HEADER TRANSFERASE 24-AUG-04 1WOO
TITLE CRYSTAL STRUCTURE OF T-PROTEIN OF THE GLYCINE CLEAVAGE SYSTEM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: AMINOMETHYLTRANSFERASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: GLYCINE CLEAVAGE SYSTEM T PROTEIN;
COMPND 5 EC: 2.1.2.10;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOTOGA MARITIMA;
SOURCE 3 ORGANISM_TAXID: 2336;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: B834(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET21A
KEYWDS GLYCINE CLEAVAGE SYSTEM, TETRAHYDROFOLATE, T-PROTEIN, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.H.LEE,D.J.KIM,H.J.AHN,J.Y.HA,S.W.SUH
REVDAT 5 13-MAR-24 1WOO 1 REMARK
REVDAT 4 24-AUG-11 1WOO 1 HET HETATM HETNAM VERSN
REVDAT 3 24-FEB-09 1WOO 1 VERSN
REVDAT 2 25-JAN-05 1WOO 1 JRNL
REVDAT 1 07-SEP-04 1WOO 0
JRNL AUTH H.H.LEE,D.J.KIM,H.J.AHN,J.Y.HA,S.W.SUH
JRNL TITL CRYSTAL STRUCTURE OF T-PROTEIN OF THE GLYCINE CLEAVAGE
JRNL TITL 2 SYSTEM: COFACTOR BINDING, INSIGHTS INTO H-PROTEIN
JRNL TITL 3 RECOGNITION, AND MOLECULAR BASIS FOR UNDERSTANDING
JRNL TITL 4 NONKETOTIC HYPERGLYCINEMIA
JRNL REF J.BIOL.CHEM. V. 279 50514 2004
JRNL REFN ISSN 0021-9258
JRNL PMID 15355973
JRNL DOI 10.1074/JBC.M409672200
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 26.51
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 213831.720
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 96.0
REMARK 3 NUMBER OF REFLECTIONS : 16578
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 : 0.275
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1657
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.007
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) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.55
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 87.20
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2233
REMARK 3 BIN R VALUE (WORKING SET) : 0.3980
REMARK 3 BIN FREE R VALUE : 0.4930
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.30
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 229
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.033
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2821
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 32
REMARK 3 SOLVENT ATOMS : 124
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 39.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.95000
REMARK 3 B22 (A**2) : -0.81000
REMARK 3 B33 (A**2) : -1.14000
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.30
REMARK 3 ESD FROM SIGMAA (A) : 0.36
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) : 0.41
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.44
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.40
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.780
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) : 2.980 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 4.180 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 4.820 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 6.770 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.40
REMARK 3 BSOL : 37.10
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.PARAM
REMARK 3 PARAMETER FILE 3 : THF.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: NULL
REMARK 4
REMARK 4 1WOO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-AUG-04.
REMARK 100 THE DEPOSITION ID IS D_1000023821.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-JUN-04; NULL
REMARK 200 TEMPERATURE (KELVIN) : 100; NULL
REMARK 200 PH : 4.25
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; NULL
REMARK 200 RADIATION SOURCE : PAL/PLS; NULL
REMARK 200 BEAMLINE : 6B; NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 1.12714; 0.97947, 0.97935,
REMARK 200 0.9500
REMARK 200 MONOCHROMATOR : GRAPHITE; NULL
REMARK 200 OPTICS : MIRRORS; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; NULL
REMARK 200 DETECTOR MANUFACTURER : BRUKER; NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17533
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.3
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) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.7
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: MAD; NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: CRYSTAL 1 SINGLE
REMARK 200 WAVELENGTH PROTOCOL, CRYSATL 2 MAD PROTOCOL
REMARK 200 SOFTWARE USED: SHELXS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.82
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.61
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, SODIUM DIHYDROGEN PHOSPHATE,
REMARK 280 PH 4.25, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 297K
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 26.24950
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 74.70000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 26.97100
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 74.70000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.24950
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 26.97100
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A MONOMER.
