HEADER OXIDOREDUCTASE 10-MAR-15 4YNI
TITLE IRON FREE SUCCINATE BOUND RAT CYSTEINE DIOXYGENASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYSTEINE DIOXYGENASE TYPE 1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CYSTEINE DIOXYGENASE TYPE I,CDO-I;
COMPND 5 EC: 1.13.11.20;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 GENE: CDO1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PPR-IBA1/RATCDO/WT
KEYWDS NON-HEME MONO-IRON, CUPIN, SUCCINATE, IRON FREE, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.FELLNER,E.P.TCHESNOKOV,G.N.L.JAMESON,S.M.WILBANKS
REVDAT 1 23-MAR-16 4YNI 0
JRNL AUTH M.FELLNER,E.P.TCHESNOKOV,G.N.L.JAMESON,S.M.WILBANKS
JRNL TITL IRON FREE SUCCINATE BOUND RAT CYSTEINE DIOXYGENASE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9-1692
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) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.89
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.120
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 15169
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.178
REMARK 3 R VALUE (WORKING SET) : 0.175
REMARK 3 FREE R VALUE : 0.224
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.140
REMARK 3 FREE R VALUE TEST SET COUNT : 779
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 41.8996 - 4.3672 0.99 2414 125 0.1361 0.1440
REMARK 3 2 4.3672 - 3.4669 0.99 2359 155 0.1566 0.2150
REMARK 3 3 3.4669 - 3.0288 0.99 2409 111 0.1897 0.2435
REMARK 3 4 3.0288 - 2.7519 1.00 2430 114 0.2097 0.3029
REMARK 3 5 2.7519 - 2.5547 1.00 2426 129 0.2268 0.3127
REMARK 3 6 2.5547 - 2.4040 1.00 2352 145 0.2424 0.3071
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) : 0.270
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.670
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 36.89
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.30
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 : 0.010 1602
REMARK 3 ANGLE : 1.068 2171
REMARK 3 CHIRALITY : 0.058 230
REMARK 3 PLANARITY : 0.005 285
REMARK 3 DIHEDRAL : 13.542 593
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 4YNI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-MAR-15.
REMARK 100 THE DEPOSITION ID IS D_1000207758.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-DEC-13
REMARK 200 TEMPERATURE (KELVIN) : 93
REMARK 200 PH : 5.2
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
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54187
REMARK 200 MONOCHROMATOR : OSMIC VARIMAX OPTICS
REMARK 200 OPTICS : OSMIC VARIMAX OPTICS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM 7.1.0
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.3.11
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15515
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 41.890
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 10.00
REMARK 200 R MERGE (I) : 0.13400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 8.60
REMARK 200 R MERGE FOR SHELL (I) : 0.75600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.5.6
REMARK 200 STARTING MODEL: 4KWJ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.15
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.09
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: HANGING DROPS OF 1 MICROL OF 15 MG/ML
REMARK 280 WT-CDO (10MM SODIUMPHOSPHATE, 20MM NACL PH 7.5) AND 3 MICROL
REMARK 280 RESERVOIR BUFFER WERE ALLOWED TO EQUILIBRATE ABOVE THE RESERVOIR
REMARK 280 BUFFER (25% (W/V) POLYETHYLENE GLYCOL 1500, 13 MM SUCCINATE, 44
REMARK 280 MM MONO SODIUM PHOSPHATE, 44 MM GLYCINE) AND 0.6 MICROL WT-CDO
REMARK 280 SEEDS (GROWN IN THE RESERVOIR BUFFER), PH 5.2, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 60.93500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 28.84500
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 28.84500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 91.40250
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 28.84500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 28.84500
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 30.46750
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 28.84500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 28.84500
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 91.40250
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 28.84500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 28.84500
