HEADER TRANSFERASE 27-JAN-16 5HTY
TITLE SUGAR KINASES FROM SYNECHOCOCCUS ELONGATUS PCC7942-D221A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROBABLE SUGAR KINASE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SYNECHOCOCCUS ELONGATUS (STRAIN PCC 7942);
SOURCE 3 ORGANISM_TAXID: 1140;
SOURCE 4 STRAIN: PCC 7942;
SOURCE 5 GENE: SYNPCC7942_2462;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS SUGAR KINASES, SYNECHOCOCCUS ELONGATUS PCC7942-D221A, MUTATION,
KEYWDS 2 TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.XIE,M.LI,W.CHANG
REVDAT 3 20-MAR-24 5HTY 1 REMARK
REVDAT 2 15-JUN-16 5HTY 1 REMARK
REVDAT 1 08-JUN-16 5HTY 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. 2.82 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) : 2.82
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.63
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 3 NUMBER OF REFLECTIONS : 10011
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.201
REMARK 3 R VALUE (WORKING SET) : 0.196
REMARK 3 FREE R VALUE : 0.245
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.960
REMARK 3 FREE R VALUE TEST SET COUNT : 997
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 32.6363 - 5.3785 0.99 1336 153 0.1661 0.1976
REMARK 3 2 5.3785 - 4.2721 1.00 1326 141 0.1723 0.2134
REMARK 3 3 4.2721 - 3.7329 1.00 1304 148 0.1820 0.2442
REMARK 3 4 3.7329 - 3.3920 1.00 1288 143 0.2074 0.2827
REMARK 3 5 3.3920 - 3.1491 1.00 1301 146 0.2149 0.2540
REMARK 3 6 3.1491 - 2.9636 1.00 1281 142 0.2456 0.2842
REMARK 3 7 2.9636 - 2.8152 0.89 1178 124 0.2600 0.3423
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) : 0.230
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.220
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 : 0.002 3280
REMARK 3 ANGLE : 0.635 4483
REMARK 3 CHIRALITY : 0.024 500
REMARK 3 PLANARITY : 0.003 589
REMARK 3 DIHEDRAL : 12.337 1170
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): 26.6440 4.2683 21.2908
REMARK 3 T TENSOR
REMARK 3 T11: 0.1831 T22: 0.2146
REMARK 3 T33: 0.2180 T12: 0.0252
REMARK 3 T13: -0.0230 T23: -0.0114
REMARK 3 L TENSOR
REMARK 3 L11: 0.4876 L22: 1.0827
REMARK 3 L33: 1.4921 L12: 0.2341
REMARK 3 L13: -0.4877 L23: -0.1685
REMARK 3 S TENSOR
REMARK 3 S11: -0.0450 S12: 0.0698 S13: -0.0234
REMARK 3 S21: -0.1787 S22: -0.0199 S23: 0.0135
REMARK 3 S31: 0.0478 S32: -0.0998 S33: 0.0532
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 5HTY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-FEB-16.
REMARK 100 THE DEPOSITION ID IS D_1000217749.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-JAN-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) : 0.97916
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 : 10021
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
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 (%) : 99.9
REMARK 200 DATA REDUNDANCY : 7.000
REMARK 200 R MERGE (I) : 0.14300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.9400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.40
REMARK 200 R MERGE FOR SHELL (I) : 0.46800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.480
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 (%): 45.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.25