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 GLU A 363
REMARK 465 VAL A 364
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 THR A 30 -66.80 -101.45
REMARK 500 SER A 42 -84.51 -127.32
REMARK 500 THR A 235 37.22 71.23
REMARK 500 GLU A 245 -6.41 -59.84
REMARK 500 ASN A 312 170.84 174.27
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 THG A 2887
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1WOP RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH FOLINIC ACID
REMARK 900 RELATED ID: 1WOR RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH DIHYDROLIPOIC ACID
REMARK 900 RELATED ID: 1WOS RELATED DB: PDB
REMARK 900 THE SAME PROTEIN OF NATIVE FORM
DBREF 1WOO A 1 364 UNP Q9WY54 GCST_THEMA 1 364
SEQRES 1 A 364 MET LYS ARG THR PRO LEU PHE GLU LYS HIS VAL GLU LEU
SEQRES 2 A 364 GLY ALA LYS MET VAL ASP PHE ALA GLY TRP GLU MET PRO
SEQRES 3 A 364 LEU TYR TYR THR SER ILE PHE GLU GLU VAL MET ALA VAL
SEQRES 4 A 364 ARG LYS SER VAL GLY MET PHE ASP VAL SER HIS MET GLY
SEQRES 5 A 364 GLU PHE LEU VAL LYS GLY PRO GLU ALA VAL SER PHE ILE
SEQRES 6 A 364 ASP PHE LEU ILE THR ASN ASP PHE SER SER LEU PRO ASP
SEQRES 7 A 364 GLY LYS ALA ILE TYR SER VAL MET CYS ASN GLU ASN GLY
SEQRES 8 A 364 GLY ILE ILE ASP ASP LEU VAL VAL TYR LYS VAL SER PRO
SEQRES 9 A 364 ASP GLU ALA LEU MET VAL VAL ASN ALA ALA ASN ILE GLU
SEQRES 10 A 364 LYS ASP PHE ASN TRP ILE LYS SER HIS SER LYS ASN PHE
SEQRES 11 A 364 ASP VAL GLU VAL SER ASN ILE SER ASP THR THR ALA LEU
SEQRES 12 A 364 ILE ALA PHE GLN GLY PRO LYS ALA GLN GLU THR LEU GLN
SEQRES 13 A 364 GLU LEU VAL GLU ASP GLY LEU GLU GLU ILE ALA TYR TYR
SEQRES 14 A 364 SER PHE ARG LYS SER ILE VAL ALA GLY VAL GLU THR LEU
SEQRES 15 A 364 VAL SER ARG THR GLY TYR THR GLY GLU ASP GLY PHE GLU
SEQRES 16 A 364 LEU MET LEU GLU ALA LYS ASN ALA PRO LYS VAL TRP ASP
SEQRES 17 A 364 ALA LEU MET ASN LEU LEU ARG LYS ILE ASP GLY ARG PRO
SEQRES 18 A 364 ALA GLY LEU GLY ALA ARG ASP VAL CYS ARG LEU GLU ALA
SEQRES 19 A 364 THR TYR LEU LEU TYR GLY GLN ASP MET ASP GLU ASN THR
SEQRES 20 A 364 ASN PRO PHE GLU VAL GLY LEU SER TRP VAL VAL LYS LEU
SEQRES 21 A 364 ASN LYS ASP PHE VAL GLY LYS GLU ALA LEU LEU LYS ALA
SEQRES 22 A 364 LYS GLU LYS VAL GLU ARG LYS LEU VAL ALA LEU GLU LEU
SEQRES 23 A 364 SER GLY LYS ARG ILE ALA ARG LYS GLY TYR GLU VAL LEU
SEQRES 24 A 364 LYS ASN GLY GLU ARG VAL GLY GLU ILE THR SER GLY ASN
SEQRES 25 A 364 PHE SER PRO THR LEU GLY LYS SER ILE ALA LEU ALA LEU
