PHOSPHATE, 26% PEG 8000,
REMARK 280 PH 7.3, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
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 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 50.30000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 50.30000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 46.07500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 40.00500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 46.07500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 40.00500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 50.30000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 46.07500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 40.00500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 50.30000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 46.07500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 40.00500
REMARK 290 SMTRY3 8 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: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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 TRP B 147A
REMARK 465 THR B 147B
REMARK 465 ALA B 147C
REMARK 465 ASN B 147D
REMARK 465 VAL B 147E
REMARK 465 GLY B 147F
REMARK 465 LYS B 147G
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 ARG B 97 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 126 CG CD NE CZ NH1 NH2
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 CG2 VAL B 158 O HOH B 594 1.71
REMARK 500 O HOH B 475 O HOH B 536 1.90
REMARK 500 O CYS A 1 N LEU A 3 1.96
REMARK 500 O ASP A 14L O HOH A 604 2.10
REMARK 500 O GLY B 142 O HOH B 517 2.18
REMARK 500
REMARK 500 REMARK: NULL
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 HOH A 646 O HOH B 661 4556 0.59
REMARK 500 O HOH B 628 O HOH B 641 7545 0.67
REMARK 500 O HOH B 650 O HOH B 651 3655 0.73
REMARK 500 O HOH B 592 O HOH B 617 7555 0.78
REMARK 500 O HOH A 627 O HOH B 663 7545 1.02
REMARK 500 NH1 ARG A 14D NH1 ARG A 14D 4556 1.63
REMARK 500 O HOH B 585 O HOH B 615 7555 1.67
REMARK 500 O HOH B 601 O HOH B 601 3655 1.73
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 ASP C 300 N ASP C 300 CA 0.275
REMARK 500 ASP C 300 CG ASP C 300 OD1 0.409
REMARK 500 ASP C 300 CG ASP C 300 OD2 0.525
REMARK 500 ASP C 300 CA ASP C 300 C 0.348
REMARK 500 ASP C 300 C ASP C 300 O 0.135
REMARK 500 PRO C 305 N PRO C 305 CA 0.190
REMARK 500 PRO C 305 CG PRO C 305 CD 0.210
REMARK 500 PRO C 305 CD PRO C 305 N 0.214
REMARK 500 GLY C 306 CA GLY C 306 C 0.232
REMARK 500 GLY C 306 C GLY C 306 O 0.296
REMARK 500 GLU C 307 CG GLU C 307 CD 0.105
REMARK 500 GLU C 307 CD GLU C 307 OE1 0.337
REMARK 500 GLU C 307 CD GLU C 307 OE2 0.214
REMARK 500 GLU C 307 C GLU C 307 O 0.173
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 C 300 CB - CA - C ANGL. DEV. = -12.1 DEGREES
REMARK 500 ASP C 300 N - CA - CB ANGL. DEV. = -11.3 DEGREES
