HEADER HYDROLASE/HYDROLASE INHIBITOR 05-NOV-98 1BZX
TITLE THE CRYSTAL STRUCTURE OF ANIONIC SALMON TRYPSIN IN COMPLEX WITH BOVINE
TITLE 2 PANCREATIC TRYPSIN INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (TRYPSIN);
COMPND 3 CHAIN: E;
COMPND 4 EC: 3.4.21.4;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: PROTEIN (BOVINE PANCREATIC TRYPSIN INHIBITOR);
COMPND 7 CHAIN: I
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SALMO SALAR;
SOURCE 3 ORGANISM_COMMON: ATLANTIC SALMON;
SOURCE 4 ORGANISM_TAXID: 8030;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 7 ORGANISM_COMMON: CATTLE;
SOURCE 8 ORGANISM_TAXID: 9913
KEYWDS TRYPSIN, SERINE PROTEINASES, COLD ADAPTATION, INHIBITOR, SUBSTRATE
KEYWDS 2 SPECIFICITY, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR R.HELLAND,I.LEIROS,G.I.BERGLUND,N.P.WILLASSEN,A.O.SMALAS
REVDAT 4 09-AUG-23 1BZX 1 REMARK SEQADV LINK
REVDAT 3 24-FEB-09 1BZX 1 VERSN
REVDAT 2 29-DEC-99 1BZX 4 HEADER COMPND REMARK JRNL
REVDAT 2 2 4 ATOM SOURCE SEQRES
REVDAT 1 11-NOV-98 1BZX 0
JRNL AUTH R.HELLAND,I.LEIROS,G.I.BERGLUND,N.P.WILLASSEN,A.O.SMALAS
JRNL TITL THE CRYSTAL STRUCTURE OF ANIONIC SALMON TRYPSIN IN COMPLEX
JRNL TITL 2 WITH BOVINE PANCREATIC TRYPSIN INHIBITOR.
JRNL REF EUR.J.BIOCHEM. V. 256 317 1998
JRNL REFN ISSN 0014-2956
JRNL PMID 9760170
JRNL DOI 10.1046/J.1432-1327.1998.2560317.X
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.8
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 97.3
REMARK 3 NUMBER OF REFLECTIONS : 25273
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) : 0.206
REMARK 3 FREE R VALUE : 0.238
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) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.19
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2107
REMARK 3 BIN R VALUE (WORKING SET) : 0.3600
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
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 : 2120
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 1
REMARK 3 SOLVENT ATOMS : 85
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 33.99
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.29
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) : 0.22
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) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.743
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
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 : PARHCSDX.PRO
REMARK 3 PARAMETER FILE 2 : PARAM19.SOL
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 2 : TOPH19.SOL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1BZX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB.
REMARK 100 THE DEPOSITION ID IS D_1000008349.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 293
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : BM1A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.873
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, CCP4
REMARK 200 DATA SCALING SOFTWARE : CCP4
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25996
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 15.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.3
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : 0.08300
REMARK 200 R SYM (I) : 0.07700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.37
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.5
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : 0.34000
REMARK 200 R SYM FOR SHELL (I) : 0.29300
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: PDB ENTRY 2PTC, PDB ENTRY 2TBS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.73
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES PH 7.5, 0.8-1.2 M
REMARK 280 POTASSIUM SODIUM TARTRATE
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
REMARK 290 7555 Y,X,-Z+1/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+2/3
REMARK 290 10555 -Y,-X,-Z+5/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/6
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 74.05000
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 148.10000
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 111.07500
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 185.12500
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 37.02500
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 74.05000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 148.10000
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 185.12500
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 111.07500
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 37.02500
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: 1410 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12260 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 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 475
