HEADER BLOOD CLOTTING 09-MAR-00 1E05
TITLE PLASMA ALPHA ANTITHROMBIN-III
CAVEAT 1E05 GUP D 3 HAS WRONG CHIRALITY AT ATOM C5
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ANTITHROMBIN-III;
COMPND 3 CHAIN: I, L;
COMPND 4 SYNONYM: ATIII, SERPIN C1
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 OTHER_DETAILS: PLASMA ALPHA ANTITHROMBIN-III
KEYWDS BLOOD CLOTTING, SERPIN
EXPDTA X-RAY DIFFRACTION
AUTHOR A.J.MCCOY,R.SKINNER,J.-P.ABRAHAMS,X.Y.PEI,R.W.CARRELL
REVDAT 7 06-DEC-23 1E05 1 HETSYN
REVDAT 6 29-JUL-20 1E05 1 CAVEAT COMPND REMARK HETNAM
REVDAT 6 2 1 LINK SITE ATOM
REVDAT 5 09-NOV-11 1E05 1 COMPND REMARK HETSYN FORMUL
REVDAT 5 2 1 SITE VERSN
REVDAT 4 24-FEB-09 1E05 1 VERSN
REVDAT 3 14-JUN-01 1E05 1 SSBOND LINK ATOM TER
REVDAT 3 2 1 HETATM CONECT MASTER
REVDAT 2 21-JUL-00 1E05 1 REMARK
REVDAT 1 02-JUN-00 1E05 0
JRNL AUTH A.J.MCCOY,X.Y.PEI,R.SKINNER,J.-P.ABRAHAMS,R.W.CARRELL
JRNL TITL STRUCTURE OF BETA-ANTITHROMBIN AND THE EFFECT OF
JRNL TITL 2 GLYCOSYLATION ON ANTITHROMBIN'S HEPARIN AFFINITY AND
JRNL TITL 3 ACTIVITY.
JRNL REF J.MOL.BIOL. V. 326 823 2003
JRNL REFN ISSN 0022-2836
JRNL PMID 12581643
JRNL DOI 10.1016/S0022-2836(02)01382-7
REMARK 2
REMARK 2 RESOLUTION. 2.62 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.62
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 72.0
REMARK 3 NUMBER OF REFLECTIONS : NULL
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : SAME AS 2ANT
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.196
REMARK 3 FREE R VALUE : 0.256
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1248
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6535
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 298
REMARK 3 SOLVENT ATOMS : 70
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 53.00
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.371
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.298
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 14.454
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.007 ; 0.011
REMARK 3 ANGLE DISTANCE (A) : 0.023 ; 0.018
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : 0.016 ; 0.020
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : 0.028 ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : 0.190 ; 0.150
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : 0.146 ; 0.150
REMARK 3 MULTIPLE TORSION (A) : 0.193 ; 0.150
REMARK 3 H-BOND (X...Y) (A) : 0.123 ; 0.150
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : 4.400 ; 7.000
REMARK 3 STAGGERED (DEGREES) : 18.700; 15.000
REMARK 3 TRANSVERSE (DEGREES) : 24.800; 20.000
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 2.722 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 4.737 ; 5.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 4.596 ; 4.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 6.640 ; 6.000
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1E05 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 09-MAR-00.
