HEADER BLOOD CLOTTING 24-OCT-05 2BEH
TITLE CRYSTAL STRUCTURE OF ANTITHROMBIN VARIANT S137A/V317C/T401C WITH
TITLE 2 PLASMA LATENT ANTITHROMBIN
CAVEAT 2BEH NAG A 1 HAS WRONG CHIRALITY AT ATOM C1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ANTITHROMBIN-III;
COMPND 3 CHAIN: I;
COMPND 4 SYNONYM: ATIII;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: ANTITHROMBIN-III;
COMPND 9 CHAIN: L;
COMPND 10 SYNONYM: ATIII
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: SERPINC1, AT3;
SOURCE 6 EXPRESSION_SYSTEM: MESOCRICETUS AURATUS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: GOLDEN HAMSTER;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 10036;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: BHK;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606;
SOURCE 14 OTHER_DETAILS: FROM HUMAN PLASMA
KEYWDS ANTITHROMBIN DIMER, BLOOD CLOTTING
EXPDTA X-RAY DIFFRACTION
AUTHOR D.J.JOHNSON,S.A.LUIS,J.A.HUNTINGTON
REVDAT 6 20-OCT-21 2BEH 1 SEQADV HETSYN
REVDAT 5 29-JUL-20 2BEH 1 CAVEAT COMPND REMARK HET
REVDAT 5 2 1 HETNAM FORMUL LINK SITE
REVDAT 5 3 1 ATOM
REVDAT 4 13-JUL-11 2BEH 1 VERSN
REVDAT 3 16-MAR-10 2BEH 1 JRNL
REVDAT 2 24-FEB-09 2BEH 1 VERSN
REVDAT 1 01-NOV-05 2BEH 0
JRNL AUTH D.J.JOHNSON,J.LANGDOWN,W.LI,S.A.LUIS,T.P.BAGLIN,
JRNL AUTH 2 J.A.HUNTINGTON
JRNL TITL CRYSTAL STRUCTURE OF MONOMERIC NATIVE ANTITHROMBIN REVEALS A
JRNL TITL 2 NOVEL REACTIVE CENTER LOOP CONFORMATION.
JRNL REF J.BIOL.CHEM. V. 281 35478 2006
JRNL REFN ISSN 0021-9258
JRNL PMID 16973611
JRNL DOI 10.1074/JBC.M607204200
REMARK 2
REMARK 2 RESOLUTION. 2.70 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) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.10
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1029627.030
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 30199
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : R-FREE SET TAKEN FROM 1E04
REMARK 3 R VALUE (WORKING SET) : 0.219
REMARK 3 FREE R VALUE : 0.265
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1520
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.007
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) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.87
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.70
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4695
REMARK 3 BIN R VALUE (WORKING SET) : 0.3430
REMARK 3 BIN FREE R VALUE : 0.3710
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 245
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.024
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6231
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 129
REMARK 3 SOLVENT ATOMS : 17
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 63.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -6.73000
REMARK 3 B22 (A**2) : 19.51000
REMARK 3 B33 (A**2) : -12.78000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -10.46000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.36
REMARK 3 ESD FROM SIGMAA (A) : 0.44
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) : 0.45
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.46
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.500
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.80
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.860
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) : 1.520 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.670 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 11.720; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 14.170; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.30
REMARK 3 BSOL : 31.05
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : CARBOHYDRATE.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : GOL.PAR
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : CARBOHYDRATE.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : GOL.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2BEH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-OCT-05.
REMARK 100 THE DEPOSITION ID IS D_1000034998.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-APR-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SRS
REMARK 200 BEAMLINE : PX14.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.488
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30217
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 39.100
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
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) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.1
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: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.76
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.84
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, PH 7.4, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 293K
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 48.63700
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: CHAIN I IS THE ACTIVE MONOMER, AND L IS THE LATENT MONOMER.