REMARK 475 ZERO OCCUPANCY RESIDUES
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)
REMARK 475 M RES C SSEQI
REMARK 475 ALA E 243
REMARK 475 SER E 244
REMARK 475 TYR E 245
REMARK 475 GLY I 557
REMARK 475 ALA I 558
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 LYS E 23 CG CD CE NZ
REMARK 480 GLU E 49 CG CD OE1 OE2
REMARK 480 ARG E 62 CB CG CD NE CZ NH1 NH2
REMARK 480 TYR E 97 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 480 LYS E 107 CD CE NZ
REMARK 480 LYS E 110 CG CD CE NZ
REMARK 480 THR E 116 OG1 CG2
REMARK 480 ASP E 236 CG OD1 OD2
REMARK 480 ASP I 503 CG OD1 OD2
REMARK 480 LYS I 526 CG CD CE NZ
REMARK 480 LYS I 546 CE NZ
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 LYS I 515 C ALA I 516 N -0.140
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 SER E 37 45.36 -151.35
REMARK 500 HIS E 71 -64.76 -132.67
REMARK 500 ASN E 115 -160.46 -162.97
REMARK 500 SER E 214 -72.60 -122.34
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 CA E 700 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU E 70 OE1
REMARK 620 2 ASN E 72 O 95.6
REMARK 620 3 VAL E 75 O 146.4 75.5
REMARK 620 4 GLU E 77 OE1 105.1 95.5 108.0
REMARK 620 5 GLU E 80 OE1 86.8 173.9 99.4 89.1
REMARK 620 6 HOH E 773 O 58.8 89.2 88.3 163.7 87.3
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA E 700
DBREF 1BZX E 16 245 UNP P35031 TRY1_SALSA 21 242
DBREF 1BZX I 501 558 UNP P00974 BPT1_BOVIN 36 93
SEQADV 1BZX PRO E 24 UNP P35031 ALA 29 CONFLICT
SEQADV 1BZX PRO E 28 UNP P35031 THR 33 CONFLICT
SEQRES 1 E 222 ILE VAL GLY GLY TYR GLU CYS LYS PRO TYR SER GLN PRO
SEQRES 2 E 222 HIS GLN VAL SER LEU ASN SER GLY TYR HIS PHE CYS GLY
SEQRES 3 E 222 GLY SER LEU VAL ASN GLU ASN TRP VAL VAL SER ALA ALA
SEQRES 4 E 222 HIS CYS TYR LYS SER ARG VAL GLU VAL ARG LEU GLY GLU
SEQRES 5 E 222 HIS ASN ILE LYS VAL THR GLU GLY SER GLU GLN PHE ILE
SEQRES 6 E 222 SER SER SER ARG VAL ILE ARG HIS PRO ASN TYR SER SER
SEQRES 7 E 222 TYR ASN ILE ASP ASN ASP ILE MET LEU ILE LYS LEU SER
SEQRES 8 E 222 LYS PRO ALA THR LEU ASN THR TYR VAL GLN PRO VAL ALA
SEQRES 9 E 222 LEU PRO THR SER CYS ALA PRO ALA GLY THR MET CYS THR
SEQRES 10 E 222 VAL SER GLY TRP GLY ASN THR MET SER SER THR ALA ASP
SEQRES 11 E 222 SER ASN LYS LEU GLN CYS LEU ASN ILE PRO ILE LEU SER
SEQRES 12 E 222 TYR SER ASP CYS ASN ASN SER TYR PRO GLY MET ILE THR
SEQRES 13 E 222 ASN ALA MET PHE CYS ALA GLY TYR LEU GLU GLY GLY LYS
SEQRES 14 E 222 ASP SER CYS GLN GLY ASP SER GLY GLY PRO VAL VAL CYS
SEQRES 15 E 222 ASN GLY GLU LEU GLN GLY VAL VAL SER TRP GLY TYR GLY
SEQRES 16 E 222 CYS ALA GLU PRO GLY ASN PRO GLY VAL TYR ALA LYS VAL
SEQRES 17 E 222 CYS ILE PHE ASN ASP TRP LEU THR SER THR MET ALA SER
SEQRES 18 E 222 TYR
SEQRES 1 I 58 ARG PRO ASP PHE CYS LEU GLU PRO PRO TYR THR GLY PRO
SEQRES 2 I 58 CYS LYS ALA ARG ILE ILE ARG TYR PHE TYR ASN ALA LYS
SEQRES 3 I 58 ALA GLY LEU CYS GLN THR PHE VAL TYR GLY GLY CYS ARG
SEQRES 4 I 58 ALA LYS ARG ASN ASN PHE LYS SER ALA GLU ASP CYS MET
SEQRES 5 I 58 ARG THR CYS GLY GLY ALA
HET CA E 700 1
HETNAM CA CALCIUM ION
FORMUL 3 CA CA 2+
FORMUL 4 HOH *85(H2 O)
HELIX 1 1 ALA E 56 CYS E 58 5 3
HELIX 2 2 TYR E 165 SER E 171 1 7
HELIX 3 3 VAL E 231 ILE E 233 5 3
HELIX 4 4 ASN E 235 ALA E 243 1 9
HELIX 5 5 ASP I 503 LEU I 506 5 4
HELIX 6 6 ALA I 548 CYS I 555 1 8
SHEET 1 A 7 GLN E 81 SER E 84 0
SHEET 2 A 7 GLU E 64 LEU E 67 -1 N LEU E 67 O GLN E 81
SHEET 3 A 7 GLN E 30 ASN E 34 -1 N ASN E 34 O GLU 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 SER E 85 ARG E 90 -1 N ILE E 89 O LEU E 105
SHEET 1 B 2 MET E 135 GLY E 140 0
SHEET 2 B 2 GLN E 156 PRO E 161 -1 N ILE E 160 O CYS E 136
SHEET 1 C 4 MET E 180 ALA E 183 0
SHEET 2 C 4 GLY E 226 LYS E 230 -1 N TYR E 228 O PHE 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 518 ASN I 524 0
SHEET 2 D 2 LEU I 529 TYR I 535 -1 N TYR I 535 O ILE I 518
SSBOND 1 CYS E 22 CYS E 157 1555 1555 2.03
SSBOND 2 CYS E 42 CYS E 58 1555 1555 2.02
SSBOND 3 CYS E 128 CYS E 232 1555 1555 2.02
SSBOND 4 CYS E 136 CYS E 201 1555 1555 2.03
SSBOND 5 CYS E 168 CYS E 182 1555 1555 2.04
SSBOND 6 CYS E 191 CYS E 220 1555 1555 2.02
SSBOND 7 CYS I 505 CYS I 555 1555 1555 2.02
SSBOND 8 CYS I 514 CYS I 538 1555 1555 2.02
SSBOND 9 CYS I 530 CYS I 551 1555 1555 2.05
LINK OE1 GLU E 70 CA CA E 700 1555 1555 2.48
LINK O ASN E 72 CA CA E 700 1555 1555 2.62
LINK O VAL E 75 CA CA E 700 1555 1555 2.39
LINK OE1 GLU E 77 CA CA E 700 1555 1555 2.67
LINK OE1 GLU E 80 CA CA E 700 1555 1555 2.58
LINK CA CA E 700 O HOH E 773 1555 1555 3.21
SITE 1 AC1 5 GLU E 70 ASN E 72 VAL E 75 GLU E 77
SITE 2 AC1 5 GLU E 80
CRYST1 84.120 84.120 222.150 90.00 90.00 120.00 P 61 2 2 12
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 0.011888 0.006863 0.000000 0.00000
SCALE2 0.000000 0.013727 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004501 0.00000
(ATOM LINES ARE NOT SHOWN.)
END