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M BIS-TRIS PH 6.5, 20% W/V
REMARK 280 POLYETHYLENE GLYCOL MONOMETHYL ETHER 5000, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 281K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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 48.94350
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 23.60300
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 48.94350
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 23.60300
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: 0 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17860 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 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 MET A -1
REMARK 465 GLY A 0
REMARK 465 MET A 1
REMARK 465 GLY A 422
REMARK 465 LEU A 423
REMARK 465 LYS A 424
REMARK 465 ARG A 425
REMARK 465 THR A 426
REMARK 465 LEU A 427
REMARK 465 GLU A 428
REMARK 465 HIS A 429
REMARK 465 HIS A 430
REMARK 465 HIS A 431
REMARK 465 HIS A 432
REMARK 465 HIS A 433
REMARK 465 HIS A 434
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 39 65.42 -159.62
REMARK 500 LEU A 113 42.07 -88.16
REMARK 500 THR A 219 -162.05 -164.07
REMARK 500 LEU A 415 39.20 -97.62
REMARK 500 PHE A 418 46.79 -89.46
REMARK 500
REMARK 500 REMARK: NULL
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: 5HTV RELATED DB: PDB
REMARK 900 RELATED ID: 5HTX 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 5HTY A 1 426 UNP Q31KC7 Q31KC7_SYNE7 1 426
SEQADV 5HTY MET A -1 UNP Q31KC7 EXPRESSION TAG
SEQADV 5HTY GLY A 0 UNP Q31KC7 EXPRESSION TAG
SEQADV 5HTY ALA A 221 UNP Q31KC7 ASP 221 ENGINEERED MUTATION
SEQADV 5HTY LEU A 427 UNP Q31KC7 EXPRESSION TAG
SEQADV 5HTY GLU A 428 UNP Q31KC7 EXPRESSION TAG
SEQADV 5HTY HIS A 429 UNP Q31KC7 EXPRESSION TAG
SEQADV 5HTY HIS A 430 UNP Q31KC7 EXPRESSION TAG
SEQADV 5HTY HIS A 431 UNP Q31KC7 EXPRESSION TAG
SEQADV 5HTY HIS A 432 UNP Q31KC7 EXPRESSION TAG
SEQADV 5HTY HIS A 433 UNP Q31KC7 EXPRESSION TAG
SEQADV 5HTY HIS A 434 UNP Q31KC7 EXPRESSION TAG
SEQRES 1 A 436 MET GLY MET VAL VAL ALA LEU GLY LEU ASP PHE GLY THR
SEQRES 2 A 436 SER GLY ALA ARG ALA ILE ALA CYS ASP PHE ASP SER ASP
SEQRES 3 A 436 ARG SER VAL SER VAL SER VAL THR PHE PRO LYS THR SER
SEQRES 4 A 436 GLN ASN TRP PRO GLN VAL TRP ARG GLU ALA LEU TRP GLN
SEQRES 5 A 436 LEU LEU THR GLN ILE PRO ALA ASP TRP ARG SER ARG ILE
SEQRES 6 A 436 GLU ARG ILE ALA ILE ASP GLY THR SER GLY THR VAL LEU
SEQRES 7 A 436 LEU CYS ASP ARG GLU GLY GLN PRO GLN THR GLU PRO LEU
SEQRES 8 A 436 LEU TYR ASN GLN ALA CYS PRO ILE ASP LEU ALA ASP LEU
SEQRES 9 A 436 ALA ASP TRP VAL PRO ALA ASP HIS ALA ALA LEU SER SER
SEQRES 10 A 436 THR SER SER LEU ALA LYS LEU TRP PHE TRP GLN GLN GLN
SEQRES 11 A 436 PHE GLY ALA LEU PRO PRO ASP TRP GLN ILE LEU ALA GLN
SEQRES 12 A 436 ALA ASP TRP LEU SER LEU GLN LEU HIS GLY CYS SER GLN
SEQRES 13 A 436 GLN SER ASP TYR HIS ASN ALA LEU LYS LEU GLY TYR SER
SEQRES 14 A 436 PRO ASP ARG GLU ARG PHE SER LYS ASN LEU LEU ASP SER
SEQRES 15 A 436 GLU LEU GLY ALA LEU LEU PRO VAL VAL HIS GLU PRO GLY
SEQRES 16 A 436 VAL ALA ILE GLY PRO ILE LEU PRO ALA ILE ALA GLN GLU
SEQRES 17 A 436 PHE GLY LEU SER PRO ASP CYS GLN ILE CYS ALA GLY THR