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: 3970 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31880 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 14.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, L, 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 HIS I 1
REMARK 465 GLY I 2
REMARK 465 SER I 3
REMARK 465 ALA I 30
REMARK 465 THR I 31
REMARK 465 GLU I 32
REMARK 465 ASP I 33
REMARK 465 GLU I 34
REMARK 465 GLY I 35
REMARK 465 SER I 36
REMARK 465 GLU I 37
REMARK 465 GLN I 38
REMARK 465 LYS I 39
REMARK 465 ILE I 40
REMARK 465 GLU I 357
REMARK 465 GLY I 358
REMARK 465 ARG I 359
REMARK 465 ASP I 360
REMARK 465 LYS I 432
REMARK 465 HIS L 1
REMARK 465 GLY L 2
REMARK 465 SER L 3
REMARK 465 PRO L 4
REMARK 465 SER L 25
REMARK 465 PRO L 26
REMARK 465 GLU L 27
REMARK 465 LYS L 28
REMARK 465 LYS L 29
REMARK 465 ALA L 30
REMARK 465 THR L 31
REMARK 465 GLU L 32
REMARK 465 ASP L 33
REMARK 465 GLU L 34
REMARK 465 GLY L 35
REMARK 465 SER L 36
REMARK 465 GLU L 37
REMARK 465 GLN L 38
REMARK 465 LYS L 39
REMARK 465 ILE L 40
REMARK 465 PRO L 41
REMARK 465 GLU L 42
REMARK 465 LYS L 114
REMARK 465 ARG L 399
REMARK 465 VAL L 400
REMARK 465 THR L 401
REMARK 465 PHE L 402
REMARK 465 VAL L 431
REMARK 465 LYS L 432
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 MET I 17 CG SD CE
REMARK 470 ASN I 18 CG OD1 ND2
REMARK 470 MET I 20 CG SD CE
REMARK 470 LYS I 29 CG CD CE NZ
REMARK 470 GLU I 42 CG CD OE1 OE2
REMARK 470 ARG I 47 CD NE CZ NH1 NH2
REMARK 470 ASP I 117 CG OD1 OD2
REMARK 470 LYS I 125 CD CE NZ
REMARK 470 ARG I 132 CG CD NE CZ NH1 NH2
REMARK 470 LYS I 133 CD CE NZ
REMARK 470 LYS I 136 CG CD CE NZ
REMARK 470 LYS I 139 CG CD CE NZ
REMARK 470 LEU I 152 CG CD1 CD2
REMARK 470 LYS I 169 CE NZ
REMARK 470 LYS I 188 CG CD CE NZ
REMARK 470 LYS I 193 CD CE NZ
REMARK 470 ARG I 197 CD NE CZ NH1 NH2
REMARK 470 GLU I 205 CG CD OE1 OE2
REMARK 470 ARG I 235 CD NE CZ NH1 NH2
REMARK 470 GLU I 237 CD OE1 OE2
REMARK 470 LYS I 257 CE NZ
REMARK 470 LYS I 275 NZ
REMARK 470 LYS I 294 CD CE NZ
REMARK 470 ILE I 325 CD1
REMARK 470 LYS I 332 CE NZ
REMARK 470 GLU I 333 CG CD OE1 OE2
REMARK 470 LYS I 348 CE NZ
REMARK 470 ASP I 361 CG OD1 OD2
REMARK 470 GLU I 378 CD OE1 OE2
REMARK 470 GLU I 381 CG CD OE1 OE2
REMARK 470 LYS I 403 CD CE NZ
REMARK 470 LYS L 11 CG CD CE NZ
