HEADER COMPLEX (SERINE PROTEASE/INHIBITOR) 15-JUL-98 3TGI
TITLE WILD-TYPE RAT ANIONIC TRYPSIN COMPLEXED WITH BOVINE
TITLE 2 PANCREATIC TRYPSIN INHIBITOR (BPTI)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRYPSIN;
COMPND 3 CHAIN: E;
COMPND 4 EC: 3.4.21.4;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: BOVINE PANCREATIC TRYPSIN INHIBITOR;
COMPND 7 CHAIN: I;
COMPND 8 SYNONYM: BPTI
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: NORWAY RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 ORGAN: PANCREATIC;
SOURCE 6 MOL_ID: 2;
SOURCE 7 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 8 ORGANISM_COMMON: CATTLE;
SOURCE 9 ORGANISM_TAXID: 9913
KEYWDS COMPLEX (SERINE PROTEASE/INHIBITOR)
EXPDTA X-RAY DIFFRACTION
AUTHOR A.PASTERNAK,D.RINGE,L.HEDSTROM
REVDAT 2 24-FEB-09 3TGI 1 VERSN
REVDAT 1 23-DEC-98 3TGI 0
JRNL AUTH A.PASTERNAK,D.RINGE,L.HEDSTROM
JRNL TITL COMPARISON OF ANIONIC AND CATIONIC TRYPSINOGENS:
JRNL TITL 2 THE ANIONIC ACTIVATION DOMAIN IS MORE FLEXIBLE IN
JRNL TITL 3 SOLUTION AND DIFFERS IN ITS MODE OF BPTI BINDING
JRNL TITL 4 IN THE CRYSTAL STRUCTURE
JRNL REF PROTEIN SCI. V. 8 253 1999
JRNL REFN ISSN 0961-8368
JRNL PMID 10210204
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 88.9
REMARK 3 NUMBER OF REFLECTIONS : 24932
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) : 0.177
REMARK 3 FREE R VALUE : 0.210
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 8
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.88
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2333
REMARK 3 BIN R VALUE (WORKING SET) : 0.2570
REMARK 3 BIN FREE R VALUE : 0.2730
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 283
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 : 2104
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 11
REMARK 3 SOLVENT ATOMS : 227
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.32
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 27.60
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.67
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 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 : CA.PAR
REMARK 3 PARAMETER FILE 3 : SO4.PAR
REMARK 3 PARAMETER FILE 4 : WATER.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 2 : CA.TOP
REMARK 3 TOPOLOGY FILE 3 : SO4.TOP
REMARK 3 TOPOLOGY FILE 4 : WATER.TOPH
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: ALSO TOPH19.PEP USED
REMARK 4
REMARK 4 3TGI COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 277
REMARK 200 PH : 8.5
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 RUH2R
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IIC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25741
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 88.9
REMARK 200 DATA REDUNDANCY : 2.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.86
REMARK 200 COMPLETENESS FOR SHELL (%) : 80.3
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: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER
REMARK 200 SOFTWARE USED: X-PLOR 3.851
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.32
