HEADER TRANSFERASE 23-APR-09 3H6E
TITLE THE CRYSTAL STRUCTURE OF A CARBOHYDRATE KINASE FROM NOVOSPHINGOBIUM
TITLE 2 AROMATICIVORANS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBOHYDRATE KINASE, FGGY;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: NOVOSPHINGOBIUM AROMATICIVORANS;
SOURCE 3 ORGANISM_TAXID: 279238;
SOURCE 4 STRAIN: DSM 12444;
SOURCE 5 GENE: SARO_1051;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-CODON+RIL - STRATAGENE;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: BC-PSGX3(BC)
KEYWDS CARBOHYDRATE KINASE, NOVOSPHINGOBIUM AROMATICIVORANS, STRAIN DSM
KEYWDS 2 12444, SGX, 11200I, KINASE, TRANSFERASE, STRUCTURAL GENOMICS, PSI-2,
KEYWDS 3 PROTEIN STRUCTURE INITIATIVE, NEW YORK SGX RESEARCH CENTER FOR
KEYWDS 4 STRUCTURAL GENOMICS, NYSGXRC
EXPDTA X-RAY DIFFRACTION
AUTHOR Z.ZHANG,S.K.BURLEY,S.SWAMINATHAN,NEW YORK SGX RESEARCH CENTER FOR
AUTHOR 2 STRUCTURAL GENOMICS (NYSGXRC)
REVDAT 3 10-FEB-21 3H6E 1 AUTHOR JRNL LINK
REVDAT 2 13-JUL-11 3H6E 1 VERSN
REVDAT 1 02-JUN-09 3H6E 0
JRNL AUTH Z.ZHANG,S.K.BURLEY,S.SWAMINATHAN
JRNL TITL THE CRYSTAL STRUCTURE OF CARBOHYDRATE KINASE FROM
JRNL TITL 2 NOVOSPHINGOBIUM AROMATICIVORANS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.50 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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 51.28
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.140
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 34918
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.223
REMARK 3 R VALUE (WORKING SET) : 0.220
REMARK 3 FREE R VALUE : 0.274
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030
REMARK 3 FREE R VALUE TEST SET COUNT : 1755
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 51.2903 - 5.8757 0.99 2754 127 0.2302 0.2416
REMARK 3 2 5.8757 - 4.6647 1.00 2638 132 0.1915 0.2593
REMARK 3 3 4.6647 - 4.0754 1.00 2548 132 0.1764 0.2272
REMARK 3 4 4.0754 - 3.7029 1.00 2561 139 0.1922 0.2475
REMARK 3 5 3.7029 - 3.4375 1.00 2570 130 0.2073 0.2603
REMARK 3 6 3.4375 - 3.2349 1.00 2479 179 0.2221 0.2553
REMARK 3 7 3.2349 - 3.0729 1.00 2519 158 0.2326 0.3032
REMARK 3 8 3.0729 - 2.9392 1.00 2502 125 0.2405 0.3132
REMARK 3 9 2.9392 - 2.8260 1.00 2544 118 0.2381 0.3015
REMARK 3 10 2.8260 - 2.7285 1.00 2543 116 0.2444 0.3155
REMARK 3 11 2.7285 - 2.6432 1.00 2511 126 0.2481 0.3321
REMARK 3 12 2.6432 - 2.5676 1.00 2532 131 0.2401 0.3211
REMARK 3 13 2.5676 - 2.5001 1.00 2462 142 0.2198 0.2892
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.36
REMARK 3 B_SOL : 36.76
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.370
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.250
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 38.41
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.29
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -6.41130
REMARK 3 B22 (A**2) : -0.35040
REMARK 3 B33 (A**2) : 6.76170
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 7318
REMARK 3 ANGLE : 0.833 10004
REMARK 3 CHIRALITY : 0.057 1125
REMARK 3 PLANARITY : 0.003 1313
REMARK 3 DIHEDRAL : 16.721 2630
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 3H6E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-MAY-09.