REMARK 470 ARG L 13 CG CD NE CZ NH1 NH2
REMARK 470 MET L 17 CG SD CE
REMARK 470 ILE L 22 CG2 CD1
REMARK 470 ARG L 24 CG CD NE CZ NH1 NH2
REMARK 470 ARG L 46 CG CD NE CZ NH1 NH2
REMARK 470 LYS L 53 CD CE NZ
REMARK 470 LYS L 107 CE NZ
REMARK 470 GLU L 113 CG CD OE1 OE2
REMARK 470 GLN L 118 CG CD OE1 NE2
REMARK 470 LYS L 125 CG CD CE NZ
REMARK 470 ARG L 129 CG CD NE CZ NH1 NH2
REMARK 470 ARG L 132 CG CD NE CZ NH1 NH2
REMARK 470 ASN L 135 CG OD1 ND2
REMARK 470 LYS L 136 CG CD CE NZ
REMARK 470 LYS L 139 CD CE NZ
REMARK 470 LYS L 150 CD CE NZ
REMARK 470 LYS L 169 CG CD CE NZ
REMARK 470 GLU L 177 CG CD OE1 OE2
REMARK 470 GLN L 181 CG CD OE1 NE2
REMARK 470 ARG L 183 CG CD NE CZ NH1 NH2
REMARK 470 LYS L 188 CG CD CE NZ
REMARK 470 ASP L 200 CG OD1 OD2
REMARK 470 GLU L 205 CG CD OE1 OE2
REMARK 470 GLU L 209 CG CD OE1 OE2
REMARK 470 LYS L 228 CG CD CE NZ
REMARK 470 GLU L 232 CG CD OE1 OE2
REMARK 470 ARG L 235 CG CD NE CZ NH1 NH2
REMARK 470 LYS L 236 CD CE NZ
REMARK 470 GLU L 245 CG CD OE1 OE2
REMARK 470 GLU L 255 CG CD OE1 OE2
REMARK 470 LYS L 257 CD CE NZ
REMARK 470 GLU L 265 CG CD OE1 OE2
REMARK 470 LYS L 287 CG CD CE NZ
REMARK 470 GLU L 289 CG CD OE1 OE2
REMARK 470 LYS L 290 CG CD CE NZ
REMARK 470 LYS L 294 CG CD CE NZ
REMARK 470 LYS L 297 CD CE NZ
REMARK 470 GLU L 298 CG CD OE1 OE2
REMARK 470 GLU L 306 CG CD OE1 OE2
REMARK 470 GLU L 333 CG CD OE1 OE2
REMARK 470 LYS L 348 CG CD CE NZ
REMARK 470 LYS L 350 CD CE NZ
REMARK 470 LYS L 370 CD CE NZ
REMARK 470 ASN L 396 CG OD1 ND2
REMARK 470 ASN L 398 CG OD1 ND2
REMARK 470 ARG L 406 CG CD NE CZ NH1 NH2
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 ALA I 43 N - CA - C ANGL. DEV. = -19.8 DEGREES
REMARK 500 CYS I 317 CA - CB - SG ANGL. DEV. = 9.9 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 VAL I 5 88.66 91.64
REMARK 500 ASP I 14 30.96 -90.10
REMARK 500 ASN I 18 72.58 76.72
REMARK 500 PRO I 19 173.11 -45.65
REMARK 500 MET I 20 -23.29 70.43
REMARK 500 PRO I 26 -177.60 -53.38
REMARK 500 GLU I 42 -151.57 -163.98
REMARK 500 ALA I 43 5.48 -176.44
REMARK 500 SER I 82 -75.73 -61.72
REMARK 500 ASN I 96 -137.00 39.49
REMARK 500 LYS I 107 7.47 59.00
REMARK 500 SER I 112 124.51 -32.80
REMARK 500 GLU I 113 13.79 45.34
REMARK 500 ARG I 132 -74.36 -105.00
REMARK 500 LYS I 133 1.12 -57.58
REMARK 500 LYS I 139 82.00 -65.18