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 4000 0.2 M LISO4 0.1 M TRIS
REMARK 280 PH 8.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 41.46000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 20.73000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 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 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 20.73000
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 41.46000
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1870 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11840 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -46.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, I
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY I 57
REMARK 465 ALA I 58
REMARK 465 ILE I 59
REMARK 465 GLY I 60
REMARK 465 PRO I 61
REMARK 465 TRP I 62
REMARK 465 GLU I 63
REMARK 465 ASN I 64
REMARK 465 LEU I 65
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 E 117 CG CD NE CZ NH1 NH2
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 E 578 O HOH E 578 5434 2.09
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 I 39 NE - CZ - NH2 ANGL. DEV. = 3.7 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 ASP E 49 -10.72 -48.09
REMARK 500 HIS E 71 -61.96 -137.39
REMARK 500 SER E 214 -69.10 -129.08
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 E 718 DISTANCE = 5.78 ANGSTROMS
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 CA E 800 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU E 70 OE1
REMARK 620 2 ASN E 72 O 88.4
REMARK 620 3 VAL E 75 O 160.9 84.6
REMARK 620 4 GLU E 80 OE2 104.4 162.9 86.5
REMARK 620 5 HOH E 526 O 80.5 105.9 84.4 87.6
REMARK 620 6 GLU E 77 OE1 94.8 86.5 102.4 81.2 166.5
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CAT
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: THE CATALYTIC TRIAD
REMARK 800 SITE_IDENTIFIER: P1
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: THE INHIBITOR RESIDUE IN THE PRIMARY
REMARK 800 SPECIFICITY SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA E 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 I 990
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 I 991
DBREF 3TGI E 16 245 UNP P00763 TRY2_RAT 24 246
DBREF 3TGI I 1 65 UNP P00974 BPT1_BOVIN 36 100
SEQRES 1 E 223 ILE VAL GLY GLY TYR THR CYS GLN GLU ASN SER VAL PRO
SEQRES 2 E 223 TYR GLN VAL SER LEU ASN SER GLY TYR HIS PHE CYS GLY
SEQRES 3 E 223 GLY SER LEU ILE ASN ASP GLN TRP VAL VAL SER ALA ALA
SEQRES 4 E 223 HIS CYS TYR LYS SER ARG ILE GLN VAL ARG LEU GLY GLU
SEQRES 5 E 223 HIS ASN ILE ASN VAL LEU GLU GLY ASN GLU GLN PHE VAL
SEQRES 6 E 223 ASN ALA ALA LYS ILE ILE LYS HIS PRO ASN PHE ASP ARG
SEQRES 7 E 223 LYS THR LEU ASN ASN ASP ILE MET LEU ILE LYS LEU SER
SEQRES 8 E 223 SER PRO VAL LYS LEU ASN ALA ARG VAL ALA THR VAL ALA
SEQRES 9 E 223 LEU PRO SER SER CYS ALA PRO ALA GLY THR GLN CYS LEU
SEQRES 10 E 223 ILE SER GLY TRP GLY ASN THR LEU SER SER GLY VAL ASN
SEQRES 11 E 223 GLU PRO ASP LEU LEU GLN CYS LEU ASP ALA PRO LEU LEU