REMARK 500 PHE C 301 C - N - CA ANGL. DEV. = -15.2 DEGREES
REMARK 500 GLU C 303 O - C - N ANGL. DEV. = 10.6 DEGREES
REMARK 500 ILE C 304 C - N - CA ANGL. DEV. = -16.0 DEGREES
REMARK 500 PRO C 305 N - CA - CB ANGL. DEV. = 10.0 DEGREES
REMARK 500 PRO C 305 C - N - CA ANGL. DEV. = 9.2 DEGREES
REMARK 500 GLU C 307 N - CA - CB ANGL. DEV. = -13.7 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 CYS A 1 -167.96 -40.92
REMARK 500 PHE A 7 -75.18 -134.71
REMARK 500 GLU B 18 41.98 76.37
REMARK 500 LYS B 36 -73.29 -63.59
REMARK 500 SER B 48 158.43 159.25
REMARK 500 TYR B 60A 85.14 -162.16
REMARK 500 ASN B 60G 53.94 -163.24
REMARK 500 ASN B 62 34.19 -86.87
REMARK 500 HIS B 71 -49.86 -142.10
REMARK 500 ILE B 79 -73.80 -138.12
REMARK 500 GLU B 97A -84.09 -121.89
REMARK 500 PRO B 111 155.63 -45.98
REMARK 500 SER B 115 -167.55 -175.51
REMARK 500 GLU B 146 -72.09 -60.43
REMARK 500 SER B 214 -66.02 -104.16
REMARK 500 GLU B 217 78.88 -116.77
REMARK 500 HIS B 230 94.07 -66.04
REMARK 500 PHE B 245 42.58 -84.95
REMARK 500 PRO C 305 144.99 -39.83
REMARK 500 TYS C 308 46.19 -74.42
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B 574 DISTANCE = 6.11 ANGSTROMS
REMARK 525 HOH B 634 DISTANCE = 9.03 ANGSTROMS
REMARK 525 HOH B 635 DISTANCE = 7.10 ANGSTROMS
REMARK 525 HOH B 643 DISTANCE = 6.77 ANGSTROMS
REMARK 525 HOH B 650 DISTANCE = 5.37 ANGSTROMS
REMARK 525 HOH B 651 DISTANCE = 5.81 ANGSTROMS
REMARK 525 HOH B 655 DISTANCE = 7.42 ANGSTROMS
REMARK 525 HOH B 657 DISTANCE = 5.18 ANGSTROMS
REMARK 525 HOH B 660 DISTANCE = 5.80 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN C OF HIRUDIN
DBREF 1TWX A 1 14 UNP P00734 THRB_HUMAN 334 361
DBREF 1TWX B 16 247 UNP P00734 THRB_HUMAN 364 622
DBREF 1TWX C 300 309 UNP P00734 HIR2_HIRME 55 65
SEQADV 1TWX ALA B 183 UNP P00734 ASP 595 ENGINEERED
SEQADV 1TWX LYS B 185 UNP P00734 ASP 597 ENGINEERED
SEQRES 1 A 28 ALA ASP CYS GLY LEU ARG PRO LEU PHE GLU LYS LYS SER
SEQRES 2 A 28 LEU GLU ASP LYS THR GLU ARG GLU LEU LEU GLU SER TYR
SEQRES 3 A 28 ILE ASP
SEQRES 1 B 259 ILE VAL GLU GLY SER ASP ALA GLU ILE GLY MET SER PRO
SEQRES 2 B 259 TRP GLN VAL MET LEU PHE ARG LYS SER PRO GLN GLU LEU
SEQRES 3 B 259 LEU CYS GLY ALA SER LEU ILE SER ASP ARG TRP VAL LEU
SEQRES 4 B 259 THR ALA ALA HIS CYS LEU LEU TYR PRO PRO TRP ASP LYS
SEQRES 5 B 259 ASN PHE THR GLU ASN ASP LEU LEU VAL ARG ILE GLY LYS
SEQRES 6 B 259 HIS SER ARG THR ARG TYR GLU ARG ASN ILE GLU LYS ILE
SEQRES 7 B 259 SER MET LEU GLU LYS ILE TYR ILE HIS PRO ARG TYR ASN
SEQRES 8 B 259 TRP ARG GLU ASN LEU ASP ARG ASP ILE ALA LEU MET LYS
SEQRES 9 B 259 LEU LYS LYS PRO VAL ALA PHE SER ASP TYR ILE HIS PRO
SEQRES 10 B 259 VAL CYS LEU PRO ASP ARG GLU THR ALA ALA SER LEU LEU
SEQRES 11 B 259 GLN ALA GLY TYR LYS GLY ARG VAL THR GLY TRP GLY ASN
SEQRES 12 B 259 LEU LYS GLU THR TRP THR ALA ASN VAL GLY LYS GLY GLN
