HEADER ISOMERASE 22-OCT-18 6MU0
TITLE CRYSTAL STRUCTURE OF RIBOSE-5-PHOSPHATE ISOMERASE B FROM MYCOPLASMA
TITLE 2 GENITALIUM WITH BOUND RIBULOSE-5-PHOSPHATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROBABLE RIBOSE-5-PHOSPHATE ISOMERASE B;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PHOSPHORIBOISOMERASE B;
COMPND 5 EC: 5.3.1.6;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOPLASMA GENITALIUM (STRAIN ATCC 33530 / G-37
SOURCE 3 / NCTC 10195);
SOURCE 4 ORGANISM_TAXID: 243273;
SOURCE 5 STRAIN: ATCC 33530 / G-37 / NCTC 10195;
SOURCE 6 GENE: RPIB, MG396;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: MYGEA.00966.A.B1
KEYWDS SSGCID, STRUCTURAL GENOMICS, SEATTLE STRUCTURAL GENOMICS CENTER FOR
KEYWDS 2 INFECTIOUS DISEASE, ISOMERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE (SSGCID)
REVDAT 2 11-OCT-23 6MU0 1 REMARK
REVDAT 1 14-NOV-18 6MU0 0
JRNL AUTH D.M.DRANOW,D.D.LORIMER,P.S.HORANYI,T.E.EDWARDS
JRNL TITL CRYSTAL STRUCTURE OF RIBOSE-5-PHOSPHATE ISOMERASE B FROM
JRNL TITL 2 MYCOPLASMA GENITALIUM WITH BOUND RIBULOSE-5-PHOSPHATE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (DEV_3283)
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) : 1.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.10
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.8
REMARK 3 NUMBER OF REFLECTIONS : 57876
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.135
REMARK 3 R VALUE (WORKING SET) : 0.134
REMARK 3 FREE R VALUE : 0.149
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 6.150
REMARK 3 FREE R VALUE TEST SET COUNT : 3557
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 43.1318 - 3.2161 1.00 2515 145 0.1499 0.1769
REMARK 3 2 3.2161 - 2.5528 1.00 2335 155 0.1424 0.1488
REMARK 3 3 2.5528 - 2.2301 1.00 2327 146 0.1396 0.1266
REMARK 3 4 2.2301 - 2.0262 1.00 2245 171 0.1354 0.1518
REMARK 3 5 2.0262 - 1.8810 1.00 2241 161 0.1290 0.1392
REMARK 3 6 1.8810 - 1.7701 0.99 2253 152 0.1379 0.1481
REMARK 3 7 1.7701 - 1.6814 0.99 2222 137 0.1298 0.1513
REMARK 3 8 1.6814 - 1.6083 0.99 2244 119 0.1173 0.1213
REMARK 3 9 1.6083 - 1.5463 0.99 2199 163 0.1107 0.1243
REMARK 3 10 1.5463 - 1.4930 0.98 2180 150 0.1103 0.1226
REMARK 3 11 1.4930 - 1.4463 0.98 2210 142 0.1126 0.1677
REMARK 3 12 1.4463 - 1.4049 0.98 2174 143 0.1127 0.1290
REMARK 3 13 1.4049 - 1.3680 0.98 2162 143 0.1171 0.1296
REMARK 3 14 1.3680 - 1.3346 0.97 2139 138 0.1156 0.1430
REMARK 3 15 1.3346 - 1.3042 0.97 2183 135 0.1154 0.1539
REMARK 3 16 1.3042 - 1.2765 0.98 2193 118 0.1178 0.1429
REMARK 3 17 1.2765 - 1.2509 0.96 2093 162 0.1193 0.1471
REMARK 3 18 1.2509 - 1.2273 0.96 2127 134 0.1191 0.1235
REMARK 3 19 1.2273 - 1.2054 0.96 2112 140 0.1214 0.1500
REMARK 3 20 1.2054 - 1.1850 0.95 2094 123 0.1296 0.1564
REMARK 3 21 1.1850 - 1.1659 0.95 2076 131 0.1312 0.1505
REMARK 3 22 1.1659 - 1.1479 0.94 2084 155 0.1382 0.1822
REMARK 3 23 1.1479 - 1.1310 0.93 2040 132 0.1501 0.1547
REMARK 3 24 1.1310 - 1.1151 0.90 1998 132 0.1518 0.1968
REMARK 3 25 1.1151 - 1.1000 0.86 1873 130 0.1625 0.1692
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) : 0.080
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 11.810
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 13.83
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.07
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 1252
REMARK 3 ANGLE : 0.933 1701
REMARK 3 CHIRALITY : 0.079 200
REMARK 3 PLANARITY : 0.004 218
REMARK 3 DIHEDRAL : 18.876 473
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 6MU0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-OCT-18.