REMARK 100 THE DEPOSITION ID IS D_1290004652.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SRS
REMARK 200 BEAMLINE : PX7.2
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 : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23397
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.620
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 72.0
REMARK 200 DATA REDUNDANCY : 1.800
REMARK 200 R MERGE (I) : 0.04800
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) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 2ANT
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.74
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALS GROWN IN MICROGRAVITY NASA
REMARK 280 SPACE SHUTTLE MISSION STS-67 20MG/ML LATENT ANTITHROMBIN-III IN
REMARK 280 20MM TRIS HCL PH 8.0 CRYSTALLIZED IN 19% PEG 4000, 50 MM NA/K
REMARK 280 PHOSPHATE PH 6.7, 0.05% AZIDE, PH 6.50
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 49.15500
REMARK 290 SMTRY3 2 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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, C, D
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, 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 400
REMARK 400 COMPOUND
REMARK 400 CHAIN I ADOPTS THE INHIBITORY CONFORMATION;
REMARK 400 CHAIN L ADOPTS THE LATENT CONFORMATION
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 PRO I 26
REMARK 465 GLU I 27
REMARK 465 LYS I 28
REMARK 465 LYS I 29
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 LYS I 432
REMARK 465 HIS L 1
REMARK 465 GLY L 2
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 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 LYS I 11 CE NZ
REMARK 470 ARG I 13 CD NE CZ NH1 NH2
REMARK 470 MET I 17 SD CE
REMARK 470 MET I 20 SD CE
REMARK 470 ILE I 22 CG1 CG2 CD1
REMARK 470 GLN I 38 CB CG CD OE1 NE2
REMARK 470 LYS I 39 CG CD CE NZ
REMARK 470 ILE I 40 CG1 CG2 CD1
REMARK 470 GLU I 42 CG CD OE1 OE2
REMARK 470 THR I 44 OG1 CG2
REMARK 470 GLU I 113 CG CD OE1 OE2
REMARK 470 LYS I 114 CG CD CE NZ
REMARK 470 GLN I 118 CG CD OE1 NE2
REMARK 470 LYS I 133 CG CD CE NZ
REMARK 470 LYS I 139 CD CE NZ
REMARK 470 GLU I 205 CG CD OE1 OE2
REMARK 470 GLU I 209 CG CD OE1 OE2
REMARK 470 ARG L 13 CD NE CZ NH1 NH2
REMARK 470 ASP L 14 CB CG OD1 OD2
REMARK 470 GLU L 42 CG CD OE1 OE2
REMARK 470 ARG L 46 CG CD NE CZ NH1 NH2
REMARK 470 LYS L 53 CG CD CE NZ
REMARK 470 LYS L 114 CG CD CE NZ
REMARK 470 ARG L 132 CG CD NE CZ NH1 NH2
REMARK 470 LYS L 136 CB CG CD CE NZ
REMARK 470 GLU L 245 CG CD OE1 OE2
REMARK 470 GLU L 289 CG CD OE1 OE2
REMARK 470 ASN L 396 CG OD1 ND2
REMARK 470 ASN L 398 CG OD1 ND2
REMARK 470 ARG L 399 CG CD NE CZ NH1 NH2
REMARK 470 PHE L 402 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS L 403 CD CE NZ