REMARK 500 ALA I 143 64.63 -108.16
REMARK 500 ALA I 168 131.13 -178.07
REMARK 500 GLU I 177 -87.70 -90.73
REMARK 500 THR I 199 -107.47 -63.77
REMARK 500 VAL I 212 -69.18 -104.82
REMARK 500 ASP I 243 0.47 -62.55
REMARK 500 GLU I 245 -158.77 -88.63
REMARK 500 ARG I 261 125.01 179.09
REMARK 500 VAL I 263 -156.45 -100.89
REMARK 500 ASP I 277 -23.44 78.84
REMARK 500 GLU I 289 -78.32 -57.45
REMARK 500 LYS I 290 153.67 -48.23
REMARK 500 LYS I 332 -64.96 -20.70
REMARK 500 GLU I 347 -62.35 -94.33
REMARK 500 LEU I 351 59.38 -115.82
REMARK 500 GLU I 381 105.91 77.18
REMARK 500 ALA I 382 178.61 132.65
REMARK 500 ALA I 383 25.96 -174.93
REMARK 500 SER I 385 141.27 -32.45
REMARK 500 ARG I 399 146.51 -31.83
REMARK 500 ASN I 428 101.08 -164.71
REMARK 500 ALA L 10 176.47 -52.92
REMARK 500 PRO L 12 -74.27 -45.12
REMARK 500 PRO L 16 9.75 -64.58
REMARK 500 ASN L 18 99.78 -171.43
REMARK 500 MET L 20 -71.90 -53.35
REMARK 500 CYS L 21 -169.01 -70.35
REMARK 500 ASN L 45 -4.55 -50.15
REMARK 500 ASP L 72 -17.31 -42.17
REMARK 500 ASN L 96 -121.53 59.36
REMARK 500 SER L 112 -31.80 -13.55
REMARK 500 ILE L 119 -60.26 -29.73
REMARK 500 ARG L 129 4.37 -69.61
REMARK 500 LYS L 133 140.93 -176.11
REMARK 500
REMARK 500 THIS ENTRY HAS 73 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1T1F RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF NATIVE ANTITHROMBIN IN ITS MONOMERIC FORM
REMARK 900 RELATED ID: 1TB6 RELATED DB: PDB
REMARK 900 2.5A CRYSTAL STRUCTURE OF THE ANTITHROMBIN-THROMBIN-HEPARIN TERNARY
REMARK 900 COMPLEX
REMARK 900 RELATED ID: 2B5T RELATED DB: PDB
REMARK 900 2.1 ANGSTROM STRUCTURE OF A NONPRODUCTIVE COMPLEX BETWEEN
REMARK 900 ANTITHROMBIN, SYNTHETIC HEPARIN MIMETIC SR123781 AND TWO S195A
REMARK 900 THROMBIN MOLECULES
DBREF 2BEH I 1 432 UNP P01008 ANT3_HUMAN 33 464
DBREF 2BEH L 1 432 UNP P01008 ANT3_HUMAN 33 464
SEQADV 2BEH ALA I 137 UNP P01008 SER 169 ENGINEERED MUTATION
SEQADV 2BEH CYS I 317 UNP P01008 VAL 349 ENGINEERED MUTATION
SEQADV 2BEH CYS I 401 UNP P01008 THR 433 ENGINEERED MUTATION
SEQRES 1 I 432 HIS GLY SER PRO VAL ASP ILE CYS THR ALA LYS PRO ARG
SEQRES 2 I 432 ASP ILE PRO MET ASN PRO MET CYS ILE TYR ARG SER PRO
SEQRES 3 I 432 GLU LYS LYS ALA THR GLU ASP GLU GLY SER GLU GLN LYS
SEQRES 4 I 432 ILE PRO GLU ALA THR ASN ARG ARG VAL TRP GLU LEU SER