REMARK 100 THE DEPOSITION ID IS D_1000237600.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-AUG-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-F
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97872
REMARK 200 MONOCHROMATOR : DIAMOND [111]
REMARK 200 OPTICS : BERYLLIUM LENSES
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-300
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 59627
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.100
REMARK 200 RESOLUTION RANGE LOW (A) : 43.099
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 9.053
REMARK 200 R MERGE (I) : 0.11100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.6700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.13
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.2
REMARK 200 DATA REDUNDANCY IN SHELL : 7.01
REMARK 200 R MERGE FOR SHELL (I) : 0.51800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.230
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MORDA
REMARK 200 STARTING MODEL: 3HE8
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.98
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MYGEA.00966.A.B1.PW38486 AT 15.59
REMARK 280 MG/ML WAS INCUBATED WITH 5 MM RIBOSE-5-PHOSPHATE, THEN WAS MIXED
REMARK 280 1:1 JCSG+(D5): 70% (V/V) MPD 0.1 M HEPES FREE ACID, PH 7.0, TRAY:
REMARK 280 302126D5, PUCK: PPF0-7, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 290K
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 69.25500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 22.67500
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 22.67500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 103.88250
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 22.67500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 22.67500
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 34.62750
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 22.67500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 22.67500
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 103.88250
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 22.67500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 22.67500
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 34.62750
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 69.25500
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4520 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12360 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 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 350 BIOMT1 2 0.000000 1.000000 0.000000 -45.35000
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 45.35000
REMARK 350 BIOMT3 2 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 ALA A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 GLU A 152
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 HIS A 0 CG ND1 CD2 CE1 NE2
REMARK 470 MET A 1 CG SD CE
REMARK 470 LYS A 62 CG CD CE NZ
REMARK 470 GLU A 93 CG CD OE1 OE2
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 LYS A 62 -46.33 -132.40
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 511 DISTANCE = 6.20 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 5RP A 201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: SSGCID-MYGEA.00966.A RELATED DB: TARGETTRACK
DBREF 6MU0 A 1 152 UNP P47636 RPIB_MYCGE 1 152
SEQADV 6MU0 MET A -7 UNP P47636 INITIATING METHIONINE
SEQADV 6MU0 ALA A -6 UNP P47636 EXPRESSION TAG
SEQADV 6MU0 HIS A -5 UNP P47636 EXPRESSION TAG
SEQADV 6MU0 HIS A -4 UNP P47636 EXPRESSION TAG
SEQADV 6MU0 HIS A -3 UNP P47636 EXPRESSION TAG
SEQADV 6MU0 HIS A -2 UNP P47636 EXPRESSION TAG
SEQADV 6MU0 HIS A -1 UNP P47636 EXPRESSION TAG
SEQADV 6MU0 HIS A 0 UNP P47636 EXPRESSION TAG
SEQRES 1 A 160 MET ALA HIS HIS HIS HIS HIS HIS MET SER PHE ASN ILE
SEQRES 2 A 160 PHE ILE ALA SER ASP HIS THR GLY LEU THR LEU LYS LYS
SEQRES 3 A 160 ILE ILE SER GLU HIS LEU LYS THR LYS GLN PHE ASN VAL
SEQRES 4 A 160 VAL ASP LEU GLY PRO ASN TYR PHE ASP ALA ASN ASP ASP
SEQRES 5 A 160 TYR PRO ASP PHE ALA PHE LEU VAL ALA ASP LYS VAL LYS
SEQRES 6 A 160 LYS ASN SER ASP LYS ASP LEU GLY ILE LEU ILE CSD GLY
SEQRES 7 A 160 THR GLY VAL GLY VAL CYS MET ALA ALA ASN LYS VAL LYS
SEQRES 8 A 160 GLY VAL LEU ALA ALA LEU VAL VAL SER GLU LYS THR ALA
SEQRES 9 A 160 ALA LEU ALA ARG GLN HIS ASP ASN ALA ASN VAL LEU CYS
SEQRES 10 A 160 LEU SER SER ARG PHE VAL THR ASP SER GLU ASN ILE LYS
SEQRES 11 A 160 ILE VAL ASP ASP PHE LEU LYS ALA ASN PHE GLU GLY GLY
SEQRES 12 A 160 ARG HIS GLN ARG ARG ILE ASP LYS ILE ILE ARG TYR GLU
SEQRES 13 A 160 LYS GLU THR GLU
MODRES 6MU0 CSD A 69 CYS MODIFIED RESIDUE
HET CSD A 69 8
HET 5RP A 201 14
HETNAM CSD 3-SULFINOALANINE
HETNAM 5RP RIBULOSE-5-PHOSPHATE
HETSYN CSD S-CYSTEINESULFINIC ACID; S-SULFINOCYSTEINE
FORMUL 1 CSD C3 H7 N O4 S
FORMUL 2 5RP C5 H11 O8 P
FORMUL 3 HOH *211(H2 O)
HELIX 1 AA1 GLY A 13 LYS A 27 1 15
HELIX 2 AA2 ASP A 44 ASN A 59 1 16
HELIX 3 AA3 GLY A 72 LYS A 81 1 10
HELIX 4 AA4 SER A 92 HIS A 102 1 11
HELIX 5 AA5 THR A 116 ALA A 130 1 15
HELIX 6 AA6 GLY A 135 THR A 151 1 17
SHEET 1 AA1 5 ASN A 30 ASP A 33 0
SHEET 2 AA1 5 ASN A 4 SER A 9 1 N ILE A 5 O VAL A 32
SHEET 3 AA1 5 LEU A 64 CSD A 69 1 O LEU A 64 N PHE A 6
SHEET 4 AA1 5 VAL A 107 SER A 111 1 O LEU A 108 N GLY A 65
SHEET 5 AA1 5 ALA A 87 LEU A 89 1 N ALA A 88 O CYS A 109
LINK C ILE A 68 N CSD A 69 1555 1555 1.33
LINK C CSD A 69 N GLY A 70 1555 1555 1.34
CISPEP 1 GLY A 35 PRO A 36 0 -1.72
SITE 1 AC1 18 ASP A 10 HIS A 11 THR A 12 CSD A 69
SITE 2 AC1 18 GLY A 70 THR A 71 GLY A 74 HIS A 102
SITE 3 AC1 18 ASP A 103 ARG A 113 ARG A 136 ARG A 140
SITE 4 AC1 18 HOH A 312 HOH A 314 HOH A 357 HOH A 363
SITE 5 AC1 18 HOH A 410 HOH A 413
CRYST1 45.350 45.350 138.510 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 0.022051 0.000000 0.000000 0.00000
SCALE2 0.000000 0.022051 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007220 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