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 LEU I 351 CA - CB - CG ANGL. DEV. = 14.2 DEGREES
REMARK 500 ARG I 413 CD - NE - CZ ANGL. DEV. = 8.9 DEGREES
REMARK 500 MET L 17 CA - CB - CG ANGL. DEV. = 11.9 DEGREES
REMARK 500 ARG L 322 CD - NE - CZ ANGL. DEV. = 9.6 DEGREES
REMARK 500 ARG L 322 NE - CZ - NH1 ANGL. DEV. = 3.5 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 PRO I 4 -84.22 -76.90
REMARK 500 ALA I 10 106.84 -40.62
REMARK 500 ASN I 96 -136.75 46.81
REMARK 500 ILE I 111 -79.33 -80.05
REMARK 500 SER I 112 -9.25 -156.57
REMARK 500 GLU I 113 -11.93 97.44
REMARK 500 ALA I 134 -158.24 -170.05
REMARK 500 ASP I 200 57.73 -158.74
REMARK 500 GLN I 254 149.93 -173.41
REMARK 500 VAL I 263 -163.73 -112.62
REMARK 500 ALA I 264 116.15 -36.91
REMARK 500 ASP I 277 -8.22 76.74
REMARK 500 ALA I 382 120.86 -178.33
REMARK 500 PRO I 407 142.62 -34.10
REMARK 500 ALA L 10 154.83 -46.65
REMARK 500 ARG L 13 38.18 -84.74
REMARK 500 ASP L 14 -70.46 -121.46
REMARK 500 MET L 17 86.02 -68.95
REMARK 500 MET L 20 -72.50 -55.90
REMARK 500 ASN L 96 -131.20 55.67
REMARK 500 ARG L 132 59.16 -111.46
REMARK 500 LYS L 133 -45.41 -147.19
REMARK 500 LYS L 136 121.52 -23.30
REMARK 500 SER L 138 68.55 -158.22
REMARK 500 ASP L 200 47.61 -144.48
REMARK 500 ASN L 208 -167.66 -126.33
REMARK 500 GLU L 245 -147.99 -72.34
REMARK 500 VAL L 263 -151.49 -92.89
REMARK 500 ASP L 277 -3.30 70.12
REMARK 500 GLU L 357 32.68 83.44
REMARK 500 LEU L 395 -168.37 -109.88
REMARK 500 VAL L 400 70.99 -103.06
REMARK 500 ALA L 404 -148.45 -143.51
REMARK 500 ARG L 406 67.34 34.69
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 GLU I 113 -10.24
REMARK 500 TYR I 166 11.37
REMARK 500 LYS L 107 -12.29
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 MAN I 803
REMARK 610 MAN L 843
REMARK 610 MAN L 844
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1ANT RELATED DB: PDB
REMARK 900 RELATED ID: 1ATH RELATED DB: PDB
REMARK 900 RELATED ID: 2ANT RELATED DB: PDB
REMARK 900 RELATED ID: 1BR8 RELATED DB: PDB
REMARK 900 RELATED ID: 1DZG RELATED DB: PDB
REMARK 900 RELATED ID: 1DZH RELATED DB: PDB
REMARK 900 RELATED ID: 1E03 RELATED DB: PDB
REMARK 900 RELATED ID: 1E04 RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 ANT3_HUMAN RESIDUE NUMBERING IS FROM START
REMARK 999 OF ANTITHROMBIN-III LEADER SEQUENCE.
REMARK 999 STRUCTURE RESIDUE NUMBERING IS FROM START OF
REMARK 999 MATURE ANTITHROMBIN-III
REMARK 999
REMARK 999 RESIDUES NOT MODELLED HAD POOR ELECTRON DENSITY
DBREF 1E05 L 1 432 UNP P01008 ANT3_HUMAN 33 464
DBREF 1E05 I 1 432 UNP P01008 ANT3_HUMAN 33 464
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 SER 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 VAL 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 THR 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 1E05 ASN I 96 ASN GLYCOSYLATION SITE
