HEADER HYDROLASE 14-MAY-16 5JYI
TITLE TRYPSIN BOUND WITH SUCCINIC ACID AT 1.9A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CATIONIC TRYPSIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: BETA-TRYPSIN;
COMPND 5 EC: 3.4.21.4
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: BOVINE;
SOURCE 4 ORGANISM_TAXID: 9913
KEYWDS SUCCINIC ACID, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.MANOHAR,N.H.V.KUTUMBARAO,L.KARTHIK,P.MALATHY,D.VELMURUGAN,
AUTHOR 2 K.GUNASEKARAN
REVDAT 2 08-NOV-23 5JYI 1 REMARK LINK
REVDAT 1 06-JUL-16 5JYI 0
JRNL AUTH R.MANOHAR,N.H.V.KUTUMBARAO,L.KARTHIK,P.MALATHY,D.VELMURUGAN,
JRNL AUTH 2 K.GUNASEKARAN
JRNL TITL TRYPSIN BOUND WITH SUCCINIC ACID AT 1.9A
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.91 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8.4_1496
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.91
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.41
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 15134
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.158
REMARK 3 R VALUE (WORKING SET) : 0.153
REMARK 3 FREE R VALUE : 0.201
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1514
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 38.4127 - 4.2550 1.00 1339 149 0.1671 0.1810
REMARK 3 2 4.2550 - 3.3780 1.00 1268 141 0.1380 0.1807
REMARK 3 3 3.3780 - 2.9511 1.00 1257 140 0.1557 0.2127
REMARK 3 4 2.9511 - 2.6814 1.00 1236 138 0.1720 0.2444
REMARK 3 5 2.6814 - 2.4892 1.00 1242 138 0.1635 0.2026
REMARK 3 6 2.4892 - 2.3425 1.00 1234 136 0.1553 0.2104
REMARK 3 7 2.3425 - 2.2252 1.00 1206 134 0.1524 0.1998
REMARK 3 8 2.2252 - 2.1283 1.00 1233 137 0.1434 0.1970
REMARK 3 9 2.1283 - 2.0464 1.00 1219 136 0.1410 0.1894
REMARK 3 10 2.0464 - 1.9758 1.00 1225 137 0.1383 0.2233
REMARK 3 11 1.9758 - 1.9140 0.96 1161 128 0.1384 0.2070
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.150
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.620
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.008 1634
REMARK 3 ANGLE : 1.164 2208
REMARK 3 CHIRALITY : 0.052 252
REMARK 3 PLANARITY : 0.005 285
REMARK 3 DIHEDRAL : 11.977 568
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5JYI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-MAY-16.
REMARK 100 THE DEPOSITION ID IS D_1000221423.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-AUG-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.8-6.5
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 : BRUKER AXS MICROSTAR
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : COPPER K-ALPHA
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15134
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 39.660
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 2.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.0000
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: PHENIX
REMARK 200 STARTING MODEL: 4I8H
REMARK 200
REMARK 200 REMARK: RECTANGULAR SHAPE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 32.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M SUCCINIC ACID,0.1M SODIUM ACETATE
REMARK 280 PH 5.8,15%(W/V) PEG3350, PH 5.5, EVAPORATION, TEMPERATURE 298.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 23.16000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 38.40500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 26.59000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 38.40500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 23.16000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 26.59000
