HEADER HYDROLASE 13-DEC-16 5MNX
TITLE NEUTRON STRUCTURE OF CATIONIC TRYPSIN IN COMPLEX WITH 2-AMINOPYRIDINE
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 HYDROGEN BONDING, PROTONATION, PROTEIN-LIGAND INTERACTION, HYDROLASE
EXPDTA NEUTRON DIFFRACTION
AUTHOR J.SCHIEBEL,T.E.SCHRADER,A.OSTERMANN,A.HEINE,G.KLEBE
REVDAT 4 17-JAN-24 5MNX 1 REMARK
REVDAT 3 14-NOV-18 5MNX 1 REMARK
REVDAT 2 23-AUG-17 5MNX 1 ATOM
REVDAT 1 24-MAY-17 5MNX 0
JRNL AUTH J.SCHIEBEL,R.GASPARI,A.SANDNER,K.NGO,H.D.GERBER,A.CAVALLI,
JRNL AUTH 2 A.OSTERMANN,A.HEINE,G.KLEBE
JRNL TITL CHARGES SHIFT PROTONATION: NEUTRON DIFFRACTION REVEALS THAT
JRNL TITL 2 ANILINE AND 2-AMINOPYRIDINE BECOME PROTONATED UPON BINDING
JRNL TITL 3 TO TRYPSIN.
JRNL REF ANGEW. CHEM. INT. ED. ENGL. V. 56 4887 2017
JRNL REFN ESSN 1521-3773
JRNL PMID 28371253
JRNL DOI 10.1002/ANIE.201701038
REMARK 2
REMARK 2 RESOLUTION. 1.42 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (DEV_2429)
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.42
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 22.17
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 90.6
REMARK 3 NUMBER OF REFLECTIONS : 38107
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.168
REMARK 3 R VALUE (WORKING SET) : 0.166
REMARK 3 FREE R VALUE : 0.206
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.020
REMARK 3 FREE R VALUE TEST SET COUNT : 1913
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 22.1683 - 3.4188 0.99 3022 146 0.1493 0.1655
REMARK 3 2 3.4188 - 2.7152 0.99 2910 129 0.1573 0.1817
REMARK 3 3 2.7152 - 2.3724 0.97 2798 145 0.1381 0.1621
REMARK 3 4 2.3724 - 2.1557 0.89 2530 135 0.1413 0.1867
REMARK 3 5 2.1557 - 2.0013 0.94 2679 135 0.1410 0.1845
REMARK 3 6 2.0013 - 1.8834 0.94 2649 153 0.1470 0.1986
REMARK 3 7 1.8834 - 1.7891 0.95 2663 151 0.1574 0.1948
REMARK 3 8 1.7891 - 1.7112 0.95 2714 128 0.1677 0.2519
REMARK 3 9 1.7112 - 1.6454 0.94 2637 146 0.1718 0.2333
REMARK 3 10 1.6454 - 1.5886 0.91 2589 126 0.2177 0.2487
REMARK 3 11 1.5886 - 1.5390 0.89 2502 135 0.2089 0.2652
REMARK 3 12 1.5390 - 1.4950 0.85 2377 149 0.2162 0.2665
REMARK 3 13 1.4950 - 1.4556 0.80 2217 138 0.2527 0.3144
REMARK 3 14 1.4556 - 1.4201 0.68 1907 97 0.3383 0.3769
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.160
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.610
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 : 0.005 3622
REMARK 3 ANGLE : 0.980 6201
REMARK 3 CHIRALITY : 0.085 256
REMARK 3 PLANARITY : 0.006 791
REMARK 3 DIHEDRAL : 11.602 911
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 5MNX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 14-DEC-16.
REMARK 100 THE DEPOSITION ID IS D_1200002712.