SEQRES 12 E 223 PRO GLN ALA ASP CYS GLU ALA SER TYR PRO GLY LYS ILE
SEQRES 13 E 223 THR ASP ASN MET VAL CYS VAL GLY PHE LEU GLU GLY GLY
SEQRES 14 E 223 LYS ASP SER CYS GLN GLY ASP SER GLY GLY PRO VAL VAL
SEQRES 15 E 223 CYS ASN GLY GLU LEU GLN GLY ILE VAL SER TRP GLY TYR
SEQRES 16 E 223 GLY CYS ALA LEU PRO ASP ASN PRO GLY VAL TYR THR LYS
SEQRES 17 E 223 VAL CYS ASN TYR VAL ASP TRP ILE GLN ASP THR ILE ALA
SEQRES 18 E 223 ALA ASN
SEQRES 1 I 65 ARG PRO ASP PHE CYS LEU GLU PRO PRO TYR THR GLY PRO
SEQRES 2 I 65 CYS LYS ALA ARG ILE ILE ARG TYR PHE TYR ASN ALA LYS
SEQRES 3 I 65 ALA GLY LEU CYS GLN THR PHE VAL TYR GLY GLY CYS ARG
SEQRES 4 I 65 ALA LYS ARG ASN ASN PHE LYS SER ALA GLU ASP CYS MET
SEQRES 5 I 65 ARG THR CYS GLY GLY ALA ILE GLY PRO TRP GLU ASN LEU
HET CA E 800 1
HET SO4 I 990 5
HET SO4 I 991 5
HETNAM CA CALCIUM ION
HETNAM SO4 SULFATE ION
FORMUL 3 CA CA 2+
FORMUL 4 SO4 2(O4 S 2-)
FORMUL 6 HOH *227(H2 O)
HELIX 1 1 ALA E 56 CYS E 58 5 3
HELIX 2 2 GLN E 165 SER E 171 1 7
HELIX 3 3 VAL E 231 ASN E 233 5 3
HELIX 4 4 VAL E 235 ALA E 243 1 9
HELIX 5 5 ASP I 3 LEU I 6 5 4
HELIX 6 6 ALA I 48 THR I 54 1 7
SHEET 1 A 7 GLN E 81 ASN E 84 0
SHEET 2 A 7 GLN E 64 LEU E 68 -1 N LEU E 68 O GLN E 81
SHEET 3 A 7 GLN E 30 ASN E 34 -1 N ASN E 34 O GLN E 64
SHEET 4 A 7 HIS E 40 ASN E 48 -1 N GLY E 44 O VAL E 31
SHEET 5 A 7 TRP E 51 SER E 54 -1 N VAL E 53 O SER E 45
SHEET 6 A 7 MET E 104 LEU E 108 -1 N ILE E 106 O VAL E 52
SHEET 7 A 7 ALA E 85 LYS E 90 -1 N ILE E 89 O LEU E 105
SHEET 1 B 2 GLN E 135 GLY E 140 0
SHEET 2 B 2 GLN E 156 PRO E 161 -1 N ALA E 160 O CYS E 136
SHEET 1 C 4 MET E 180 VAL E 183 0
SHEET 2 C 4 GLY E 226 LYS E 230 -1 N TYR E 228 O VAL E 181
SHEET 3 C 4 GLU E 204 TRP E 215 -1 N TRP E 215 O VAL E 227
SHEET 4 C 4 PRO E 198 CYS E 201 -1 N CYS E 201 O GLU E 204
SHEET 1 D 2 ILE I 18 ASN I 24 0
SHEET 2 D 2 LEU I 29 TYR I 35 -1 N TYR I 35 O ILE I 18
SSBOND 1 CYS E 22 CYS E 157 1555 1555 2.03
SSBOND 2 CYS E 42 CYS E 58 1555 1555 2.04
SSBOND 3 CYS E 128 CYS E 232 1555 1555 2.03
SSBOND 4 CYS E 136 CYS E 201 1555 1555 2.03
SSBOND 5 CYS E 168 CYS E 182 1555 1555 2.03
SSBOND 6 CYS E 191 CYS E 220 1555 1555 2.17
SSBOND 7 CYS I 5 CYS I 55 1555 1555 2.03
SSBOND 8 CYS I 14 CYS I 38 1555 1555 2.09
SSBOND 9 CYS I 30 CYS I 51 1555 1555 2.03
LINK CA CA E 800 OE1 GLU E 70 1555 1555 2.32
LINK CA CA E 800 O ASN E 72 1555 1555 2.34
LINK CA CA E 800 O VAL E 75 1555 1555 2.32
LINK CA CA E 800 OE2 GLU E 80 1555 1555 2.23
LINK CA CA E 800 O HOH E 526 1555 1555 2.49
LINK CA CA E 800 OE1 GLU E 77 1555 1555 2.45
SITE 1 CAT 3 HIS E 57 ASP E 102 SER E 195
SITE 1 P1 1 LYS I 15
SITE 1 AC1 6 GLU E 70 ASN E 72 VAL E 75 GLU E 77
SITE 2 AC1 6 GLU E 80 HOH E 526
SITE 1 AC2 4 ARG I 42 HOH I 529 HOH I 664 HOH I 691
SITE 1 AC3 4 ARG I 20 TYR I 35 HOH I 687 HOH I 705
CRYST1 92.720 92.720 62.190 90.00 90.00 120.00 P 32 2 1 6
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 0.010785 0.006227 0.000000 0.00000
SCALE2 0.000000 0.012454 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016080 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