SEQRES 5 I 432 LYS ALA ASN SER ARG PHE ALA THR THR PHE TYR GLN HIS
SEQRES 6 I 432 LEU ALA ASP SER LYS ASN ASP ASN ASP ASN ILE PHE LEU
SEQRES 7 I 432 SER PRO LEU SER ILE SER THR ALA PHE ALA MET THR LYS
SEQRES 8 I 432 LEU GLY ALA CYS ASN ASP THR LEU GLN GLN LEU MET GLU
SEQRES 9 I 432 VAL PHE LYS PHE ASP THR ILE SER GLU LYS THR SER ASP
SEQRES 10 I 432 GLN ILE HIS PHE PHE PHE ALA LYS LEU ASN CYS ARG LEU
SEQRES 11 I 432 TYR ARG LYS ALA ASN LYS ALA SER LYS LEU VAL SER ALA
SEQRES 12 I 432 ASN ARG LEU PHE GLY ASP LYS SER LEU THR PHE ASN GLU
SEQRES 13 I 432 THR TYR GLN ASP ILE SER GLU LEU VAL TYR GLY ALA LYS
SEQRES 14 I 432 LEU GLN PRO LEU ASP PHE LYS GLU ASN ALA GLU GLN SER
SEQRES 15 I 432 ARG ALA ALA ILE ASN LYS TRP VAL SER ASN LYS THR GLU
SEQRES 16 I 432 GLY ARG ILE THR ASP VAL ILE PRO SER GLU ALA ILE ASN
SEQRES 17 I 432 GLU LEU THR VAL LEU VAL LEU VAL ASN THR ILE TYR PHE
SEQRES 18 I 432 LYS GLY LEU TRP LYS SER LYS PHE SER PRO GLU ASN THR
SEQRES 19 I 432 ARG LYS GLU LEU PHE TYR LYS ALA ASP GLY GLU SER CYS
SEQRES 20 I 432 SER ALA SER MET MET TYR GLN GLU GLY LYS PHE ARG TYR
SEQRES 21 I 432 ARG ARG VAL ALA GLU GLY THR GLN VAL LEU GLU LEU PRO
SEQRES 22 I 432 PHE LYS GLY ASP ASP ILE THR MET VAL LEU ILE LEU PRO
SEQRES 23 I 432 LYS PRO GLU LYS SER LEU ALA LYS VAL GLU LYS GLU LEU
SEQRES 24 I 432 THR PRO GLU VAL LEU GLN GLU TRP LEU ASP GLU LEU GLU
SEQRES 25 I 432 GLU MET MET LEU CYS VAL HIS MET PRO ARG PHE ARG ILE
SEQRES 26 I 432 GLU ASP GLY PHE SER LEU LYS GLU GLN LEU GLN ASP MET
SEQRES 27 I 432 GLY LEU VAL ASP LEU PHE SER PRO GLU LYS SER LYS LEU
SEQRES 28 I 432 PRO GLY ILE VAL ALA GLU GLY ARG ASP ASP LEU TYR VAL
SEQRES 29 I 432 SER ASP ALA PHE HIS LYS ALA PHE LEU GLU VAL ASN GLU
SEQRES 30 I 432 GLU GLY SER GLU ALA ALA ALA SER THR ALA VAL VAL ILE
SEQRES 31 I 432 ALA GLY ARG SER LEU ASN PRO ASN ARG VAL CYS PHE LYS
SEQRES 32 I 432 ALA ASN ARG PRO PHE LEU VAL PHE ILE ARG GLU VAL PRO
SEQRES 33 I 432 LEU ASN THR ILE ILE PHE MET GLY ARG VAL ALA ASN PRO
SEQRES 34 I 432 CYS VAL LYS
SEQRES 1 L 432 HIS GLY SER PRO VAL ASP ILE CYS THR ALA LYS PRO ARG
SEQRES 2 L 432 ASP ILE PRO MET ASN PRO MET CYS ILE TYR ARG SER PRO
SEQRES 3 L 432 GLU LYS LYS ALA THR GLU ASP GLU GLY SER GLU GLN LYS
SEQRES 4 L 432 ILE PRO GLU ALA THR ASN ARG ARG VAL TRP GLU LEU SER
