HEADER TRANSFERASE 27-JAN-16 5HTV
TITLE PUTATIVE SUGAR KINASES FROM ARABIDOPSIS THALIANA IN COMPLEX WITH
TITLE 2 AMPPNP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE XYLULOSE KINASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 43-478;
COMPND 5 SYNONYM: XYLULOSE KINASE LIKE PROTEIN,XYLULOSE KINASE-1;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 3 ORGANISM_COMMON: MOUSE-EAR CRESS;
SOURCE 4 ORGANISM_TAXID: 3702;
SOURCE 5 GENE: XK-1, AT2G21370;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PMCSG7
KEYWDS PUTATIVE SUGAR KINASES, ARABIDOPSIS THALIANA, AMPPNP, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.XIE,M.LI,W.CHANG
REVDAT 2 20-MAR-24 5HTV 1 REMARK
REVDAT 1 08-JUN-16 5HTV 0
JRNL AUTH Y.XIE,M.LI,W.CHANG
JRNL TITL CRYSTAL STRUCTURES OF PUTATIVE SUGAR KINASES FROM
JRNL TITL 2 SYNECHOCOCCUS ELONGATUS PCC 7942 AND ARABIDOPSIS THALIANA
JRNL REF PLOS ONE V. 11 56067 2016
JRNL REFN ESSN 1932-6203
JRNL PMID 27223615
JRNL DOI 10.1371/JOURNAL.PONE.0156067
REMARK 2
REMARK 2 RESOLUTION. 1.78 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.78
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.40
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 45067
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.171
REMARK 3 R VALUE (WORKING SET) : 0.170
REMARK 3 FREE R VALUE : 0.204
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.430
REMARK 3 FREE R VALUE TEST SET COUNT : 1997
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 38.4042 - 4.2212 0.99 3149 146 0.1668 0.1993
REMARK 3 2 4.2212 - 3.3511 1.00 3086 143 0.1549 0.1682
REMARK 3 3 3.3511 - 2.9277 1.00 3104 146 0.1727 0.2024
REMARK 3 4 2.9277 - 2.6601 1.00 3111 140 0.1787 0.2214
REMARK 3 5 2.6601 - 2.4695 1.00 3102 142 0.1787 0.1997
REMARK 3 6 2.4695 - 2.3239 1.00 3066 150 0.1724 0.2217
REMARK 3 7 2.3239 - 2.2075 1.00 3106 132 0.1607 0.2365
REMARK 3 8 2.2075 - 2.1114 1.00 3098 148 0.1560 0.1846
REMARK 3 9 2.1114 - 2.0302 0.99 3043 143 0.1602 0.1745
REMARK 3 10 2.0302 - 1.9601 0.99 3064 148 0.1688 0.2305
REMARK 3 11 1.9601 - 1.8988 0.99 3042 138 0.1755 0.2192
REMARK 3 12 1.8988 - 1.8445 1.00 3077 141 0.1819 0.2367
REMARK 3 13 1.8445 - 1.7960 0.99 3065 146 0.1957 0.2273
REMARK 3 14 1.7960 - 1.7522 0.96 2957 134 0.2113 0.2556
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) : 0.150
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.480
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 : 0.007 3361
REMARK 3 ANGLE : 1.145 4573
REMARK 3 CHIRALITY : 0.042 513
REMARK 3 PLANARITY : 0.005 583
REMARK 3 DIHEDRAL : 12.725 1234
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 5HTV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-FEB-16.
