HEADER HYDROLASE 22-SEP-09 3JZ1
TITLE CRYSTAL STRUCTURE OF HUMAN THROMBIN MUTANT N143P IN E:NA+ FORM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THROMBIN LIGHT CHAIN;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.4.21.5;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: THROMBIN HEAVY CHAIN;
COMPND 9 CHAIN: B;
COMPND 10 EC: 3.4.21.5;
COMPND 11 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 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_COMMON: HUMAN;
SOURCE 12 ORGANISM_TAXID: 9606;
SOURCE 13 GENE: F2;
SOURCE 14 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 15 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 10029
KEYWDS SERINE PROTEASE, ACUTE PHASE, BLOOD COAGULATION, CLEAVAGE ON PAIR OF
KEYWDS 2 BASIC RESIDUES, DISEASE MUTATION, DISULFIDE BOND, GAMMA-
KEYWDS 3 CARBOXYGLUTAMIC ACID, GLYCOPROTEIN, HYDROLASE, KRINGLE, PROTEASE,
KEYWDS 4 SECRETED, ZYMOGEN
EXPDTA X-RAY DIFFRACTION
AUTHOR W.NIU,Z.CHEN,L.A.BUSH-PELC,A.BAH,P.S.GANDHI,E.DI CERA
REVDAT 6 06-SEP-23 3JZ1 1 REMARK
REVDAT 5 13-OCT-21 3JZ1 1 SEQADV HETSYN
REVDAT 4 29-JUL-20 3JZ1 1 COMPND REMARK HETNAM LINK
REVDAT 4 2 1 SITE
REVDAT 3 13-JUL-11 3JZ1 1 VERSN
REVDAT 2 12-JAN-10 3JZ1 1 JRNL
REVDAT 1 20-OCT-09 3JZ1 0
JRNL AUTH W.NIU,Z.CHEN,L.A.BUSH-PELC,A.BAH,P.S.GANDHI,E.DI CERA
JRNL TITL MUTANT N143P REVEALS HOW NA+ ACTIVATES THROMBIN
JRNL REF J.BIOL.CHEM. V. 284 36175 2009
JRNL REFN ISSN 0021-9258
JRNL PMID 19846563
JRNL DOI 10.1074/JBC.M109.069500
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.O.PINEDA,C.J.CARRELL,L.A.BUSH,S.PRASAD,S.CACCIA,Z.CHEN,
REMARK 1 AUTH 2 F.S.MATHEWS,E.DI CERA
REMARK 1 TITL MOLECULAR DISSECTION OF NA+ BINDING TO THROMBIN
REMARK 1 REF J.BIOL.CHEM. V. 279 31842 2004
REMARK 1 REFN ISSN 0021-9258
REMARK 1 PMID 15152000
REMARK 1 REFERENCE 2
REMARK 1 AUTH P.S.GANDHI,Z.CHEN,F.S.MATHEWS,E.DI CERA
REMARK 1 TITL STRUCTURAL IDENTIFICATION OF THE PATHWAY OF LONG-RANGE
REMARK 1 TITL 2 COMMUNICATION IN AN ALLOSTERIC ENZYME
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 105 1832 2009
REMARK 1 REFN ISSN 0027-8424
REMARK 1 PMID 18250335
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.2
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) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 26.57
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 343924.060
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.5
REMARK 3 NUMBER OF REFLECTIONS : 36289
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) : 0.203
REMARK 3 FREE R VALUE : 0.216
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1818
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
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) : 1.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.70
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 89.30
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 5370
REMARK 3 BIN R VALUE (WORKING SET) : 0.3580
REMARK 3 BIN FREE R VALUE : 0.3720
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.90
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 274
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 : 2238
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 30
REMARK 3 SOLVENT ATOMS : 214
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 18.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.40
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) : 0.20
REMARK 3 ESD FROM SIGMAA (A) : 0.35
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) : 0.22
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.35
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.800
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 25.50
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.130
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 : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 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 3JZ1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-SEP-09.
REMARK 100 THE DEPOSITION ID IS D_1000055338.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-DEC-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 14-BM-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9
REMARK 200 MONOCHROMATOR : BENT GE(111) MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36932
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 4.100
REMARK 200 R MERGE (I) : 0.06100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.66
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.30
REMARK 200 R MERGE FOR SHELL (I) : 0.32000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP FROM CCP4
REMARK 200 STARTING MODEL: PDB ENTRY 1SHH
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.49
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M NANO3 AND 20% PEG 3350, PH 6.8,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K
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 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 59.98950
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 23.83500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 59.98950
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 23.83500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8550 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23650 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -63.0 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 350 BIOMT1 2 -1.000000 0.000000 0.000000 -2.02536
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 50.64752
REMARK 350
REMARK 350 BIOMOLECULE: 2
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: 3090 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13010 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 N NO3 A 404 LIES ON A SPECIAL POSITION.
REMARK 375 O2 NO3 A 404 LIES ON A SPECIAL POSITION.