REMARK 100 THE DEPOSITION ID IS D_1000052749.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-APR-09
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 : NSLS
REMARK 200 BEAMLINE : X29A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35006
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 114.710
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 13.70
REMARK 200 R MERGE (I) : 0.08200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 29.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.64
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 13.80
REMARK 200 R MERGE FOR SHELL (I) : 0.19100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 11.50
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.41
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M MAGNESESIUM CHLORIDE
REMARK 280 HEXAHYDRATE, 0.1 M BIS-TRIS PH 6.5, 25% W/V PEG 3350, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 291K
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 26.30700
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 114.56700
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.59900
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 114.56700
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.30700
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 40.59900
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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 MSE A -1
REMARK 465 SER A 0
REMARK 465 LEU A 1
REMARK 465 SER A 2
REMARK 465 THR A 3
REMARK 465 GLY A 4
REMARK 465 ALA A 5
REMARK 465 GLY A 450
REMARK 465 SER A 451
REMARK 465 TRP A 452
REMARK 465 ALA A 453
REMARK 465 ALA A 468
REMARK 465 ALA A 469
REMARK 465 LYS A 470
REMARK 465 VAL A 471
REMARK 465 GLU A 472
REMARK 465 GLU A 473
REMARK 465 GLY A 474
REMARK 465 HIS A 475
REMARK 465 HIS A 476
REMARK 465 HIS A 477
REMARK 465 HIS A 478
REMARK 465 HIS A 479
REMARK 465 HIS A 480
REMARK 465 MSE B -1
REMARK 465 SER B 0
REMARK 465 ASN B 421
REMARK 465 ASP B 422
REMARK 465 VAL B 423
REMARK 465 SER B 451
REMARK 465 GLU B 472
REMARK 465 GLU B 473
REMARK 465 GLY B 474
REMARK 465 HIS B 475
REMARK 465 HIS B 476
REMARK 465 HIS B 477
REMARK 465 HIS B 478
REMARK 465 HIS B 479
REMARK 465 HIS B 480
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 VAL B 471 CG1 CG2
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 ARG A 33 117.20 173.77
REMARK 500 ILE A 40 -26.85 -145.19
REMARK 500 ASP A 41 10.69 -161.15
REMARK 500 PHE A 89 161.77 179.59
REMARK 500 ASP A 123 -126.25 53.97
REMARK 500 HIS A 138 59.34 -141.81
REMARK 500 HIS A 172 61.68 35.97
REMARK 500 ASP A 174 -4.88 73.54
REMARK 500 GLU A 215 -73.28 -67.79
REMARK 500 ILE A 245 -74.47 -92.84
REMARK 500 ALA A 246 -111.46 44.21
REMARK 500 GLU A 307 -53.90 70.97
REMARK 500 ARG A 342 127.73 -39.43