REMARK 100 THE DEPOSITION ID IS D_1000217745.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-MAY-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97917
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 45097
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750
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 (%) : 99.5
REMARK 200 DATA REDUNDANCY : 4.100
REMARK 200 R MERGE (I) : 0.07300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.8100
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.81
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.00
REMARK 200 R MERGE FOR SHELL (I) : 0.50900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AUTOSOL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.15
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS PH 6.5, 20% W/V
REMARK 280 POLYETHYLENE GLYCOL MONOMETHYL ETHER 5,000, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 281K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 43.72700
REMARK 290 SMTRY3 2 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: 720 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17870 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -2.0 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 SER A -2
REMARK 465 ASN A -1
REMARK 465 ALA A 0
REMARK 465 VAL A 1
REMARK 465 MET A 2
REMARK 465 SER A 3
REMARK 465 GLY A 4
REMARK 465 ASN A 5
REMARK 465 LYS A 6
REMARK 465 GLY A 7
REMARK 465 THR A 8
REMARK 465 ASN A 9
REMARK 465 TYR A 10
REMARK 465 GLY A 435
REMARK 465 LEU A 436
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 O HOH A 752 O HOH A 761 1.98
REMARK 500 O HOH A 639 O HOH A 873 2.07
REMARK 500 O HOH A 852 O HOH A 874 2.09
REMARK 500 O HOH A 633 O HOH A 902 2.13
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 SER A 171 -168.52 -128.73
REMARK 500 ASP A 283 -124.25 50.63
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 ANP A 501
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5HTN RELATED DB: PDB
REMARK 900 RELATED ID: 5HTJ RELATED DB: PDB
REMARK 900 RELATED ID: 5HTP RELATED DB: PDB
REMARK 900 RELATED ID: 5HTR RELATED DB: PDB
REMARK 900 RELATED ID: 5HTX RELATED DB: PDB
REMARK 900 RELATED ID: 5HTY RELATED DB: PDB
REMARK 900 RELATED ID: 5HU2 RELATED DB: PDB
REMARK 900 RELATED ID: 5HUX RELATED DB: PDB
REMARK 900 RELATED ID: 5HV7 RELATED DB: PDB
DBREF 5HTV A 1 436 UNP Q8L794 Q8L794_ARATH 43 478
SEQADV 5HTV SER A -2 UNP Q8L794 EXPRESSION TAG
SEQADV 5HTV ASN A -1 UNP Q8L794 EXPRESSION TAG
SEQADV 5HTV ALA A 0 UNP Q8L794 EXPRESSION TAG
SEQRES 1 A 439 SER ASN ALA VAL MET SER GLY ASN LYS GLY THR ASN TYR
SEQRES 2 A 439 GLU LYS LEU TYR LEU GLY MET ASP PHE GLY THR SER GLY
SEQRES 3 A 439 GLY ARG PHE THR VAL ILE ASP GLU GLN GLY GLU ILE LYS
SEQRES 4 A 439 ALA GLN GLY LYS ARG GLU TYR PRO PRO PHE MET LYS GLU
SEQRES 5 A 439 GLU SER MET GLY TRP ALA SER SER TRP LYS ALA THR LEU
SEQRES 6 A 439 PHE SER LEU LEU GLU ASP ILE PRO VAL THR VAL ARG SER
SEQRES 7 A 439 LEU VAL SER SER ILE SER LEU ASP GLY THR SER ALA THR
SEQRES 8 A 439 THR LEU ILE LEU ASN SER GLU SER GLY GLU VAL LEU CYS
SEQRES 9 A 439 GLN PRO TYR LEU TYR ASN GLN SER CYS PRO ASP ALA LEU
SEQRES 10 A 439 PRO GLU VAL LYS SER ILE ALA PRO ALA ASN HIS THR VAL
SEQRES 11 A 439 CYS SER GLY THR SER THR LEU CYS LYS LEU VAL SER TRP
SEQRES 12 A 439 TRP ASN THR GLU VAL PRO ASN ARG GLU SER ALA VAL LEU
SEQRES 13 A 439 LEU HIS GLN ALA ASP TRP LEU LEU TRP LEU LEU HIS GLY
SEQRES 14 A 439 ARG LEU GLY VAL SER ASP TYR ASN ASN ALA LEU LYS VAL
SEQRES 15 A 439 GLY TYR ASP PRO GLU SER GLU SER TYR PRO SER TRP LEU
SEQRES 16 A 439 LEU GLY GLN PRO TYR SER GLN LEU LEU PRO LYS VAL GLN