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 A -4
REMARK 465 PHE A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 GLY A 0
REMARK 465 ARG A 15
REMARK 465 ARG B 75
REMARK 465 TYR B 76
REMARK 465 GLU B 77
REMARK 465 ARG B 77A
REMARK 465 TRP B 148
REMARK 465 THR B 149
REMARK 465 ALA B 149A
REMARK 465 ASN B 149B
REMARK 465 VAL B 149C
REMARK 465 GLY B 149D
REMARK 465 LYS B 149E
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 TRP B 60D CB TRP B 60D CG -0.126
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 B 93 NE - CZ - NH1 ANGL. DEV. = -3.6 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 PHE A 7 -87.51 -129.90
REMARK 500 SER B 48 -179.25 -170.31
REMARK 500 TYR B 60A 82.67 -157.11
REMARK 500 PRO B 60C -3.12 -57.25
REMARK 500 ASN B 60G 76.59 -157.14
REMARK 500 ILE B 79 -11.22 65.50
REMARK 500 GLU B 97A -74.56 -104.81
REMARK 500 LYS B 145 -158.89 167.28
REMARK 500 GLU B 146 54.04 -118.61
REMARK 500 ASP B 186A -4.41 87.50
REMARK 500 GLU B 192 -112.65 45.89
REMARK 500 PHE B 245 -149.85 -109.47
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 NA A 402 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR A 14J O
REMARK 620 2 NO3 A 404 O1 81.6
REMARK 620 3 NO3 A 404 N 103.8 25.9
REMARK 620 4 NO3 A 404 O3 103.0 47.4 28.3
REMARK 620 5 HOH A1132 O 79.7 73.3 90.4 118.4
REMARK 620 6 TYR B 134 OH 93.3 174.9 158.2 134.6 106.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 401 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG B 221A O
REMARK 620 2 LYS B 224 O 95.1
REMARK 620 3 HOH B1119 O 87.2 97.3
REMARK 620 4 HOH B1124 O 160.7 73.3 79.2
REMARK 620 5 HOH B1131 O 102.2 162.4 80.6 89.1
REMARK 620 6 HOH B1138 O 101.1 80.2 171.5 92.2 99.4
REMARK 620 N 1 2 3 4 5
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1SHH RELATED DB: PDB
REMARK 900 SLOW FORM OF THROMBIN BOUND WITH PPACK
REMARK 900 RELATED ID: 3BEI RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE SLOW FORM OF THROMBIN IN A SELF-INHIBITED
REMARK 900 CONFORMATION
REMARK 900 RELATED ID: 3JZ2 RELATED DB: PDB
DBREF 3JZ1 A -4 15 UNP P00734 THRB_HUMAN 328 363
DBREF 3JZ1 B 16 247 UNP P00734 THRB_HUMAN 364 622
SEQADV 3JZ1 PRO B 143 UNP P00734 ASN 506 ENGINEERED MUTATION
SEQRES 1 A 36 THR PHE GLY SER GLY GLU ALA ASP CYS GLY LEU ARG PRO
SEQRES 2 A 36 LEU PHE GLU LYS LYS SER LEU GLU ASP LYS THR GLU ARG
SEQRES 3 A 36 GLU LEU LEU GLU SER TYR ILE ASP GLY ARG
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 PRO
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 ASP ARG ASP
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
MODRES 3JZ1 ASN B 60G ASN GLYCOSYLATION SITE
HET NA A 402 1
HET NO3 A 404 4
HET NAG B 301 14
HET NA B 401 1
HET NO3 B 403 4
HET GOL B 405 6
HETNAM NA SODIUM ION
HETNAM NO3 NITRATE ION
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM GOL GLYCEROL
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 NA 2(NA 1+)
FORMUL 4 NO3 2(N O3 1-)
FORMUL 5 NAG C8 H15 N O6
FORMUL 8 GOL C3 H8 O3
FORMUL 9 HOH *214(H2 O)
HELIX 1 1 PHE A 7 SER A 11 5 5
HELIX 2 2 THR A 14B ASP A 14L 1 11
HELIX 3 3 ALA B 55 CYS B 58 5 4
HELIX 4 4 PRO B 60B ASP B 60E 5 4
HELIX 5 5 THR B 60I ASN B 62 5 3
HELIX 6 6 ASP B 125 LEU B 130 1 9
HELIX 7 7 GLU B 164 SER B 171 1 8
HELIX 8 8 CYS B 191 SER B 195 5 5
HELIX 9 9 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 VAL B 138 O VAL B 158
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 LYS B 81 SER B 83 0
SHEET 2 B 7 LEU B 64 ILE B 68 -1 N ILE B 68 O LYS B 81
SHEET 3 B 7 GLN B 30 ARG B 35 -1 N PHE B 34 O LEU B 65
SHEET 4 B 7 GLU B 39 LEU B 46 -1 O LEU B 41 N LEU B 33
SHEET 5 B 7 TRP B 51 THR B 54 -1 O LEU B 53 N SER B 45
SHEET 6 B 7 ALA B 104 LEU B 108 -1 O MET B 106 N VAL B 52
SHEET 7 B 7 LEU B 85 ILE B 90 -1 N GLU B 86 O LYS B 107
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 2.04
SSBOND 2 CYS B 42 CYS B 58 1555 1555 2.03
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 C1 NAG B 301 1555 1555 1.47
LINK O TYR A 14J NA NA A 402 1555 1555 2.30
LINK NA NA A 402 O1 NO3 A 404 1555 1555 2.80
LINK NA NA A 402 N NO3 A 404 1555 1555 2.55
LINK NA NA A 402 O3 NO3 A 404 1555 1555 2.37
LINK NA NA A 402 O HOH A1132 1555 1555 2.38
LINK NA NA A 402 OH TYR B 134 1555 1555 2.35
LINK O ARG B 221A NA NA B 401 1555 1555 2.42
LINK O LYS B 224 NA NA B 401 1555 1555 2.30
LINK NA NA B 401 O HOH B1119 1555 1555 2.85
LINK NA NA B 401 O HOH B1124 1555 1555 2.37
LINK NA NA B 401 O HOH B1131 1555 1555 2.12
LINK NA NA B 401 O HOH B1138 1555 1555 2.37
CISPEP 1 SER B 36A PRO B 37 0 -3.19
CRYST1 119.979 47.670 50.688 90.00 92.29 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 0.008335 0.000000 0.000333 0.00000
SCALE2 0.000000 0.020978 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019744 0.00000
(ATOM LINES ARE NOT SHOWN.)
END