MODRES 1E05 ASN I 135 ASN GLYCOSYLATION SITE
MODRES 1E05 ASN I 155 ASN GLYCOSYLATION SITE
MODRES 1E05 ASN I 192 ASN GLYCOSYLATION SITE
MODRES 1E05 ASN L 96 ASN GLYCOSYLATION SITE
MODRES 1E05 ASN L 135 ASN GLYCOSYLATION SITE
MODRES 1E05 ASN L 155 ASN GLYCOSYLATION SITE
MODRES 1E05 ASN L 192 ASN GLYCOSYLATION SITE
HET NAG A 1 14
HET NAG A 2 14
HET NAG B 1 14
HET NAG B 2 14
HET BMA B 3 11
HET NAG C 1 14
HET NAG C 2 14
HET NAG D 1 14
HET NAG D 2 14
HET GUP D 3 11
HET MAN D 4 11
HET NAG D 5 14
HET GAL D 6 11
HET MAN D 7 11
HET BMA D 8 11
HET MAN I 803 11
HET NAG I 821 14
HET NAG I 861 14
HET GOL I 901 6
HET PO4 L 501 5
HET NAG L 801 14
HET NAG L 821 14
HET MAN L 843 11
HET MAN L 844 11
HET GOL L 901 6
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM GUP ALPHA-L-GULOPYRANOSE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
HETNAM GAL BETA-D-GALACTOPYRANOSE
HETNAM GOL GLYCEROL
HETNAM PO4 PHOSPHATE ION
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 BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE
HETSYN GUP ALPHA-L-GULOSE; L-GULOSE; GULOSE; ALPHA-L-
HETSYN 2 GUP GULOPYRANOSIDE
HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE
HETSYN GAL BETA-D-GALACTOSE; D-GALACTOSE; GALACTOSE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 NAG 13(C8 H15 N O6)
FORMUL 4 BMA 2(C6 H12 O6)
FORMUL 6 GUP C6 H12 O6
FORMUL 6 MAN 5(C6 H12 O6)
FORMUL 6 GAL C6 H12 O6
FORMUL 10 GOL 2(C3 H8 O3)
FORMUL 11 PO4 O4 P 3-
FORMUL 17 HOH *70(H2 O)
HELIX 1 14 LYS I 11 ILE I 15 5 5
HELIX 2 15 ASN I 45 SER I 69 1 25
HELIX 3 16 SER I 79 LYS I 91 1 13
HELIX 4 17 LEU I 92 ALA I 94 5 3
HELIX 5 18 CYS I 95 PHE I 106 1 12
HELIX 6 19 LYS I 107 ILE I 111 5 5
HELIX 7 20 ASP I 117 TYR I 131 1 15
HELIX 8 21 ASN I 155 GLY I 167 1 13
HELIX 9 22 ASN I 178 LYS I 193 1 16
HELIX 10 23 SER I 230 THR I 234 5 5
HELIX 11 24 ALA I 264 GLY I 266 5 3
HELIX 12 25 SER I 291 LEU I 299 1 9
HELIX 13 26 THR I 300 LEU I 311 1 12
HELIX 14 27 LEU I 331 MET I 338 1 8
HELIX 15 28 VAL I 341 SER I 345 5 5
HELIX 16 1 GLU L 42 SER L 69 1 28
HELIX 17 2 SER L 79 LEU L 92 1 14
HELIX 18 3 CYS L 95 PHE L 106 1 12
HELIX 19 4 LYS L 107 ILE L 111 5 5
HELIX 20 5 ASP L 117 ARG L 132 1 16
HELIX 21 6 ASN L 155 GLY L 167 1 13
HELIX 22 7 ASN L 178 LYS L 193 1 16
HELIX 23 8 SER L 230 THR L 234 5 5
HELIX 24 9 ALA L 264 GLY L 266 5 3
HELIX 25 10 LEU L 292 GLU L 298 1 7
HELIX 26 11 THR L 300 LEU L 311 1 12
HELIX 27 12 LEU L 331 MET L 338 1 8
HELIX 28 13 VAL L 341 SER L 345 5 5
SHEET 1 A 7 ILE L 76 LEU L 78 0
SHEET 2 A 7 THR L 419 VAL L 426 -1 N ARG L 425 O ILE L 76
SHEET 3 A 7 PHE L 408 GLU L 414 -1 N GLU L 414 O THR L 419
SHEET 4 A 7 ILE L 279 LEU L 285 -1 N ILE L 284 O LEU L 409
SHEET 5 A 7 GLN L 268 PRO L 273 -1 N LEU L 272 O MET L 281
SHEET 6 A 7 SER L 250 ARG L 262 -1 N ARG L 261 O VAL L 269