SEQRES 26 A 364 VAL SER LYS SER VAL LYS ILE GLY ASP GLN LEU GLY VAL
SEQRES 27 A 364 VAL PHE PRO GLY GLY LYS LEU VAL GLU ALA LEU VAL VAL
SEQRES 28 A 364 LYS LYS PRO PHE TYR ARG GLY SER VAL ARG ARG GLU VAL
HET THG A2887 32
HETNAM THG (6S)-5,6,7,8-TETRAHYDROFOLATE
FORMUL 2 THG C19 H23 N7 O6
FORMUL 3 HOH *124(H2 O)
HELIX 1 1 LEU A 6 LEU A 13 1 8
HELIX 2 2 SER A 31 SER A 42 1 12
HELIX 3 3 GLU A 60 ILE A 69 1 10
HELIX 4 4 ASN A 112 ALA A 114 5 3
HELIX 5 5 ASN A 115 SER A 125 1 11
HELIX 6 6 LYS A 150 GLN A 156 1 7
HELIX 7 7 GLU A 157 VAL A 159 5 3
HELIX 8 8 GLY A 162 ILE A 166 5 5
HELIX 9 9 ASN A 202 ILE A 217 1 16
HELIX 10 10 GLY A 223 THR A 235 1 13
HELIX 11 11 ASN A 248 GLY A 253 5 6
HELIX 12 12 LEU A 254 VAL A 258 5 5
HELIX 13 13 GLY A 266 LYS A 276 1 11
SHEET 1 A 2 LYS A 16 PHE A 20 0
SHEET 2 A 2 TRP A 23 TYR A 28 -1 O LEU A 27 N LYS A 16
SHEET 1 B 6 PHE A 171 VAL A 176 0
SHEET 2 B 6 VAL A 179 SER A 184 -1 O THR A 181 N SER A 174
SHEET 3 B 6 GLY A 193 GLU A 199 -1 O MET A 197 N LEU A 182
SHEET 4 B 6 THR A 141 GLN A 147 -1 N ALA A 142 O LEU A 198
SHEET 5 B 6 GLY A 44 ASP A 47 -1 N PHE A 46 O ALA A 145
SHEET 6 B 6 ARG A 220 ALA A 222 1 O ALA A 222 N MET A 45
SHEET 1 C 5 LYS A 80 CYS A 87 0
SHEET 2 C 5 ILE A 93 SER A 103 -1 O LEU A 97 N SER A 84
SHEET 3 C 5 GLU A 106 VAL A 111 -1 O LEU A 108 N TYR A 100
SHEET 4 C 5 GLY A 52 LYS A 57 -1 N PHE A 54 O MET A 109
SHEET 5 C 5 GLU A 133 ASN A 136 -1 O SER A 135 N LEU A 55
SHEET 1 D 7 ARG A 279 LEU A 286 0
SHEET 2 D 7 LYS A 319 SER A 327 -1 O ALA A 322 N LEU A 284
SHEET 3 D 7 GLU A 303 SER A 314 -1 N SER A 314 O LYS A 319
SHEET 4 D 7 GLU A 297 LYS A 300 -1 N VAL A 298 O VAL A 305
SHEET 5 D 7 GLN A 335 PHE A 340 -1 O GLY A 337 N LEU A 299
SHEET 6 D 7 LYS A 344 VAL A 351 -1 O LYS A 344 N PHE A 340
SHEET 7 D 7 ARG A 279 LEU A 286 -1 N ALA A 283 O VAL A 351
CISPEP 1 LYS A 353 PRO A 354 0 2.35
SITE 1 AC1 20 MET A 51 TYR A 83 ASP A 96 VAL A 98
SITE 2 AC1 20 TYR A 100 VAL A 110 ASN A 112 TYR A 168
SITE 3 AC1 20 TYR A 169 GLY A 187 TYR A 188 GLU A 195
SITE 4 AC1 20 ARG A 227 TYR A 236 TRP A 256 ARG A 362
SITE 5 AC1 20 HOH A2907 HOH A2909 HOH A2935 HOH A2960
CRYST1 52.499 53.942 149.400 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 0.019048 0.000000 0.000000 0.00000
SCALE2 0.000000 0.018538 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006693 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