REMARK 230
REMARK 230 EXPERIMENTAL DETAILS
REMARK 230 EXPERIMENT TYPE : NEUTRON DIFFRACTION
REMARK 230 DATE OF DATA COLLECTION : 25-JUL-15
REMARK 230 TEMPERATURE (KELVIN) : 295.0
REMARK 230 PH : 7.50
REMARK 230 NUMBER OF CRYSTALS USED : 1
REMARK 230
REMARK 230 NEUTRON SOURCE : NUCLEAR REACTOR
REMARK 230 BEAMLINE : BIODIFF
REMARK 230 WAVELENGTH OR RANGE (A) : 2.675
REMARK 230 MONOCHROMATOR : NULL
REMARK 230 OPTICS : NULL
REMARK 230
REMARK 230 DETECTOR TYPE : IMAGE PLATE
REMARK 230 DETECTOR MANUFACTURER : MAATEL BIODIFF
REMARK 230 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 230 DATA SCALING SOFTWARE : HKL-2000
REMARK 230
REMARK 230 NUMBER OF UNIQUE REFLECTIONS : 38142
REMARK 230 RESOLUTION RANGE HIGH (A) : 1.420
REMARK 230 RESOLUTION RANGE LOW (A) : 25.000
REMARK 230 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 230
REMARK 230 OVERALL.
REMARK 230 COMPLETENESS FOR RANGE (%) : 90.7
REMARK 230 DATA REDUNDANCY : 2.600
REMARK 230 R MERGE (I) : 0.09400
REMARK 230 R SYM (I) : NULL
REMARK 230 <I/SIGMA(I)> FOR THE DATA SET : 8.4930
REMARK 230
REMARK 230 IN THE HIGHEST RESOLUTION SHELL.
REMARK 230 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.42
REMARK 230 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.45
REMARK 230 COMPLETENESS FOR SHELL (%) : 69.9
REMARK 230 DATA REDUNDANCY IN SHELL : 2.00
REMARK 230 R MERGE FOR SHELL (I) : 0.41400
REMARK 230 R SYM FOR SHELL (I) : NULL
REMARK 230 <I/SIGMA(I)> FOR SHELL : 2.051
REMARK 230
REMARK 230 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 230 SOFTWARE USED : PHASER
REMARK 230 STARTING MODEL: 4I8H
REMARK 230
REMARK 230 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM SULFATE, 0.1 M HEPES PH
REMARK 280 7.5, 16% (W/V) PEG 8000, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 277K
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 27.54800
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 33.81550
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 29.35050
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 33.81550
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.54800
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 29.35050
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 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 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 SER A 61 CB OG
REMARK 470 LYS A 109 CG CD CE NZ
REMARK 470 SER A 113 OG
REMARK 470 SER A 122 OG
REMARK 470 SER A 127 OG
REMARK 470 LYS A 145 CD CE NZ
REMARK 470 SER A 146 OG
REMARK 470 THR A 149 OG1 CG2
REMARK 470 SER A 166 OG
REMARK 470 SER A 167 OG
REMARK 470 LYS A 169 CE NZ
REMARK 470 SER A 170 OG
REMARK 470 GLU A 186 CG CD OE1 OE2
REMARK 470 LYS A 188A CE NZ
REMARK 470 GLN A 192 CG CD OE1 NE2
REMARK 470 LYS A 204 CE NZ
REMARK 470 LYS A 222 CD CE NZ
REMARK 470 SER A 236 OG
REMARK 470 LYS A 239 CE NZ
REMARK 470 GLN A 240 CG CD OE1 NE2
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 OD1 ASP A 153 D1 DOD A 405 1.54
REMARK 500 OE1 GLU A 77 D2 DOD A 410 1.59
REMARK 500 OD1 ASP A 189 D2 DOD A 411 1.60
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 HH TYR A 59 OD1 ASP A 153 4545 1.54