SEQRES 5 L 432 LYS ALA ASN SER ARG PHE ALA THR THR PHE TYR GLN HIS
SEQRES 6 L 432 LEU ALA ASP SER LYS ASN ASP ASN ASP ASN ILE PHE LEU
SEQRES 7 L 432 SER PRO LEU SER ILE SER THR ALA PHE ALA MET THR LYS
SEQRES 8 L 432 LEU GLY ALA CYS ASN ASP THR LEU GLN GLN LEU MET GLU
SEQRES 9 L 432 VAL PHE LYS PHE ASP THR ILE SER GLU LYS THR SER ASP
SEQRES 10 L 432 GLN ILE HIS PHE PHE PHE ALA LYS LEU ASN CYS ARG LEU
SEQRES 11 L 432 TYR ARG LYS ALA ASN LYS SER SER LYS LEU VAL SER ALA
SEQRES 12 L 432 ASN ARG LEU PHE GLY ASP LYS SER LEU THR PHE ASN GLU
SEQRES 13 L 432 THR TYR GLN ASP ILE SER GLU LEU VAL TYR GLY ALA LYS
SEQRES 14 L 432 LEU GLN PRO LEU ASP PHE LYS GLU ASN ALA GLU GLN SER
SEQRES 15 L 432 ARG ALA ALA ILE ASN LYS TRP VAL SER ASN LYS THR GLU
SEQRES 16 L 432 GLY ARG ILE THR ASP VAL ILE PRO SER GLU ALA ILE ASN
SEQRES 17 L 432 GLU LEU THR VAL LEU VAL LEU VAL ASN THR ILE TYR PHE
SEQRES 18 L 432 LYS GLY LEU TRP LYS SER LYS PHE SER PRO GLU ASN THR
SEQRES 19 L 432 ARG LYS GLU LEU PHE TYR LYS ALA ASP GLY GLU SER CYS
SEQRES 20 L 432 SER ALA SER MET MET TYR GLN GLU GLY LYS PHE ARG TYR
SEQRES 21 L 432 ARG ARG VAL ALA GLU GLY THR GLN VAL LEU GLU LEU PRO
SEQRES 22 L 432 PHE LYS GLY ASP ASP ILE THR MET VAL LEU ILE LEU PRO
SEQRES 23 L 432 LYS PRO GLU LYS SER LEU ALA LYS VAL GLU LYS GLU LEU
SEQRES 24 L 432 THR PRO GLU VAL LEU GLN GLU TRP LEU ASP GLU LEU GLU
SEQRES 25 L 432 GLU MET MET LEU VAL VAL HIS MET PRO ARG PHE ARG ILE
SEQRES 26 L 432 GLU ASP GLY PHE SER LEU LYS GLU GLN LEU GLN ASP MET
SEQRES 27 L 432 GLY LEU VAL ASP LEU PHE SER PRO GLU LYS SER LYS LEU
SEQRES 28 L 432 PRO GLY ILE VAL ALA GLU GLY ARG ASP ASP LEU TYR VAL
SEQRES 29 L 432 SER ASP ALA PHE HIS LYS ALA PHE LEU GLU VAL ASN GLU
SEQRES 30 L 432 GLU GLY SER GLU ALA ALA ALA SER THR ALA VAL VAL ILE
SEQRES 31 L 432 ALA GLY ARG SER LEU ASN PRO ASN ARG VAL THR PHE LYS
SEQRES 32 L 432 ALA ASN ARG PRO PHE LEU VAL PHE ILE ARG GLU VAL PRO
SEQRES 33 L 432 LEU ASN THR ILE ILE PHE MET GLY ARG VAL ALA ASN PRO
SEQRES 34 L 432 CYS VAL LYS
MODRES 2BEH ASN I 96 ASN GLYCOSYLATION SITE
MODRES 2BEH ASN I 155 ASN GLYCOSYLATION SITE
MODRES 2BEH ASN I 192 ASN GLYCOSYLATION SITE
MODRES 2BEH ASN L 96 ASN GLYCOSYLATION SITE
MODRES 2BEH ASN L 155 ASN GLYCOSYLATION SITE
HET NAG A 1 14
HET NAG A 2 14
HET NAG B 1 14
HET NAG B 2 14
HET MAN B 3 11
HET NAG C 1 14
HET NAG C 2 14