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 130 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 8960 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 MET A -7
REMARK 465 LYS A -6
REMARK 465 THR A -5
REMARK 465 PHE A -4
REMARK 465 ILE A -3
REMARK 465 PHE A -2
REMARK 465 LEU A -1
REMARK 465 ALA A 0
REMARK 465 LEU A 1
REMARK 465 LEU A 2
REMARK 465 GLY A 3
REMARK 465 ALA A 4
REMARK 465 ALA A 5
REMARK 465 VAL A 6
REMARK 465 ALA A 7
REMARK 465 PHE A 8
REMARK 465 PRO A 9
REMARK 465 VAL A 10
REMARK 465 ASP A 11
REMARK 465 ASP A 12
REMARK 465 ASP A 13
REMARK 465 ASP A 14
REMARK 465 LYS A 15
REMARK 465 SER A 146
REMARK 465 SER A 147
REMARK 465 GLY A 148
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 TYR A 39 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 SER A 96 OG
REMARK 470 LYS A 109 CG CD CE NZ
REMARK 470 LYS A 145 CG CD CE NZ
REMARK 470 THR A 149 OG1 CG2
REMARK 470 SER A 178 OG
REMARK 470 PHE A 181 CG CD1 CD2 CE1 CE2 CZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 512 O HOH A 533 1.76
REMARK 500 OE1 GLN A 240 O HOH A 401 1.81
REMARK 500 O HOH A 612 O HOH A 637 1.82
REMARK 500 O SER A 150 O HOH A 402 1.92
REMARK 500 O HOH A 621 O HOH A 668 1.95
REMARK 500 O HOH A 509 O HOH A 539 2.02
REMARK 500 O HOH A 590 O HOH A 647 2.02
REMARK 500 ND2 ASN A 74 OD1 ASP A 153 2.09
REMARK 500 O HOH A 549 O HOH A 659 2.11
REMARK 500 O HOH A 554 O HOH A 644 2.13
REMARK 500 O HOH A 430 O HOH A 699 2.13
REMARK 500 NZ LYS A 156 O HOH A 403 2.14
REMARK 500 O HOH A 411 O HOH A 644 2.18
REMARK 500
REMARK 500 REMARK: NULL
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 A 419 O HOH A 636 3444 2.05
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 A 71 -64.67 -128.50
REMARK 500 ASN A 115 -154.37 -148.10
REMARK 500 SER A 195 135.87 -36.70
REMARK 500 SER A 214 -65.60 -121.24
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 A 736 DISTANCE = 5.87 ANGSTROMS
REMARK 525 HOH A 737 DISTANCE = 6.04 ANGSTROMS
REMARK 525 HOH A 738 DISTANCE = 6.10 ANGSTROMS
REMARK 525 HOH A 739 DISTANCE = 6.11 ANGSTROMS
REMARK 525 HOH A 740 DISTANCE = 6.21 ANGSTROMS
REMARK 525 HOH A 741 DISTANCE = 6.24 ANGSTROMS
REMARK 525 HOH A 742 DISTANCE = 6.84 ANGSTROMS
REMARK 525 HOH A 743 DISTANCE = 7.30 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 A 301 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 70 OE1
REMARK 620 2 ASN A 72 O 86.8
REMARK 620 3 VAL A 75 O 152.6 83.4
REMARK 620 4 GLU A 80 OE2 102.1 169.7 86.4
REMARK 620 5 HOH A 427 O 74.6 100.5 82.1 77.4
REMARK 620 6 HOH A 625 O 91.8 91.3 113.8 93.5 161.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 303 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 70 O
REMARK 620 2 ASP A 71 OD1 112.3
REMARK 620 3 HOH A 499 O 98.9 145.6
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SIN A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 303
DBREF 5JYI A -7 245 UNP P00760 TRY1_BOVIN 1 246
SEQRES 1 A 246 MET LYS THR PHE ILE PHE LEU ALA LEU LEU GLY ALA ALA
SEQRES 2 A 246 VAL ALA PHE PRO VAL ASP ASP ASP ASP LYS ILE VAL GLY
SEQRES 3 A 246 GLY TYR THR CYS GLY ALA ASN THR VAL PRO TYR GLN VAL
SEQRES 4 A 246 SER LEU ASN SER GLY TYR HIS PHE CYS GLY GLY SER LEU
