HEADER LYASE 25-SEP-18 6MKM
TITLE CRYSTALLOGRAPHIC SOLVENT MAPPING ANALYSIS OF DMSO/TRIS BOUND TO APE1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA-(APURINIC OR APYRIMIDINIC SITE) LYASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 40-318;
COMPND 5 SYNONYM: APEX NUCLEASE, APEN, APURINIC-APYRIMIDINIC ENDONUCLEASE 1,
COMPND 6 APE-1, REF-1, REDOX FACTOR-1;
COMPND 7 EC: 3.1.-.-,4.2.99.18;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: APEX1, APE, APE1, APEX, APX, HAP1, REF1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS APURINIC/APYRIMIDINIC ENDONUCLEASE, DNA REPAIR, ABASIC SITE, SOLVENT
KEYWDS 2 MAPPING, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.M.GEORGIADIS,H.HE,Q.CHEN
REVDAT 4 13-MAR-24 6MKM 1 REMARK
REVDAT 3 04-DEC-19 6MKM 1 REMARK
REVDAT 2 13-MAR-19 6MKM 1 JRNL
REVDAT 1 30-JAN-19 6MKM 0
JRNL AUTH R.TRILLES,D.BEGLOV,Q.CHEN,H.HE,R.WIREMAN,A.REED,
JRNL AUTH 2 S.CHENNAMADHAVUNI,J.S.PANEK,L.E.BROWN,S.VAJDA,J.A.PORCO JR.,
JRNL AUTH 3 M.R.KELLEY,M.M.GEORGIADIS
JRNL TITL DISCOVERY OF MACROCYCLIC INHIBITORS OF APURINIC/APYRIMIDINIC
JRNL TITL 2 ENDONUCLEASE 1.
JRNL REF J. MED. CHEM. V. 62 1971 2019
JRNL REFN ISSN 1520-4804
JRNL PMID 30653918
JRNL DOI 10.1021/ACS.JMEDCHEM.8B01529
REMARK 2
REMARK 2 RESOLUTION. 1.67 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
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) : 1.67
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.63
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.1
REMARK 3 NUMBER OF REFLECTIONS : 32423
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.207
REMARK 3 R VALUE (WORKING SET) : 0.205
REMARK 3 FREE R VALUE : 0.250
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1652
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 37.6356 - 3.8282 0.97 2836 127 0.1873 0.2077
REMARK 3 2 3.8282 - 3.0390 0.99 2710 154 0.1851 0.2048
REMARK 3 3 3.0390 - 2.6549 0.99 2706 145 0.1973 0.2862
REMARK 3 4 2.6549 - 2.4122 0.99 2663 160 0.2025 0.2522
REMARK 3 5 2.4122 - 2.2394 0.99 2650 154 0.2035 0.2537
REMARK 3 6 2.2394 - 2.1073 0.99 2674 136 0.2015 0.2832
REMARK 3 7 2.1073 - 2.0018 0.99 2646 153 0.1978 0.2318
REMARK 3 8 2.0018 - 1.9147 0.97 2573 143 0.2088 0.2729
REMARK 3 9 1.9147 - 1.8410 0.95 2523 127 0.2180 0.2836
REMARK 3 10 1.8410 - 1.7774 0.91 2410 127 0.2283 0.3022
REMARK 3 11 1.7774 - 1.7219 0.88 2315 120 0.2601 0.3256
REMARK 3 12 1.7219 - 1.6726 0.78 2065 106 0.2834 0.3798
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 : 0.39
REMARK 3 B_SOL : 51.42
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.290
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.790
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 17.98
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.53
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -6.29210
REMARK 3 B22 (A**2) : 10.71690
REMARK 3 B33 (A**2) : -4.42470
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
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 : 0.004 2328
REMARK 3 ANGLE : 0.934 3157
REMARK 3 CHIRALITY : 0.064 333
REMARK 3 PLANARITY : 0.004 410
REMARK 3 DIHEDRAL : 17.325 857
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 6MKM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-SEP-18.
