HEADER HYDROLASE/HYDROLASE INHIBITOR 09-JAN-12 3VEQ
TITLE A BINARY COMPLEX BETWWEN BOVINE PANCREATIC TRYPSIN AND A ENGINEERED
TITLE 2 MUTANT TRYPSIN INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CATIONIC TRYPSIN;
COMPND 3 CHAIN: B;
COMPND 4 SYNONYM: BETA-TRYPSIN, ALPHA-TRYPSIN CHAIN 1, ALPHA-TRYPSIN CHAIN 2;
COMPND 5 EC: 3.4.21.4;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: CHYMOTRYPSIN INHIBITOR 3;
COMPND 10 CHAIN: A;
COMPND 11 SYNONYM: WCI-3;
COMPND 12 ENGINEERED: YES;
COMPND 13 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: BOVINE;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21DE3;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET-28A;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: PSOPHOCARPUS TETRAGONOLOBUS;
SOURCE 12 ORGANISM_COMMON: GOA BEAN;
SOURCE 13 ORGANISM_TAXID: 3891;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 16 EXPRESSION_SYSTEM_STRAIN: BL21DE3;
SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR U.SEN,S.MAJUMDER,S.KHAMRUI,J.DASGUPTA
REVDAT 3 08-NOV-23 3VEQ 1 REMARK SEQADV LINK
REVDAT 2 08-MAY-13 3VEQ 1 JRNL
REVDAT 1 03-OCT-12 3VEQ 0
JRNL AUTH S.MAJUMDER,S.KHAMRUI,J.DASGUPTA,J.K.DATTAGUPTA,U.SEN
JRNL TITL ROLE OF REMOTE SCAFFOLDING RESIDUES IN THE INHIBITORY LOOP
JRNL TITL 2 PRE-ORGANIZATION, FLEXIBILITY, RIGIDIFICATION AND ENZYME
JRNL TITL 3 INHIBITION OF SERINE PROTEASE INHIBITORS
JRNL REF BIOCHIM.BIOPHYS.ACTA V.1824 882 2012
JRNL REFN ISSN 0006-3002
JRNL PMID 22709512
JRNL DOI 10.1016/J.BBAPAP.2012.04.009
REMARK 2
REMARK 2 RESOLUTION. 2.25 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.91
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1319403.810
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 90.8
REMARK 3 NUMBER OF REFLECTIONS : 14218
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) : 0.218
REMARK 3 FREE R VALUE : 0.274
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 712
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.010
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) : 2.25
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.39
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.20
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2339
REMARK 3 BIN R VALUE (WORKING SET) : 0.3190
REMARK 3 BIN FREE R VALUE : 0.3610
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.20
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 129
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.032
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2998
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 1
REMARK 3 SOLVENT ATOMS : 159
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 32.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 6.04000
REMARK 3 B22 (A**2) : -4.66000
REMARK 3 B33 (A**2) : -1.37000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -5.87000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.29
REMARK 3 ESD FROM SIGMAA (A) : 0.27
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) : 0.36
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.30
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 25.60
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) : 1.700 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.910 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.000 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.070 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.45
REMARK 3 BSOL : 63.14
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 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED
REMARK 4
REMARK 4 3VEQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-JAN-12.
REMARK 100 THE DEPOSITION ID IS D_1000069952.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-SEP-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
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 RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : AUTOMAR