SEQRES 5 A 246 ILE ASN SER GLN TRP VAL VAL SER ALA ALA HIS CYS TYR
SEQRES 6 A 246 LYS SER GLY ILE GLN VAL ARG LEU GLY GLU ASP ASN ILE
SEQRES 7 A 246 ASN VAL VAL GLU GLY ASN GLU GLN PHE ILE SER ALA SER
SEQRES 8 A 246 LYS SER ILE VAL HIS PRO SER TYR ASN SER ASN THR LEU
SEQRES 9 A 246 ASN ASN ASP ILE MET LEU ILE LYS LEU LYS SER ALA ALA
SEQRES 10 A 246 SER LEU ASN SER ARG VAL ALA SER ILE SER LEU PRO THR
SEQRES 11 A 246 SER CYS ALA SER ALA GLY THR GLN CYS LEU ILE SER GLY
SEQRES 12 A 246 TRP GLY ASN THR LYS SER SER GLY THR SER TYR PRO ASP
SEQRES 13 A 246 VAL LEU LYS CYS LEU LYS ALA PRO ILE LEU SER ASP SER
SEQRES 14 A 246 SER CYS LYS SER ALA TYR PRO GLY GLN ILE THR SER ASN
SEQRES 15 A 246 MET PHE CYS ALA GLY TYR LEU GLU GLY GLY LYS ASP SER
SEQRES 16 A 246 CYS GLN GLY ASP SER GLY GLY PRO VAL VAL CYS SER GLY
SEQRES 17 A 246 LYS LEU GLN GLY ILE VAL SER TRP GLY SER GLY CYS ALA
SEQRES 18 A 246 GLN LYS ASN LYS PRO GLY VAL TYR THR LYS VAL CYS ASN
SEQRES 19 A 246 TYR VAL SER TRP ILE LYS GLN THR ILE ALA SER ASN
HET CA A 301 1
HET SIN A 302 8
HET NA A 303 1
HETNAM CA CALCIUM ION
HETNAM SIN SUCCINIC ACID
HETNAM NA SODIUM ION
FORMUL 2 CA CA 2+
FORMUL 3 SIN C4 H6 O4
FORMUL 4 NA NA 1+
FORMUL 5 HOH *343(H2 O)
HELIX 1 AA1 ALA A 55 TYR A 59 5 5
HELIX 2 AA2 SER A 164 TYR A 172 1 9
HELIX 3 AA3 TYR A 234 ASN A 245 1 12
SHEET 1 AA1 7 TYR A 20 THR A 21 0
SHEET 2 AA1 7 LYS A 156 PRO A 161 -1 O CYS A 157 N TYR A 20
SHEET 3 AA1 7 GLN A 135 GLY A 140 -1 N ILE A 138 O LEU A 158
SHEET 4 AA1 7 PRO A 198 CYS A 201 -1 O VAL A 200 N LEU A 137
SHEET 5 AA1 7 LYS A 204 TRP A 215 -1 O LYS A 204 N CYS A 201
SHEET 6 AA1 7 GLY A 226 LYS A 230 -1 O VAL A 227 N TRP A 215
SHEET 7 AA1 7 MET A 180 ALA A 183 -1 N PHE A 181 O TYR A 228
SHEET 1 AA2 7 GLN A 30 ASN A 34 0
SHEET 2 AA2 7 HIS A 40 ASN A 48 -1 O CYS A 42 N LEU A 33
SHEET 3 AA2 7 TRP A 51 SER A 54 -1 O VAL A 53 N SER A 45
SHEET 4 AA2 7 MET A 104 LEU A 108 -1 O ILE A 106 N VAL A 52
SHEET 5 AA2 7 GLN A 81 VAL A 90 -1 N SER A 86 O LYS A 107
SHEET 6 AA2 7 GLN A 64 LEU A 67 -1 N LEU A 67 O GLN A 81
SHEET 7 AA2 7 GLN A 30 ASN A 34 -1 N ASN A 34 O GLN A 64
SSBOND 1 CYS A 22 CYS A 157 1555 1555 2.03
SSBOND 2 CYS A 42 CYS A 58 1555 1555 2.03
SSBOND 3 CYS A 128 CYS A 232 1555 1555 2.04
SSBOND 4 CYS A 136 CYS A 201 1555 1555 2.02
SSBOND 5 CYS A 168 CYS A 182 1555 1555 2.04
SSBOND 6 CYS A 191 CYS A 220 1555 1555 2.04
LINK OE1 GLU A 70 CA CA A 301 1555 1555 2.33
LINK O GLU A 70 NA NA A 303 1555 1555 2.77
LINK OD1 ASP A 71 NA NA A 303 1555 1555 2.82
LINK O ASN A 72 CA CA A 301 1555 1555 2.33
LINK O VAL A 75 CA CA A 301 1555 1555 2.35
LINK OE2 GLU A 80 CA CA A 301 1555 1555 2.27
LINK CA CA A 301 O HOH A 427 1555 1555 2.68
LINK CA CA A 301 O HOH A 625 1555 1555 2.44
LINK NA NA A 303 O HOH A 499 1555 1555 2.67
SITE 1 AC1 6 GLU A 70 ASN A 72 VAL A 75 GLU A 80
SITE 2 AC1 6 HOH A 427 HOH A 625
SITE 1 AC2 12 PHE A 41 HIS A 57 CYS A 128 TYR A 151
SITE 2 AC2 12 GLN A 192 GLY A 193 SER A 195 LYS A 230
SITE 3 AC2 12 HOH A 463 HOH A 464 HOH A 502 HOH A 573
SITE 1 AC3 4 ASN A 25 GLU A 70 ASP A 71 HOH A 499
CRYST1 46.320 53.180 76.810 90.00 90.00 90.00 P 21 21 21 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 0.021589 0.000000 0.000000 0.00000
SCALE2 0.000000 0.018804 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013019 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