REMARK 100 THE DEPOSITION ID IS D_1000237106.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-JUN-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.07109
REMARK 200 MONOCHROMATOR : ROSENBAUM-ROCK DOUBLE CRYSTAL
REMARK 200 SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32466
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.670
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.3
REMARK 200 DATA REDUNDANCY : 4.300
REMARK 200 R MERGE (I) : 0.07700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.67
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.70
REMARK 200 COMPLETENESS FOR SHELL (%) : 79.4
REMARK 200 DATA REDUNDANCY IN SHELL : 2.90
REMARK 200 R MERGE FOR SHELL (I) : 0.38400
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.06
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM MES, PH 6.0, 200 MM SODIUM
REMARK 280 CHLORIDE, 18-21% PEG4000, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
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 23.27600
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 68.30050
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 23.27600
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 68.30050
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: 1180 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12420 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 18.0 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 GLY A 34
REMARK 465 SER A 35
REMARK 465 HIS A 36
REMARK 465 MET A 37
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 LEU A 111 69.65 -117.44
REMARK 500 LYS A 125 16.41 83.79
REMARK 500 SER A 129 -143.56 50.79
REMARK 500 PHE A 232 19.54 -142.74
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TRS A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 405
DBREF 6MKM A 40 318 UNP P27695 APEX1_HUMAN 40 318
SEQADV 6MKM GLY A 34 UNP P27695 EXPRESSION TAG
SEQADV 6MKM SER A 35 UNP P27695 EXPRESSION TAG
SEQADV 6MKM HIS A 36 UNP P27695 EXPRESSION TAG
SEQADV 6MKM MET A 37 UNP P27695 EXPRESSION TAG
SEQADV 6MKM ALA A 38 UNP P27695 EXPRESSION TAG
SEQADV 6MKM SER A 39 UNP P27695 EXPRESSION TAG
SEQADV 6MKM ALA A 138 UNP P27695 CYS 138 CONFLICT
SEQRES 1 A 285 GLY SER HIS MET ALA SER GLU GLY PRO ALA LEU TYR GLU
SEQRES 2 A 285 ASP PRO PRO ASP GLN LYS THR SER PRO SER GLY LYS PRO
SEQRES 3 A 285 ALA THR LEU LYS ILE CYS SER TRP ASN VAL ASP GLY LEU
SEQRES 4 A 285 ARG ALA TRP ILE LYS LYS LYS GLY LEU ASP TRP VAL LYS
SEQRES 5 A 285 GLU GLU ALA PRO ASP ILE LEU CYS LEU GLN GLU THR LYS
SEQRES 6 A 285 CYS SER GLU ASN LYS LEU PRO ALA GLU LEU GLN GLU LEU
SEQRES 7 A 285 PRO GLY LEU SER HIS GLN TYR TRP SER ALA PRO SER ASP
SEQRES 8 A 285 LYS GLU GLY TYR SER GLY VAL GLY LEU LEU SER ARG GLN
SEQRES 9 A 285 ALA PRO LEU LYS VAL SER TYR GLY ILE GLY ASP GLU GLU
SEQRES 10 A 285 HIS ASP GLN GLU GLY ARG VAL ILE VAL ALA GLU PHE ASP
SEQRES 11 A 285 SER PHE VAL LEU VAL THR ALA TYR VAL PRO ASN ALA GLY