REMARK 500 ALA A 353 145.50 -179.03
REMARK 500 ARG A 409 73.01 -112.34
REMARK 500 PRO A 437 -177.79 -68.12
REMARK 500 ASP B 47 35.44 86.26
REMARK 500 PHE B 89 166.97 177.83
REMARK 500 ASP B 123 -132.76 54.07
REMARK 500 HIS B 172 54.97 35.78
REMARK 500 ASP B 174 -7.00 81.00
REMARK 500 LEU B 210 122.72 -38.79
REMARK 500 ILE B 245 -71.44 -88.84
REMARK 500 ALA B 246 -105.21 46.46
REMARK 500 GLU B 307 -45.21 69.45
REMARK 500 ILE B 315 106.54 -57.30
REMARK 500 ASN B 418 77.89 -162.95
REMARK 500 ALA B 419 152.55 177.23
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: NYSGXRC-11200I RELATED DB: TARGETDB
DBREF 3H6E A 2 472 UNP Q2G9H7 Q2G9H7_NOVAD 2 472
DBREF 3H6E B 2 472 UNP Q2G9H7 Q2G9H7_NOVAD 2 472
SEQADV 3H6E MSE A -1 UNP Q2G9H7 EXPRESSION TAG
SEQADV 3H6E SER A 0 UNP Q2G9H7 EXPRESSION TAG
SEQADV 3H6E LEU A 1 UNP Q2G9H7 EXPRESSION TAG
SEQADV 3H6E GLU A 473 UNP Q2G9H7 EXPRESSION TAG
SEQADV 3H6E GLY A 474 UNP Q2G9H7 EXPRESSION TAG
SEQADV 3H6E HIS A 475 UNP Q2G9H7 EXPRESSION TAG
SEQADV 3H6E HIS A 476 UNP Q2G9H7 EXPRESSION TAG
SEQADV 3H6E HIS A 477 UNP Q2G9H7 EXPRESSION TAG
SEQADV 3H6E HIS A 478 UNP Q2G9H7 EXPRESSION TAG
SEQADV 3H6E HIS A 479 UNP Q2G9H7 EXPRESSION TAG
SEQADV 3H6E HIS A 480 UNP Q2G9H7 EXPRESSION TAG
SEQADV 3H6E MSE B -1 UNP Q2G9H7 EXPRESSION TAG
SEQADV 3H6E SER B 0 UNP Q2G9H7 EXPRESSION TAG
SEQADV 3H6E LEU B 1 UNP Q2G9H7 EXPRESSION TAG
SEQADV 3H6E GLU B 473 UNP Q2G9H7 EXPRESSION TAG
SEQADV 3H6E GLY B 474 UNP Q2G9H7 EXPRESSION TAG
SEQADV 3H6E HIS B 475 UNP Q2G9H7 EXPRESSION TAG
SEQADV 3H6E HIS B 476 UNP Q2G9H7 EXPRESSION TAG
SEQADV 3H6E HIS B 477 UNP Q2G9H7 EXPRESSION TAG
SEQADV 3H6E HIS B 478 UNP Q2G9H7 EXPRESSION TAG
SEQADV 3H6E HIS B 479 UNP Q2G9H7 EXPRESSION TAG
SEQADV 3H6E HIS B 480 UNP Q2G9H7 EXPRESSION TAG
SEQRES 1 A 482 MSE SER LEU SER THR GLY ALA THR ILE VAL ILE ASP LEU
SEQRES 2 A 482 GLY LYS THR LEU SER LYS VAL SER LEU TRP ASP LEU ASP
SEQRES 3 A 482 GLY ARG MSE LEU ASP ARG GLN VAL ARG PRO SER ILE PRO
SEQRES 4 A 482 LEU GLU ILE ASP GLY ILE ARG ARG LEU ASP ALA PRO ASP
SEQRES 5 A 482 THR GLY ARG TRP LEU LEU ASP VAL LEU SER ARG TYR ALA
SEQRES 6 A 482 ASP HIS PRO VAL THR THR ILE VAL PRO VAL GLY HIS GLY
SEQRES 7 A 482 ALA GLY ILE ALA ALA LEU THR ASP GLY ARG LEU ALA PHE
SEQRES 8 A 482 PRO PRO LEU ASP TYR GLU GLN SER ILE PRO GLU ALA VAL
SEQRES 9 A 482 MSE ALA ASP TYR ARG SER GLN ARG ASP PRO PHE ALA ARG
SEQRES 10 A 482 THR GLY SER PRO ALA LEU PRO ASP GLY LEU ASN ILE GLY
SEQRES 11 A 482 SER GLN LEU TRP TRP LEU ASP GLN LEU HIS PRO ASP VAL
SEQRES 12 A 482 MSE ALA ASN ALA THR LEU LEU PRO TRP ALA GLN TYR TRP
SEQRES 13 A 482 ALA TRP PHE LEU THR GLY ARG ALA VAL SER GLU VAL THR
SEQRES 14 A 482 SER LEU GLY CYS HIS SER ASP LEU TRP ASP PRO GLN ASP
SEQRES 15 A 482 GLY ASP PHE SER PRO MSE ALA LYS ARG LEU GLY TRP ALA