SHEET 7 A 7 GLU L 312 ARG L 322 -1 N ARG L 322 O SER L 250
SHEET 1 B 6 LYS L 169 LEU L 173 0
SHEET 2 B 6 SER L 138 ASP L 149 1 N LEU L 146 O LYS L 169
SHEET 3 B 6 LEU L 213 LEU L 224 -1 N LYS L 222 O LYS L 139
SHEET 4 B 6 GLY L 379 ILE L 390 -1 N ILE L 390 O LEU L 213
SHEET 5 B 6 VAL L 364 VAL L 375 -1 N GLU L 374 O GLU L 381
SHEET 6 B 6 PHE L 323 SER L 330 -1 N PHE L 329 O HIS L 369
SHEET 1 C 2 ARG L 235 TYR L 240 0
SHEET 2 C 2 SER L 246 MET L 251 -1 N MET L 251 O ARG L 235
SHEET 1 D 6 ILE I 76 LEU I 78 0
SHEET 2 D 6 THR I 419 VAL I 426 -1 N ARG I 425 O ILE I 76
SHEET 3 D 6 PHE I 408 GLU I 414 -1 N GLU I 414 O THR I 419
SHEET 4 D 6 ILE I 279 LEU I 285 -1 N ILE I 284 O LEU I 409
SHEET 5 D 6 GLN I 268 PRO I 273 -1 N LEU I 272 O MET I 281
SHEET 6 D 6 ARG I 259 ARG I 262 -1 N ARG I 261 O VAL I 269
SHEET 1 E 5 LEU I 170 LEU I 173 0
SHEET 2 E 5 LYS I 139 ASP I 149 1 N LEU I 146 O GLN I 171
SHEET 3 E 5 LEU I 213 LYS I 222 -1 N LYS I 222 O LYS I 139
SHEET 4 E 5 ASP I 366 VAL I 375 1 N ASP I 366 O LEU I 215
SHEET 5 E 5 PHE I 323 SER I 330 -1 N PHE I 329 O HIS I 369
SHEET 1 F 2 LEU I 152 PHE I 154 0
SHEET 2 F 2 ILE I 354 ALA I 356 -1 N VAL I 355 O THR I 153
SHEET 1 G 4 ARG I 235 TYR I 240 0
SHEET 2 G 4 SER I 246 LYS I 257 -1 N MET I 251 O ARG I 235
SHEET 3 G 4 MET I 315 PRO I 321 -1 N MET I 320 O MET I 252
SHEET 4 G 4 VAL I 400 ALA I 404 1 N VAL I 400 O VAL I 317
SSBOND 1 CYS I 8 CYS I 128 1555 1555 2.03
SSBOND 2 CYS I 21 CYS I 95 1555 1555 2.02
SSBOND 3 CYS I 247 CYS I 430 1555 1555 2.03
SSBOND 4 CYS L 8 CYS L 128 1555 1555 2.03
SSBOND 5 CYS L 21 CYS L 95 1555 1555 2.03
SSBOND 6 CYS L 247 CYS L 430 1555 1555 2.02
LINK ND2 ASN I 96 C1 NAG A 1 1555 1555 1.38
LINK ND2 ASN I 135 C1 NAG I 821 1555 1555 1.38
LINK ND2 ASN I 155 C1 NAG B 1 1555 1555 1.40
LINK ND2 ASN I 192 C1 NAG I 861 1555 1555 1.31
LINK ND2 ASN L 96 C1 NAG L 801 1555 1555 1.35
LINK ND2 ASN L 135 C1 NAG L 821 1555 1555 1.36
LINK ND2 ASN L 155 C1 NAG C 1 1555 1555 1.39
LINK ND2 ASN L 192 C1 NAG D 1 1555 1555 1.39
LINK O4 NAG A 1 C1 NAG A 2 1555 1555 1.37
LINK O4 NAG B 1 C1 NAG B 2 1555 1555 1.40
LINK O4 NAG B 2 C1 BMA B 3 1555 1555 1.41
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.40
LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.42
LINK O4 NAG D 2 C1 GUP D 3 1555 1555 1.41
LINK O6 GUP D 3 C1 MAN D 4 1555 1555 1.40
LINK O3 GUP D 3 C1 MAN D 7 1555 1555 1.40
LINK O2 MAN D 4 C1 NAG D 5 1555 1555 1.38
LINK O4 NAG D 5 C1 GAL D 6 1555 1555 1.38
LINK O2 MAN D 7 C1 BMA D 8 1555 1555 1.41
CRYST1 61.410 98.310 90.410 90.00 103.32 90.00 P 1 21 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 0.016284 0.000000 0.003855 0.00000
SCALE2 0.000000 0.010172 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011366 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