SEQRES 13 B 259 PRO SER VAL LEU GLN VAL VAL ASN LEU PRO ILE VAL GLU
SEQRES 14 B 259 ARG PRO VAL CYS LYS ASP SER THR ARG ILE ARG ILE THR
SEQRES 15 B 259 ASP ASN MET PHE CYS ALA GLY TYR LYS PRO ASP GLU GLY
SEQRES 16 B 259 LYS ARG GLY ASP ALA CYS GLU GLY ASP SER GLY GLY PRO
SEQRES 17 B 259 PHE VAL MET LYS SER PRO PHE ASN ASN ARG TRP TYR GLN
SEQRES 18 B 259 MET GLY ILE VAL SER TRP GLY GLU GLY CYS ALA ARG LYS
SEQRES 19 B 259 GLY LYS TYR GLY PHE TYR THR HIS VAL PHE ARG LEU LYS
SEQRES 20 B 259 LYS TRP ILE GLN LYS VAL ILE ASP GLN PHE GLY GLU
SEQRES 1 C 10 ASP PHE GLU GLU ILE PRO GLY GLU TYS LEU
MODRES 1TWX ASN B 60G ASN GLYCOSYLATION SITE
MODRES 1TWX TYS C 308 TYR O-SULFO-L-TYROSINE
HET TYS C 308 16
HET NAG B 400 14
HETNAM TYS O-SULFO-L-TYROSINE
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
FORMUL 3 TYS C9 H11 N O6 S
FORMUL 4 NAG C8 H15 N O6
FORMUL 5 HOH *141(H2 O)
HELIX 1 1 THR A 14B ASP A 14L 1 11
HELIX 2 2 ALA B 55 CYS B 58 5 4
HELIX 3 3 PRO B 60B ASP B 60E 5 4
HELIX 4 4 THR B 60I ASN B 62 5 3
HELIX 5 5 ASP B 125 LEU B 130 1 9
HELIX 6 6 GLU B 164 ASP B 170 1 7
HELIX 7 7 LEU B 234 PHE B 245 1 12
SHEET 1 A 7 SER B 20 ASP B 21 0
SHEET 2 A 7 GLN B 156 PRO B 161 -1 O VAL B 157 N SER B 20
SHEET 3 A 7 LYS B 135 GLY B 140 -1 N GLY B 136 O LEU B 160
SHEET 4 A 7 PRO B 198 LYS B 202 -1 O VAL B 200 N ARG B 137
SHEET 5 A 7 TRP B 207 TRP B 215 -1 O TYR B 208 N MET B 201
SHEET 6 A 7 GLY B 226 HIS B 230 -1 O PHE B 227 N TRP B 215
SHEET 7 A 7 MET B 180 ALA B 183 -1 N PHE B 181 O TYR B 228
SHEET 1 B 7 GLN B 30 ARG B 35 0
SHEET 2 B 7 GLU B 39 SER B 48 -1 O GLU B 39 N ARG B 35
SHEET 3 B 7 TRP B 51 THR B 54 -1 O LEU B 53 N SER B 45
SHEET 4 B 7 ALA B 104 LEU B 108 -1 O MET B 106 N VAL B 52
SHEET 5 B 7 LYS B 81 ILE B 90 -1 N GLU B 86 O LYS B 107
SHEET 6 B 7 LEU B 64 ILE B 68 -1 N ILE B 68 O LYS B 81
SHEET 7 B 7 GLN B 30 ARG B 35 -1 N MET B 32 O ARG B 67
SHEET 1 C 2 LEU B 60 TYR B 60A 0
SHEET 2 C 2 LYS B 60F ASN B 60G-1 O LYS B 60F N TYR B 60A
SSBOND 1 CYS A 1 CYS B 122 1555 1555 2.05
SSBOND 2 CYS B 42 CYS B 58 1555 1555 2.07
SSBOND 3 CYS B 168 CYS B 182 1555 1555 2.03
SSBOND 4 CYS B 191 CYS B 220 1555 1555 2.03
LINK ND2 ASN B 60G O3 NAG B 400 1555 1555 1.38
LINK C GLU C 307 N TYS C 308 1555 1555 1.62
LINK C TYS C 308 N LEU C 309 1555 1555 1.33
CISPEP 1 SER B 36A PRO B 37 0 0.01
SITE 1 AC1 3 LEU B 60 ASN B 60G HOH B 481
SITE 1 AC2 12 PHE B 34 GLN B 38 LEU B 65 ARG B 67
SITE 2 AC2 12 ARG B 73 THR B 74 ARG B 75 TYR B 76
SITE 3 AC2 12 LYS B 81 ILE B 82 HOH C 529 HOH C 564
CRYST1 92.150 80.010 100.600 90.00 90.00 90.00 C 2 2 21 8
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 0.010852 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012498 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009940 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