HET NAG I 861 14
HET GOL I 901 6
HET NAG L 801 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
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 MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 NAG 8(C8 H15 N O6)
FORMUL 4 MAN C6 H12 O6
FORMUL 7 GOL C3 H8 O3
FORMUL 9 HOH *17(H2 O)
HELIX 1 1 LYS I 11 ILE I 15 5 5
HELIX 2 2 ASN I 45 LYS I 70 1 26
HELIX 3 3 SER I 79 LEU I 92 1 14
HELIX 4 4 CYS I 95 PHE I 106 1 12
HELIX 5 5 LYS I 107 ILE I 111 5 5
HELIX 6 6 THR I 115 ARG I 132 1 18
HELIX 7 7 ASN I 155 VAL I 165 1 11
HELIX 8 8 ASN I 178 THR I 194 1 17
HELIX 9 9 SER I 230 THR I 234 5 5
HELIX 10 10 ALA I 264 GLY I 266 5 3
HELIX 11 11 SER I 291 LEU I 299 1 9
HELIX 12 12 THR I 300 GLU I 310 1 11
HELIX 13 13 LEU I 331 MET I 338 1 8
HELIX 14 14 THR L 44 LYS L 70 1 27
HELIX 15 15 SER L 79 LEU L 92 1 14
HELIX 16 16 CYS L 95 PHE L 106 1 12
HELIX 17 17 LYS L 107 ILE L 111 5 5
HELIX 18 18 THR L 115 ARG L 132 1 18
HELIX 19 19 ASN L 155 TYR L 166 1 12
HELIX 20 20 ASN L 178 THR L 194 1 17
HELIX 21 21 SER L 230 THR L 234 5 5
HELIX 22 22 ALA L 264 GLY L 266 5 3
HELIX 23 23 SER L 291 GLU L 298 1 8
HELIX 24 24 THR L 300 LEU L 311 1 12
HELIX 25 25 LEU L 331 MET L 338 1 8
HELIX 26 26 VAL L 341 SER L 345 5 5
SHEET 1 A 7 ILE I 76 LEU I 78 0
SHEET 2 A 7 THR I 419 VAL I 426 -1 O ARG I 425 N ILE I 76
SHEET 3 A 7 PHE I 408 GLU I 414 -1 N VAL I 410 O GLY I 424
SHEET 4 A 7 ILE I 279 LEU I 285 -1 N ILE I 284 O LEU I 409
SHEET 5 A 7 GLN I 268 PRO I 273 -1 N GLN I 268 O LEU I 285
SHEET 6 A 7 SER I 246 ARG I 262 -1 N ARG I 259 O GLU I 271
SHEET 7 A 7 ARG I 235 TYR I 240 -1 N GLU I 237 O ALA I 249
SHEET 1 B 8 ILE I 76 LEU I 78 0
SHEET 2 B 8 THR I 419 VAL I 426 -1 O ARG I 425 N ILE I 76
SHEET 3 B 8 PHE I 408 GLU I 414 -1 N VAL I 410 O GLY I 424
SHEET 4 B 8 ILE I 279 LEU I 285 -1 N ILE I 284 O LEU I 409
SHEET 5 B 8 GLN I 268 PRO I 273 -1 N GLN I 268 O LEU I 285
SHEET 6 B 8 SER I 246 ARG I 262 -1 N ARG I 259 O GLU I 271
SHEET 7 B 8 GLU I 312 PRO I 321 -1 O MET I 314 N PHE I 258
SHEET 8 B 8 CYS I 401 LYS I 403 1 O PHE I 402 N CYS I 317
SHEET 1 C 5 GLN I 171 LEU I 173 0
SHEET 2 C 5 LYS I 139 ASP I 149 1 N LEU I 146 O GLN I 171
SHEET 3 C 5 LEU I 213 LEU I 224 -1 O VAL I 214 N PHE I 147
SHEET 4 C 5 VAL I 364 VAL I 375 1 O SER I 365 N LEU I 213
SHEET 5 C 5 PHE I 323 SER I 330 -1 N PHE I 329 O HIS I 369