REMARK 500 DH TYR A 59 OD1 ASP A 153 4545 1.54
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 -77.07 -119.51
REMARK 500 ASN A 115 -157.51 -143.20
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 A 301 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 70 OE1
REMARK 620 2 ASN A 72 O 91.5
REMARK 620 3 VAL A 75 O 167.3 82.7
REMARK 620 4 GLU A 80 OE2 100.1 158.0 89.2
REMARK 620 5 DOD A 410 O 86.8 86.6 104.0 75.6
REMARK 620 6 DOD A 453 O 80.8 101.6 89.3 98.7 165.3
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 A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 2AP A 302
DBREF 5MNX A 16 245 UNP P00760 TRY1_BOVIN 24 246
SEQRES 1 A 223 ILE VAL GLY GLY TYR THR CYS GLY ALA ASN THR VAL PRO
SEQRES 2 A 223 TYR GLN VAL SER LEU ASN SER GLY TYR HIS PHE CYS GLY
SEQRES 3 A 223 GLY SER LEU ILE ASN SER GLN TRP VAL VAL SER ALA ALA
SEQRES 4 A 223 HIS CYS TYR LYS SER GLY ILE GLN VAL ARG LEU GLY GLU
SEQRES 5 A 223 ASP ASN ILE ASN VAL VAL GLU GLY ASN GLU GLN PHE ILE
SEQRES 6 A 223 SER ALA SER LYS SER ILE VAL HIS PRO SER TYR ASN SER
SEQRES 7 A 223 ASN THR LEU ASN ASN ASP ILE MET LEU ILE LYS LEU LYS
SEQRES 8 A 223 SER ALA ALA SER LEU ASN SER ARG VAL ALA SER ILE SER
SEQRES 9 A 223 LEU PRO THR SER CYS ALA SER ALA GLY THR GLN CYS LEU
SEQRES 10 A 223 ILE SER GLY TRP GLY ASN THR LYS SER SER GLY THR SER
SEQRES 11 A 223 TYR PRO ASP VAL LEU LYS CYS LEU LYS ALA PRO ILE LEU
SEQRES 12 A 223 SER ASP SER SER CYS LYS SER ALA TYR PRO GLY GLN ILE
SEQRES 13 A 223 THR SER ASN MET PHE CYS ALA GLY TYR LEU GLU GLY GLY
SEQRES 14 A 223 LYS ASP SER CYS GLN GLY ASP SER GLY GLY PRO VAL VAL
SEQRES 15 A 223 CYS SER GLY LYS LEU GLN GLY ILE VAL SER TRP GLY SER
SEQRES 16 A 223 GLY CYS ALA GLN LYS ASN LYS PRO GLY VAL TYR THR LYS
SEQRES 17 A 223 VAL CYS ASN TYR VAL SER TRP ILE LYS GLN THR ILE ALA
SEQRES 18 A 223 SER ASN
HET CA A 301 1
HET 2AP A 302 12
HETNAM CA CALCIUM ION
HETNAM 2AP 2-AMINOPYRIDINE
FORMUL 2 CA CA 2+
FORMUL 3 2AP C5 H7 N2 1+
FORMUL 4 DOD *134(D2 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 SER A 244 1 11
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 ILE A 89 O LEU A 105
SHEET 6 AA2 7 GLN A 64 LEU A 67 -1 N VAL A 65 O ILE A 83
SHEET 7 AA2 7 GLN A 30 ASN A 34 -1 N SER A 32 O ARG A 66
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 2.03
SSBOND 4 CYS A 136 CYS A 201 1555 1555 2.04
SSBOND 5 CYS A 168 CYS A 182 1555 1555 2.03
SSBOND 6 CYS A 191 CYS A 220 1555 1555 2.03
LINK OE1 GLU A 70 CA CA A 301 1555 1555 2.28
LINK O ASN A 72 CA CA A 301 1555 1555 2.29
LINK O VAL A 75 CA CA A 301 1555 1555 2.23
LINK OE2 GLU A 80 CA CA A 301 1555 1555 2.38
LINK CA CA A 301 O DOD A 410 1555 1555 2.42
LINK CA CA A 301 O DOD A 453 1555 1555 2.26
SITE 1 AC1 6 GLU A 70 ASN A 72 VAL A 75 GLU A 80
SITE 2 AC1 6 DOD A 410 DOD A 453
SITE 1 AC2 5 ASP A 189 SER A 190 GLY A 216 GLY A 219
SITE 2 AC2 5 GLY A 226
CRYST1 55.096 58.701 67.631 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 0.018150 0.000000 0.000000 0.00000
SCALE2 0.000000 0.017035 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014786 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