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 30.46750
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 60.93500
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 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 1
REMARK 465 GLU A 2
REMARK 465 ARG A 3
REMARK 465 PHE A 191
REMARK 465 THR A 192
REMARK 465 THR A 193
REMARK 465 SER A 194
REMARK 465 GLY A 195
REMARK 465 SER A 196
REMARK 465 LEU A 197
REMARK 465 GLU A 198
REMARK 465 ASN A 199
REMARK 465 ASN A 200
REMARK 465 SER A 201
REMARK 465 ALA A 202
REMARK 465 TRP A 203
REMARK 465 SER A 204
REMARK 465 HIS A 205
REMARK 465 PRO A 206
REMARK 465 GLN A 207
REMARK 465 PHE A 208
REMARK 465 GLU A 209
REMARK 465 LYS A 210
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 OE2 GLU A 46 O HOH A 446 2.03
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 ASN A 128 -7.64 77.79
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 NA A 301 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 135 OD1
REMARK 620 2 GLY A 138 O 114.8
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA 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
DBREF 4YNI A 1 200 UNP P21816 CDO1_RAT 1 200
SEQADV 4YNI SER A 201 UNP P21816 EXPRESSION TAG
SEQADV 4YNI ALA A 202 UNP P21816 EXPRESSION TAG
SEQADV 4YNI TRP A 203 UNP P21816 EXPRESSION TAG
SEQADV 4YNI SER A 204 UNP P21816 EXPRESSION TAG
SEQADV 4YNI HIS A 205 UNP P21816 EXPRESSION TAG
SEQADV 4YNI PRO A 206 UNP P21816 EXPRESSION TAG
SEQADV 4YNI GLN A 207 UNP P21816 EXPRESSION TAG
SEQADV 4YNI PHE A 208 UNP P21816 EXPRESSION TAG
SEQADV 4YNI GLU A 209 UNP P21816 EXPRESSION TAG
SEQADV 4YNI LYS A 210 UNP P21816 EXPRESSION TAG
SEQRES 1 A 210 MET GLU ARG THR GLU LEU LEU LYS PRO ARG THR LEU ALA
SEQRES 2 A 210 ASP LEU ILE ARG ILE LEU HIS GLU LEU PHE ALA GLY ASP
SEQRES 3 A 210 GLU VAL ASN VAL GLU GLU VAL GLN ALA VAL LEU GLU ALA
SEQRES 4 A 210 TYR GLU SER ASN PRO ALA GLU TRP ALA LEU TYR ALA LYS
SEQRES 5 A 210 PHE ASP GLN TYR ARG TYR THR ARG ASN LEU VAL ASP GLN
SEQRES 6 A 210 GLY ASN GLY LYS PHE ASN LEU MET ILE LEU CYS TRP GLY
SEQRES 7 A 210 GLU GLY HIS GLY SER SER ILE HIS ASP HIS THR ASP SER
SEQRES 8 A 210 HIS CYS PHE LEU LYS LEU LEU GLN GLY ASN LEU LYS GLU
SEQRES 9 A 210 THR LEU PHE ASP TRP PRO ASP LYS LYS SER ASN GLU MET
SEQRES 10 A 210 ILE LYS LYS SER GLU ARG THR LEU ARG GLU ASN GLN CYS
SEQRES 11 A 210 ALA TYR ILE ASN ASP SER ILE GLY LEU HIS ARG VAL GLU
SEQRES 12 A 210 ASN VAL SER HIS THR GLU PRO ALA VAL SER LEU HIS LEU
SEQRES 13 A 210 TYR SER PRO PRO PHE ASP THR CYS HIS ALA PHE ASP GLN
SEQRES 14 A 210 ARG THR GLY HIS LYS ASN LYS VAL THR MET THR PHE HIS
SEQRES 15 A 210 SER LYS PHE GLY ILE ARG THR PRO PHE THR THR SER GLY
SEQRES 16 A 210 SER LEU GLU ASN ASN SER ALA TRP SER HIS PRO GLN PHE
SEQRES 17 A 210 GLU LYS
HET NA A 301 1
HET SIN A 302 8
HETNAM NA SODIUM ION
HETNAM SIN SUCCINIC ACID
FORMUL 2 NA NA 1+
FORMUL 3 SIN C4 H6 O4
FORMUL 4 HOH *87(H2 O)
HELIX 1 AA1 THR A 11 PHE A 23 1 13
HELIX 2 AA2 ASN A 29 TYR A 40 1 12
HELIX 3 AA3 ASN A 43 ALA A 48 1 6
HELIX 4 AA4 GLN A 65 LYS A 69 5 5
SHEET 1 AA1 7 CYS A 130 ILE A 133 0
SHEET 2 AA1 7 HIS A 92 GLN A 99 -1 N LEU A 95 O ALA A 131
SHEET 3 AA1 7 ALA A 151 SER A 158 -1 O SER A 158 N HIS A 92
SHEET 4 AA1 7 ASN A 71 TRP A 77 -1 N MET A 73 O HIS A 155
SHEET 5 AA1 7 THR A 59 ASP A 64 -1 N ASN A 61 O ILE A 74
SHEET 6 AA1 7 SER A 183 LYS A 184 1 O SER A 183 N LEU A 62
SHEET 7 AA1 7 ILE A 187 ARG A 188 -1 O ILE A 187 N LYS A 184
SHEET 1 AA2 3 ILE A 85 HIS A 86 0
SHEET 2 AA2 3 THR A 163 PHE A 167 -1 O PHE A 167 N ILE A 85
SHEET 3 AA2 3 LYS A 174 THR A 178 -1 O VAL A 177 N CYS A 164
SHEET 1 AA3 3 LYS A 119 LEU A 125 0
SHEET 2 AA3 3 LEU A 102 PHE A 107 -1 N LEU A 102 O LEU A 125
SHEET 3 AA3 3 LEU A 139 GLU A 143 -1 O GLU A 143 N LYS A 103
LINK SG CYS A 93 CE2 TYR A 157 1555 1555 1.84
LINK OD1 ASP A 135 NA NA A 301 1555 1555 2.24
LINK O GLY A 138 NA NA A 301 1555 1555 3.01
CISPEP 1 SER A 158 PRO A 159 0 -3.34
SITE 1 AC1 5 ASP A 87 HIS A 88 ASN A 134 ASP A 135
SITE 2 AC1 5 GLY A 138
SITE 1 AC2 10 TYR A 58 ARG A 60 LEU A 75 HIS A 86
SITE 2 AC2 10 HIS A 88 CYS A 93 HIS A 140 TYR A 157
SITE 3 AC2 10 MET A 179 HOH A 486
CRYST1 57.690 57.690 121.870 90.00 90.00 90.00 P 43 21 2 8
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 0.017334 0.000000 0.000000 0.00000
SCALE2 0.000000 0.017334 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008205 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