SHEET 1 D 4 GLN I 171 LEU I 173 0
SHEET 2 D 4 LYS I 139 ASP I 149 1 N LEU I 146 O GLN I 171
SHEET 3 D 4 LEU I 213 LEU I 224 -1 O VAL I 214 N PHE I 147
SHEET 4 D 4 GLY I 379 SER I 380 -1 O SER I 380 N GLY I 223
SHEET 1 E 8 ALA I 387 ILE I 390 0
SHEET 2 E 8 GLU L 312 PRO L 321 1 O VAL L 317 N VAL I 389
SHEET 3 E 8 CYS L 247 ARG L 262 -1 N GLN L 254 O VAL L 318
SHEET 4 E 8 GLN L 268 PRO L 273 -1 O VAL L 269 N ARG L 261
SHEET 5 E 8 ILE L 279 LEU L 285 -1 O MET L 281 N LEU L 272
SHEET 6 E 8 PHE L 408 GLU L 414 -1 O PHE L 411 N VAL L 282
SHEET 7 E 8 THR L 419 VAL L 426 -1 O GLY L 424 N VAL L 410
SHEET 8 E 8 ILE L 76 LEU L 78 -1 N ILE L 76 O ARG L 425
SHEET 1 F 4 ALA I 387 ILE I 390 0
SHEET 2 F 4 GLU L 312 PRO L 321 1 O VAL L 317 N VAL I 389
SHEET 3 F 4 CYS L 247 ARG L 262 -1 N GLN L 254 O VAL L 318
SHEET 4 F 4 ARG L 235 PHE L 239 -1 N PHE L 239 O CYS L 247
SHEET 1 G 6 LYS L 169 LEU L 173 0
SHEET 2 G 6 LYS L 139 ASP L 149 1 N LEU L 146 O GLN L 171
SHEET 3 G 6 LEU L 213 LEU L 224 -1 O VAL L 216 N ARG L 145
SHEET 4 G 6 GLY L 379 ILE L 390 -1 O ALA L 382 N PHE L 221
SHEET 5 G 6 VAL L 364 VAL L 375 -1 N ASP L 366 O VAL L 389
SHEET 6 G 6 PHE L 323 SER L 330 -1 N PHE L 323 O VAL L 375
SHEET 1 H 2 THR L 153 PHE L 154 0
SHEET 2 H 2 VAL L 355 GLU L 357 -1 O GLU L 357 N THR L 153
SSBOND 1 CYS I 8 CYS I 128 1555 1555 2.04
SSBOND 2 CYS I 21 CYS I 95 1555 1555 2.03
SSBOND 3 CYS I 247 CYS I 430 1555 1555 2.04
SSBOND 4 CYS I 317 CYS I 401 1555 1555 2.05
SSBOND 5 CYS L 8 CYS L 128 1555 1555 2.03
SSBOND 6 CYS L 21 CYS L 95 1555 1555 2.03
SSBOND 7 CYS L 247 CYS L 430 1555 1555 2.04
LINK ND2 ASN I 96 C1 NAG A 1 1555 1555 1.45
LINK ND2 ASN I 155 C1 NAG B 1 1555 1555 1.45
LINK ND2 ASN I 192 C1 NAG I 861 1555 1555 1.45
LINK ND2 ASN L 96 C1 NAG L 801 1555 1555 1.44
LINK ND2 ASN L 155 C1 NAG C 1 1555 1555 1.45
LINK O4 NAG A 1 C1 NAG A 2 1555 1555 1.40
LINK O4 NAG B 1 C1 NAG B 2 1555 1555 1.39
LINK O4 NAG B 2 C1 MAN B 3 1555 1555 1.40
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.39
CRYST1 68.073 97.274 87.388 90.00 105.03 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 0.014690 0.000000 0.003944 0.00000
SCALE2 0.000000 0.010280 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011849 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