REMARK 200 DATA SCALING SOFTWARE : AUTOMAR
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14218
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.250
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 (%) : 90.8
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) : 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: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 2QYI
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 34.37
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.87
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
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 61.49850
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 19.91300
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 61.49850
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 19.91300
REMARK 290 SMTRY3 4 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 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: 2330 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15840 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, A
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 LYS A 779
REMARK 465 SER A 780
REMARK 465 GLU A 781
REMARK 465 THR A 782
REMARK 465 ALA A 783
REMARK 465 SER A 784
REMARK 465 SER A 785
REMARK 465 HIS A 786
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 B 68 -71.39 -137.79
REMARK 500 ASN B 112 -158.41 -138.13
REMARK 500 SER B 145 100.86 -165.06
REMARK 500 ASP B 186 173.32 179.43
REMARK 500 SER B 192 145.48 -39.30
REMARK 500 SER B 207 -83.95 -110.23
REMARK 500 ALA B 213 20.06 47.48
REMARK 500 ASP A 605 -136.16 -121.09
REMARK 500 ASP A 606 -91.28 -101.63
REMARK 500 ALA A 610 40.97 -89.69
REMARK 500 GLU A 611 19.49 -156.45
REMARK 500 TRP A 628 20.55 -68.58
REMARK 500 ALA A 629 -153.40 -107.83
REMARK 500 HIS A 630 -95.65 53.50
REMARK 500 ASN A 641 40.81 -106.00
REMARK 500 PRO A 645 93.28 -56.87
REMARK 500 PRO A 673 150.19 -46.91
REMARK 500 SER A 687 -47.03 86.27
REMARK 500 LYS A 721 139.35 -170.63
REMARK 500 SER A 728 -9.38 73.44
REMARK 500 ASN A 729 -19.80 61.64
REMARK 500 ASP A 741 -85.67 -76.41
REMARK 500 GLU A 743 4.03 56.71
REMARK 500 ASP A 744 100.42 -165.40
REMARK 500 CYS A 747 55.43 -97.35
REMARK 500 ASP A 756 -169.52 -78.99
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 B 301 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 67 OE1
REMARK 620 2 ASN B 69 O 88.3
REMARK 620 3 VAL B 72 O 160.3 79.9
REMARK 620 4 GLU B 77 OE2 102.8 154.7 94.3
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2QYI RELATED DB: PDB
REMARK 900 RELATED ID: 3I29 RELATED DB: PDB
DBREF 3VEQ B 16 238 UNP P00760 TRY1_BOVIN 24 246
DBREF 3VEQ A 604 786 UNP P10822 ICW3_PSOTE 25 207
SEQADV 3VEQ VAL B 118 UNP P00760 ILE 126 ENGINEERED MUTATION
SEQADV 3VEQ ALA B 199 UNP P00760 SER 207 ENGINEERED MUTATION
SEQADV 3VEQ ARG A 668 UNP P10822 LEU 89 ENGINEERED MUTATION
SEQRES 1 B 223 ILE VAL GLY GLY TYR THR CYS GLY ALA ASN THR VAL PRO
SEQRES 2 B 223 TYR GLN VAL SER LEU ASN SER GLY TYR HIS PHE CYS GLY
SEQRES 3 B 223 GLY SER LEU ILE ASN SER GLN TRP VAL VAL SER ALA ALA
SEQRES 4 B 223 HIS CYS TYR LYS SER GLY ILE GLN VAL ARG LEU GLY GLU
SEQRES 5 B 223 ASP ASN ILE ASN VAL VAL GLU GLY ASN GLU GLN PHE ILE
SEQRES 6 B 223 SER ALA SER LYS SER ILE VAL HIS PRO SER TYR ASN SER
SEQRES 7 B 223 ASN THR LEU ASN ASN ASP ILE MET LEU ILE LYS LEU LYS
SEQRES 8 B 223 SER ALA ALA SER LEU ASN SER ARG VAL ALA SER VAL SER
SEQRES 9 B 223 LEU PRO THR SER CYS ALA SER ALA GLY THR GLN CYS LEU
SEQRES 10 B 223 ILE SER GLY TRP GLY ASN THR LYS SER SER GLY THR SER
SEQRES 11 B 223 TYR PRO ASP VAL LEU LYS CYS LEU LYS ALA PRO ILE LEU
SEQRES 12 B 223 SER ASP SER SER CYS LYS SER ALA TYR PRO GLY GLN ILE
SEQRES 13 B 223 THR SER ASN MET PHE CYS ALA GLY TYR LEU GLU GLY GLY
SEQRES 14 B 223 LYS ASP SER CYS GLN GLY ASP SER GLY GLY PRO VAL VAL
SEQRES 15 B 223 CYS ALA GLY LYS LEU GLN GLY ILE VAL SER TRP GLY SER