SEQRES 16 A 482 ALA ARG PHE ALA PRO ILE VAL ARG ALA GLY ASP THR VAL
SEQRES 17 A 482 GLY ALA LEU LEU PRO ALA ILE ALA GLU ARG THR GLY LEU
SEQRES 18 A 482 SER PRO ASP VAL GLN VAL LEU ALA GLY LEU HIS ASP SER
SEQRES 19 A 482 ASN ALA ALA LEU LEU ALA ALA ARG GLY PHE ALA GLU ILE
SEQRES 20 A 482 ALA ASP ASN GLU ALA THR VAL LEU SER THR GLY THR TRP
SEQRES 21 A 482 PHE ILE ALA MSE ARG LEU PRO ALA THR PRO VAL ASP THR
SEQRES 22 A 482 ALA THR LEU PRO GLU ALA ARG ASP CYS LEU VAL ASN VAL
SEQRES 23 A 482 ASP VAL HIS GLY ARG PRO VAL PRO SER ALA ARG PHE MSE
SEQRES 24 A 482 GLY GLY ARG GLU ILE GLU THR LEU ILE GLU ILE ASP THR
SEQRES 25 A 482 ARG ARG VAL ASP ILE LYS PRO ASP GLN PRO ALA LEU LEU
SEQRES 26 A 482 ALA ALA VAL PRO GLU VAL LEU ARG HIS GLY ARG MSE ILE
SEQRES 27 A 482 LEU PRO THR LEU MSE ARG GLY PHE GLY PRO TYR PRO HIS
SEQRES 28 A 482 GLY ARG PHE ALA TRP ILE ASN ARG PRO GLU ASP TRP PHE
SEQRES 29 A 482 GLU ARG ARG ALA ALA ALA CYS LEU TYR ALA ALA LEU VAL
SEQRES 30 A 482 ALA ASP THR ALA LEU ASP LEU ILE GLY SER THR GLY ARG
SEQRES 31 A 482 ILE LEU VAL GLU GLY ARG PHE ALA GLU ALA ASP VAL PHE
SEQRES 32 A 482 VAL ARG ALA LEU ALA SER LEU ARG PRO ASP CYS ALA VAL
SEQRES 33 A 482 TYR THR ALA ASN ALA HIS ASN ASP VAL SER PHE GLY ALA
SEQRES 34 A 482 LEU ARG LEU ILE ASP PRO GLY LEU ARG PRO GLN GLY GLU
SEQRES 35 A 482 LEU VAL ARG ILE GLU PRO LEU ASP THR GLY SER TRP ALA
SEQRES 36 A 482 ASP LEU ASP THR TYR ARG ASN ARG TRP GLN ALA GLU VAL
SEQRES 37 A 482 GLU ALA ALA LYS VAL GLU GLU GLY HIS HIS HIS HIS HIS
SEQRES 38 A 482 HIS
SEQRES 1 B 482 MSE SER LEU SER THR GLY ALA THR ILE VAL ILE ASP LEU
SEQRES 2 B 482 GLY LYS THR LEU SER LYS VAL SER LEU TRP ASP LEU ASP
SEQRES 3 B 482 GLY ARG MSE LEU ASP ARG GLN VAL ARG PRO SER ILE PRO
SEQRES 4 B 482 LEU GLU ILE ASP GLY ILE ARG ARG LEU ASP ALA PRO ASP
SEQRES 5 B 482 THR GLY ARG TRP LEU LEU ASP VAL LEU SER ARG TYR ALA
SEQRES 6 B 482 ASP HIS PRO VAL THR THR ILE VAL PRO VAL GLY HIS GLY
SEQRES 7 B 482 ALA GLY ILE ALA ALA LEU THR ASP GLY ARG LEU ALA PHE
SEQRES 8 B 482 PRO PRO LEU ASP TYR GLU GLN SER ILE PRO GLU ALA VAL
SEQRES 9 B 482 MSE ALA ASP TYR ARG SER GLN ARG ASP PRO PHE ALA ARG
SEQRES 10 B 482 THR GLY SER PRO ALA LEU PRO ASP GLY LEU ASN ILE GLY
SEQRES 11 B 482 SER GLN LEU TRP TRP LEU ASP GLN LEU HIS PRO ASP VAL
SEQRES 12 B 482 MSE ALA ASN ALA THR LEU LEU PRO TRP ALA GLN TYR TRP
SEQRES 13 B 482 ALA TRP PHE LEU THR GLY ARG ALA VAL SER GLU VAL THR
SEQRES 14 B 482 SER LEU GLY CYS HIS SER ASP LEU TRP ASP PRO GLN ASP
SEQRES 15 B 482 GLY ASP PHE SER PRO MSE ALA LYS ARG LEU GLY TRP ALA
SEQRES 16 B 482 ALA ARG PHE ALA PRO ILE VAL ARG ALA GLY ASP THR VAL
SEQRES 17 B 482 GLY ALA LEU LEU PRO ALA ILE ALA GLU ARG THR GLY LEU
SEQRES 18 B 482 SER PRO ASP VAL GLN VAL LEU ALA GLY LEU HIS ASP SER
SEQRES 19 B 482 ASN ALA ALA LEU LEU ALA ALA ARG GLY PHE ALA GLU ILE