SEQRES 18 A 436 THR ALA SER ILE ALA ALA PHE LEU ALA SER GLY ALA HIS
SEQRES 19 A 436 GLN PRO GLY GLU ALA VAL THR SER LEU GLY SER THR ILE
SEQRES 20 A 436 VAL LEU LYS LEU LEU SER GLN VAL ALA VAL SER ASP ARG
SEQRES 21 A 436 LEU THR GLY VAL TYR SER HIS LYS LEU GLY GLY TYR TRP
SEQRES 22 A 436 LEU THR GLY GLY ALA SER ASN CYS GLY GLY ALA THR LEU
SEQRES 23 A 436 ARG GLN PHE PHE PRO ASP THR GLU LEU GLU SER LEU SER
SEQRES 24 A 436 CYS GLN ILE ASP PRO THR LYS LYS SER GLY LEU ASP TYR
SEQRES 25 A 436 TYR PRO LEU PRO SER ARG GLY GLU ARG PHE PRO ILE ALA
SEQRES 26 A 436 ASP PRO ASP ARG LEU PRO GLN LEU GLU PRO ARG PRO GLU
SEQRES 27 A 436 ASN PRO VAL GLN PHE LEU GLN GLY LEU LEU GLU GLY LEU
SEQRES 28 A 436 THR GLN VAL GLU THR LEU GLY TYR GLN ARG LEU GLN ASP
SEQRES 29 A 436 LEU GLY ALA THR PRO LEU LYS ARG ILE TRP THR ALA GLY
SEQRES 30 A 436 GLY GLY ALA LYS ASN ALA VAL TRP GLN GLN LEU ARG GLN
SEQRES 31 A 436 GLN ALA ILE GLY VAL PRO ILE ALA ILE ALA PRO ASN THR
SEQRES 32 A 436 GLU ALA ALA PHE GLY THR ALA ARG LEU ALA ALA PHE GLY
SEQRES 33 A 436 LEU ALA ALA PHE HIS SER ALA GLY LEU LYS ARG THR LEU
SEQRES 34 A 436 GLU HIS HIS HIS HIS HIS HIS
HELIX 1 AA1 ASN A 39 ILE A 55 1 17
HELIX 2 AA2 PRO A 56 SER A 61 1 6
HELIX 3 AA3 ASP A 98 ALA A 103 5 6
HELIX 4 AA4 SER A 117 GLY A 130 1 14
HELIX 5 AA5 GLN A 141 GLY A 151 1 11
HELIX 6 AA6 ALA A 161 GLY A 165 5 5
HELIX 7 AA7 SER A 174 SER A 180 1 7
HELIX 8 AA8 LEU A 200 PHE A 207 1 8
HELIX 9 AA9 ALA A 221 ALA A 228 1 8
HELIX 10 AB1 GLY A 280 ARG A 285 1 6
HELIX 11 AB2 PRO A 289 CYS A 298 1 10
HELIX 12 AB3 ASN A 337 LEU A 363 1 27
HELIX 13 AB4 GLY A 375 LYS A 379 5 5
HELIX 14 AB5 ASN A 380 GLY A 392 1 13
HELIX 15 AB6 GLU A 402 GLY A 414 1 13
SHEET 1 AA1 6 ARG A 25 THR A 32 0
SHEET 2 AA1 6 GLY A 13 ASP A 20 -1 N ALA A 14 O VAL A 31
SHEET 3 AA1 6 VAL A 3 PHE A 9 -1 N ASP A 8 O ARG A 15
SHEET 4 AA1 6 ARG A 65 GLY A 70 1 O ASP A 69 N LEU A 7
SHEET 5 AA1 6 GLN A 214 CYS A 216 1 O CYS A 216 N ILE A 66
SHEET 6 AA1 6 ALA A 195 PRO A 198 -1 N GLY A 197 O ILE A 215
SHEET 1 AA2 5 ARG A 25 THR A 32 0
SHEET 2 AA2 5 GLY A 13 ASP A 20 -1 N ALA A 14 O VAL A 31
SHEET 3 AA2 5 VAL A 3 PHE A 9 -1 N ASP A 8 O ARG A 15
SHEET 4 AA2 5 ARG A 65 GLY A 70 1 O ASP A 69 N LEU A 7
SHEET 5 AA2 5 THR A 219 THR A 220 1 O THR A 219 N GLY A 70
SHEET 1 AA3 2 VAL A 75 CYS A 78 0
SHEET 2 AA3 2 GLN A 137 ALA A 140 -1 O GLN A 137 N CYS A 78
SHEET 1 AA4 2 GLN A 155 ASP A 157 0
SHEET 2 AA4 2 VAL A 188 HIS A 190 1 O HIS A 190 N SER A 156
SHEET 1 AA5 6 HIS A 265 LEU A 267 0
SHEET 2 AA5 6 TYR A 270 ALA A 276 -1 O TYR A 270 N LEU A 267
SHEET 3 AA5 6 ILE A 245 SER A 251 -1 N SER A 251 O TRP A 271
SHEET 4 AA5 6 GLU A 236 LEU A 241 -1 N SER A 240 O VAL A 246
SHEET 5 AA5 6 ARG A 370 ALA A 374 1 O ALA A 374 N LEU A 241
SHEET 6 AA5 6 ILE A 395 ILE A 397 1 O ALA A 396 N THR A 373
CISPEP 1 SER A 23 ASP A 24 0 -2.97
CISPEP 2 PHE A 320 PRO A 321 0 2.77
CISPEP 3 GLU A 332 PRO A 333 0 0.84
CRYST1 97.887 47.206 89.835 90.00 91.58 90.00 C 1 2 1 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 0.010216 0.000000 0.000283 0.00000
SCALE2 0.000000 0.021184 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011136 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