SEQRES 12 A 285 ARG GLY LEU VAL ARG LEU GLU TYR ARG GLN ARG TRP ASP
SEQRES 13 A 285 GLU ALA PHE ARG LYS PHE LEU LYS GLY LEU ALA SER ARG
SEQRES 14 A 285 LYS PRO LEU VAL LEU CYS GLY ASP LEU ASN VAL ALA HIS
SEQRES 15 A 285 GLU GLU ILE ASP LEU ARG ASN PRO LYS GLY ASN LYS LYS
SEQRES 16 A 285 ASN ALA GLY PHE THR PRO GLN GLU ARG GLN GLY PHE GLY
SEQRES 17 A 285 GLU LEU LEU GLN ALA VAL PRO LEU ALA ASP SER PHE ARG
SEQRES 18 A 285 HIS LEU TYR PRO ASN THR PRO TYR ALA TYR THR PHE TRP
SEQRES 19 A 285 THR TYR MET MET ASN ALA ARG SER LYS ASN VAL GLY TRP
SEQRES 20 A 285 ARG LEU ASP TYR PHE LEU LEU SER HIS SER LEU LEU PRO
SEQRES 21 A 285 ALA LEU CYS ASP SER LYS ILE ARG SER LYS ALA LEU GLY
SEQRES 22 A 285 SER ASP HIS CYS PRO ILE THR LEU TYR LEU ALA LEU
HET TRS A 401 8
HET DMS A 402 4
HET DMS A 403 4
HET EDO A 404 4
HET EDO A 405 4
HETNAM TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL
HETNAM DMS DIMETHYL SULFOXIDE
HETNAM EDO 1,2-ETHANEDIOL
HETSYN TRS TRIS BUFFER
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 TRS C4 H12 N O3 1+
FORMUL 3 DMS 2(C2 H6 O S)
FORMUL 5 EDO 2(C2 H6 O2)
FORMUL 7 HOH *158(H2 O)
HELIX 1 AA1 GLY A 71 LYS A 78 1 8
HELIX 2 AA2 LYS A 79 ALA A 88 1 10
HELIX 3 AA3 PRO A 105 SER A 115 5 11
HELIX 4 AA4 ASP A 148 ASP A 152 5 5
HELIX 5 AA5 GLY A 176 VAL A 180 5 5
HELIX 6 AA6 ARG A 181 SER A 201 1 21
HELIX 7 AA7 GLU A 216 LEU A 220 5 5
HELIX 8 AA8 PRO A 223 LYS A 227 5 5
HELIX 9 AA9 THR A 233 VAL A 247 1 15
HELIX 10 AB1 SER A 252 TYR A 257 1 6
HELIX 11 AB2 HIS A 289 PRO A 293 5 5
SHEET 1 AA1 6 HIS A 116 SER A 120 0
SHEET 2 AA1 6 VAL A 131 SER A 135 -1 O SER A 135 N HIS A 116
SHEET 3 AA1 6 ILE A 91 GLN A 95 -1 N LEU A 92 O LEU A 134
SHEET 4 AA1 6 LEU A 62 ASN A 68 1 N CYS A 65 O CYS A 93
SHEET 5 AA1 6 ILE A 312 LEU A 316 -1 O LEU A 314 N ILE A 64
SHEET 6 AA1 6 LEU A 295 ILE A 300 -1 N LYS A 299 O THR A 313
SHEET 1 AA2 6 LYS A 141 TYR A 144 0
SHEET 2 AA2 6 VAL A 157 GLU A 161 -1 O VAL A 159 N SER A 143
SHEET 3 AA2 6 VAL A 166 TYR A 171 -1 O LEU A 167 N ALA A 160
SHEET 4 AA2 6 LEU A 205 ASP A 210 1 O VAL A 206 N VAL A 168
SHEET 5 AA2 6 ASP A 283 LEU A 287 -1 O LEU A 286 N LEU A 207
SHEET 6 AA2 6 ALA A 250 ASP A 251 -1 N ALA A 250 O LEU A 287
CISPEP 1 VAL A 247 PRO A 248 0 -2.39
SITE 1 AC1 9 ASP A 70 GLU A 96 LYS A 98 TYR A 171
SITE 2 AC1 9 ASP A 308 HOH A 511 HOH A 519 HOH A 537
SITE 3 AC1 9 HOH A 561
SITE 1 AC2 4 ASN A 174 ALA A 230 LEU A 282 HOH A 562
SITE 1 AC3 5 GLN A 137 ALA A 138 LEU A 140 PHE A 162
SITE 2 AC3 5 ASP A 163
SITE 1 AC4 5 HIS A 215 GLU A 216 ARG A 237 GLN A 238
SITE 2 AC4 5 GLY A 241
SITE 1 AC5 6 ALA A 38 TRP A 119 SER A 120 ALA A 121
SITE 2 AC5 6 TYR A 144 HOH A 514
CRYST1 46.552 136.601 45.084 90.00 90.00 90.00 P 21 21 2 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 0.021481 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007321 0.000000 0.00000
SCALE3 0.000000 0.000000 0.022181 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