SEQRES 16 B 223 GLY CYS ALA GLN LYS ASN LYS PRO GLY VAL TYR THR LYS
SEQRES 17 B 223 VAL CYS ASN TYR VAL SER TRP ILE LYS GLN THR ILE ALA
SEQRES 18 B 223 SER ASN
SEQRES 1 A 183 ASP ASP ASP LEU VAL ASP ALA GLU GLY ASN LEU VAL GLU
SEQRES 2 A 183 ASN GLY GLY THR TYR TYR LEU LEU PRO HIS ILE TRP ALA
SEQRES 3 A 183 HIS GLY GLY GLY ILE GLU THR ALA LYS THR GLY ASN GLU
SEQRES 4 A 183 PRO CYS PRO LEU THR VAL VAL ARG SER PRO ASN GLU VAL
SEQRES 5 A 183 SER LYS GLY GLU PRO ILE ARG ILE SER SER GLN PHE ARG
SEQRES 6 A 183 SER LEU PHE ILE PRO ARG GLY SER LEU VAL ALA LEU GLY
SEQRES 7 A 183 PHE ALA ASN PRO PRO SER CYS ALA ALA SER PRO TRP TRP
SEQRES 8 A 183 THR VAL VAL ASP SER PRO GLN GLY PRO ALA VAL LYS LEU
SEQRES 9 A 183 SER GLN GLN LYS LEU PRO GLU LYS ASP ILE LEU VAL PHE
SEQRES 10 A 183 LYS PHE GLU LYS VAL SER HIS SER ASN ILE HIS VAL TYR
SEQRES 11 A 183 LYS LEU LEU TYR CYS GLN HIS ASP GLU GLU ASP VAL LYS
SEQRES 12 A 183 CYS ASP GLN TYR ILE GLY ILE HIS ARG ASP ARG ASN GLY
SEQRES 13 A 183 ASN ARG ARG LEU VAL VAL THR GLU GLU ASN PRO LEU GLU
SEQRES 14 A 183 LEU VAL LEU LEU LYS ALA LYS SER GLU THR ALA SER SER
SEQRES 15 A 183 HIS
HET CA B 301 1
HETNAM CA CALCIUM ION
FORMUL 3 CA CA 2+
FORMUL 4 HOH *159(H2 O)
HELIX 1 1 ALA B 53 TYR B 57 5 5
HELIX 2 2 SER B 159 TYR B 167 1 9
HELIX 3 3 TYR B 227 SER B 237 1 11
HELIX 4 4 PRO A 713 LEU A 718 1 6
SHEET 1 A 7 TYR B 20 THR B 21 0
SHEET 2 A 7 LYS B 151 PRO B 156 -1 O CYS B 152 N TYR B 20
SHEET 3 A 7 GLN B 130 GLY B 135 -1 N ILE B 133 O LEU B 153
SHEET 4 A 7 PRO B 195 CYS B 198 -1 O VAL B 197 N LEU B 132
SHEET 5 A 7 LYS B 201 TRP B 208 -1 O LYS B 201 N CYS B 198
SHEET 6 A 7 GLY B 219 LYS B 223 -1 O VAL B 220 N TRP B 208
SHEET 7 A 7 MET B 175 ALA B 178 -1 N PHE B 176 O TYR B 221
SHEET 1 B 7 GLN B 30 ASN B 34 0
SHEET 2 B 7 HIS B 38 LEU B 44 -1 O CYS B 40 N LEU B 33
SHEET 3 B 7 TRP B 49 SER B 52 -1 O VAL B 51 N SER B 43
SHEET 4 B 7 MET B 101 LEU B 105 -1 O ILE B 103 N VAL B 50
SHEET 5 B 7 GLN B 78 VAL B 87 -1 N ILE B 86 O LEU B 102
SHEET 6 B 7 GLN B 62 LEU B 65 -1 N VAL B 63 O ILE B 80
SHEET 7 B 7 GLN B 30 ASN B 34 -1 N ASN B 34 O GLN B 62
SHEET 1 C 6 ALA A 679 PHE A 682 0
SHEET 2 C 6 ILE A 661 SER A 664 -1 N ARG A 662 O GLY A 681
SHEET 3 C 6 GLY A 619 PRO A 625 -1 N TYR A 621 O ILE A 661
SHEET 4 C 6 GLU A 772 LYS A 777 -1 O LEU A 776 N TYR A 622
SHEET 5 C 6 TYR A 733 GLN A 739 -1 N TYR A 733 O LEU A 773
SHEET 6 C 6 PHE A 720 LYS A 724 -1 N GLU A 723 O LYS A 734
SHEET 1 D 7 ALA A 679 PHE A 682 0
SHEET 2 D 7 ILE A 661 SER A 664 -1 N ARG A 662 O GLY A 681
SHEET 3 D 7 GLY A 619 PRO A 625 -1 N TYR A 621 O ILE A 661
SHEET 4 D 7 GLU A 772 LYS A 777 -1 O LEU A 776 N TYR A 622
SHEET 5 D 7 TYR A 733 GLN A 739 -1 N TYR A 733 O LEU A 773
SHEET 6 D 7 LYS A 746 ARG A 755 -1 O GLN A 749 N TYR A 737
SHEET 7 D 7 ARG A 761 THR A 766 -1 O VAL A 764 N GLY A 752
SHEET 1 E 2 ILE A 634 ALA A 637 0
SHEET 2 E 2 THR A 647 ARG A 650 -1 O VAL A 649 N GLU A 635
SHEET 1 F 2 THR A 695 SER A 699 0
SHEET 2 F 2 GLY A 702 LYS A 706 -1 O GLY A 702 N SER A 699
SSBOND 1 CYS B 22 CYS B 152 1555 1555 2.03
SSBOND 2 CYS B 40 CYS B 56 1555 1555 2.04
SSBOND 3 CYS B 124 CYS B 225 1555 1555 2.04
SSBOND 4 CYS B 131 CYS B 198 1555 1555 2.03
SSBOND 5 CYS B 163 CYS B 177 1555 1555 2.03
SSBOND 6 CYS B 188 CYS B 212 1555 1555 2.03
SSBOND 7 CYS A 644 CYS A 688 1555 1555 2.03
SSBOND 8 CYS A 738 CYS A 747 1555 1555 2.03
LINK OE1 GLU B 67 CA CA B 301 1555 1555 2.33
LINK O ASN B 69 CA CA B 301 1555 1555 2.37
LINK O VAL B 72 CA CA B 301 1555 1555 2.30
LINK OE2 GLU B 77 CA CA B 301 1555 1555 2.23
SITE 1 AC1 4 GLU B 67 ASN B 69 VAL B 72 GLU B 77
CRYST1 122.997 39.826 76.783 90.00 119.65 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 0.008130 0.000000 0.004628 0.00000
SCALE2 0.000000 0.025109 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014986 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