SEQRES 17 A 439 ALA PRO GLY THR SER ILE GLY ASN LEU LYS GLU SER PHE
SEQRES 18 A 439 THR ARG GLN PHE GLY PHE PRO ASP ASP CYS ILE VAL CYS
SEQRES 19 A 439 THR GLY THR THR ASP SER ILE ALA ALA PHE LEU ALA ALA
SEQRES 20 A 439 ARG ALA THR GLU PRO GLY LYS ALA VAL THR SER LEU GLY
SEQRES 21 A 439 SER THR LEU ALA ILE LYS LEU LEU SER THR LYS ARG VAL
SEQRES 22 A 439 ASP ASP ALA ARG TYR GLY VAL TYR SER HIS ARG LEU ASP
SEQRES 23 A 439 ASP LYS TRP LEU VAL GLY GLY ALA SER ASN THR GLY GLY
SEQRES 24 A 439 ALA ILE LEU ARG GLN LEU PHE SER ASP GLU GLN LEU GLU
SEQRES 25 A 439 ARG LEU SER GLN GLU ILE ASN PRO MET VAL GLY SER PRO
SEQRES 26 A 439 LEU ASP TYR TYR PRO LEU GLN SER SER GLY GLU ARG PHE
SEQRES 27 A 439 PRO ILE ALA ASP PRO ASN LEU ALA PRO ARG LEU LEU PRO
SEQRES 28 A 439 ARG PRO GLU SER ASP VAL GLU PHE LEU HIS GLY ILE LEU
SEQRES 29 A 439 GLU SER ILE ALA ARG ILE GLU GLY LYS GLY TYR LYS LEU
SEQRES 30 A 439 LEU LYS GLU LEU GLY ALA THR GLU ALA GLU GLU VAL LEU
SEQRES 31 A 439 THR ALA GLY GLY GLY ALA LYS ASN ASP LYS TRP ILE LYS
SEQRES 32 A 439 ILE ARG GLN ARG VAL LEU GLY LEU PRO VAL LYS LYS ALA
SEQRES 33 A 439 VAL HIS THR GLU ALA SER TYR GLY ALA SER LEU LEU ALA
SEQRES 34 A 439 LEU LYS GLY ALA LYS GLN ASN SER GLY LEU
HET ANP A 501 31
HETNAM ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER
FORMUL 2 ANP C10 H17 N6 O12 P3
FORMUL 3 HOH *324(H2 O)
HELIX 1 AA1 GLY A 53 ILE A 69 1 17
HELIX 2 AA2 PRO A 70 SER A 75 1 6
HELIX 3 AA3 CYS A 110 ASP A 112 5 3
HELIX 4 AA4 ALA A 113 ALA A 121 1 9
HELIX 5 AA5 SER A 132 THR A 143 1 12
HELIX 6 AA6 ASN A 147 GLU A 149 5 3
HELIX 7 AA7 GLN A 156 GLY A 166 1 11
HELIX 8 AA8 ALA A 176 GLY A 180 5 5
HELIX 9 AA9 PRO A 189 GLY A 194 1 6
HELIX 10 AB1 GLN A 195 LEU A 201 5 7
HELIX 11 AB2 LYS A 215 GLY A 223 1 9
HELIX 12 AB3 ASP A 236 ALA A 243 1 8
HELIX 13 AB4 ASP A 272 GLY A 276 5 5
HELIX 14 AB5 GLY A 295 PHE A 303 1 9
HELIX 15 AB6 SER A 304 GLU A 314 1 11
HELIX 16 AB7 SER A 352 LEU A 378 1 27
HELIX 17 AB8 GLY A 390 LYS A 394 5 5
HELIX 18 AB9 ASN A 395 GLY A 407 1 13
HELIX 19 AC1 GLU A 417 SER A 434 1 18
SHEET 1 AA1 6 ILE A 35 GLU A 42 0
SHEET 2 AA1 6 GLY A 23 ILE A 29 -1 N VAL A 28 O LYS A 36
SHEET 3 AA1 6 LEU A 13 PHE A 19 -1 N GLY A 16 O THR A 27
SHEET 4 AA1 6 VAL A 77 GLY A 84 1 O SER A 78 N LEU A 13
SHEET 5 AA1 6 ILE A 229 CYS A 231 1 O CYS A 231 N ILE A 80
SHEET 6 AA1 6 SER A 210 ASN A 213 -1 N ILE A 211 O VAL A 230
SHEET 1 AA2 5 ILE A 35 GLU A 42 0
SHEET 2 AA2 5 GLY A 23 ILE A 29 -1 N VAL A 28 O LYS A 36
SHEET 3 AA2 5 LEU A 13 PHE A 19 -1 N GLY A 16 O THR A 27
SHEET 4 AA2 5 VAL A 77 GLY A 84 1 O SER A 78 N LEU A 13
SHEET 5 AA2 5 THR A 234 THR A 235 1 O THR A 234 N GLY A 84
SHEET 1 AA3 2 THR A 89 ASN A 93 0
SHEET 2 AA3 2 ALA A 151 HIS A 155 -1 O LEU A 154 N LEU A 90
SHEET 1 AA4 2 VAL A 170 ASP A 172 0
SHEET 2 AA4 2 LYS A 203 GLN A 205 1 O LYS A 203 N SER A 171
SHEET 1 AA5 6 TYR A 278 LEU A 282 0
SHEET 2 AA5 6 LYS A 285 SER A 292 -1 O LEU A 287 N HIS A 280
SHEET 3 AA5 6 LEU A 260 SER A 266 -1 N SER A 266 O TRP A 286
SHEET 4 AA5 6 LYS A 251 LEU A 256 -1 N SER A 255 O ALA A 261
SHEET 5 AA5 6 GLU A 385 ALA A 389 1 O LEU A 387 N ALA A 252
SHEET 6 AA5 6 VAL A 410 LYS A 412 1 O LYS A 411 N VAL A 386
CISPEP 1 PHE A 335 PRO A 336 0 5.67
CISPEP 2 LEU A 347 PRO A 348 0 -3.71
SITE 1 AC1 12 GLY A 257 SER A 258 GLY A 296 ARG A 300
SITE 2 AC1 12 ASP A 305 LEU A 308 GLY A 390 GLY A 391
SITE 3 AC1 12 LYS A 394 ASN A 395 TRP A 398 HOH A 636
CRYST1 49.565 87.454 53.364 90.00 96.78 90.00 P 1 21 1 2
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 0.020176 0.000000 0.002400 0.00000
SCALE2 0.000000 0.011435 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018871 0.00000
(ATOM LINES ARE NOT SHOWN.)
END