SEQRES 20 B 482 ALA ASP ASN GLU ALA THR VAL LEU SER THR GLY THR TRP
SEQRES 21 B 482 PHE ILE ALA MSE ARG LEU PRO ALA THR PRO VAL ASP THR
SEQRES 22 B 482 ALA THR LEU PRO GLU ALA ARG ASP CYS LEU VAL ASN VAL
SEQRES 23 B 482 ASP VAL HIS GLY ARG PRO VAL PRO SER ALA ARG PHE MSE
SEQRES 24 B 482 GLY GLY ARG GLU ILE GLU THR LEU ILE GLU ILE ASP THR
SEQRES 25 B 482 ARG ARG VAL ASP ILE LYS PRO ASP GLN PRO ALA LEU LEU
SEQRES 26 B 482 ALA ALA VAL PRO GLU VAL LEU ARG HIS GLY ARG MSE ILE
SEQRES 27 B 482 LEU PRO THR LEU MSE ARG GLY PHE GLY PRO TYR PRO HIS
SEQRES 28 B 482 GLY ARG PHE ALA TRP ILE ASN ARG PRO GLU ASP TRP PHE
SEQRES 29 B 482 GLU ARG ARG ALA ALA ALA CYS LEU TYR ALA ALA LEU VAL
SEQRES 30 B 482 ALA ASP THR ALA LEU ASP LEU ILE GLY SER THR GLY ARG
SEQRES 31 B 482 ILE LEU VAL GLU GLY ARG PHE ALA GLU ALA ASP VAL PHE
SEQRES 32 B 482 VAL ARG ALA LEU ALA SER LEU ARG PRO ASP CYS ALA VAL
SEQRES 33 B 482 TYR THR ALA ASN ALA HIS ASN ASP VAL SER PHE GLY ALA
SEQRES 34 B 482 LEU ARG LEU ILE ASP PRO GLY LEU ARG PRO GLN GLY GLU
SEQRES 35 B 482 LEU VAL ARG ILE GLU PRO LEU ASP THR GLY SER TRP ALA
SEQRES 36 B 482 ASP LEU ASP THR TYR ARG ASN ARG TRP GLN ALA GLU VAL
SEQRES 37 B 482 GLU ALA ALA LYS VAL GLU GLU GLY HIS HIS HIS HIS HIS
SEQRES 38 B 482 HIS
MODRES 3H6E MSE A 27 MET SELENOMETHIONINE
MODRES 3H6E MSE A 103 MET SELENOMETHIONINE
MODRES 3H6E MSE A 142 MET SELENOMETHIONINE
MODRES 3H6E MSE A 186 MET SELENOMETHIONINE
MODRES 3H6E MSE A 262 MET SELENOMETHIONINE
MODRES 3H6E MSE A 297 MET SELENOMETHIONINE
MODRES 3H6E MSE A 335 MET SELENOMETHIONINE
MODRES 3H6E MSE A 341 MET SELENOMETHIONINE
MODRES 3H6E MSE B 27 MET SELENOMETHIONINE
MODRES 3H6E MSE B 103 MET SELENOMETHIONINE
MODRES 3H6E MSE B 142 MET SELENOMETHIONINE
MODRES 3H6E MSE B 186 MET SELENOMETHIONINE
MODRES 3H6E MSE B 262 MET SELENOMETHIONINE
MODRES 3H6E MSE B 297 MET SELENOMETHIONINE
MODRES 3H6E MSE B 335 MET SELENOMETHIONINE
MODRES 3H6E MSE B 341 MET SELENOMETHIONINE
HET MSE A 27 8
HET MSE A 103 8
HET MSE A 142 8
HET MSE A 186 8
HET MSE A 262 8
HET MSE A 297 8
HET MSE A 335 8
HET MSE A 341 8
HET MSE B 27 8
HET MSE B 103 8
HET MSE B 142 8
HET MSE B 186 8
HET MSE B 262 8
HET MSE B 297 8
HET MSE B 335 8
HET MSE B 341 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 16(C5 H11 N O2 SE)
FORMUL 3 HOH *321(H2 O)
HELIX 1 1 ASP A 47 TYR A 62 1 16
HELIX 2 2 PRO A 99 SER A 108 1 10
HELIX 3 3 PRO A 112 GLY A 117 1 6
HELIX 4 4 ASN A 126 HIS A 138 1 13
HELIX 5 5 HIS A 138 ASN A 144 1 7
HELIX 6 6 TRP A 150 LEU A 158 1 9
HELIX 7 7 VAL A 166 GLY A 170 1 5
HELIX 8 8 SER A 184 LEU A 190 1 7
HELIX 9 9 TRP A 192 PHE A 196 5 5
HELIX 10 10 LEU A 210 GLY A 218 1 9
HELIX 11 11 ASP A 231 ARG A 240 1 10
HELIX 12 12 ASP A 270 LEU A 274 5 5
HELIX 13 13 PRO A 275 ARG A 278 5 4
HELIX 14 14 MSE A 297 GLU A 307 1 11
HELIX 15 15 ILE A 308 ARG A 312 5 5
HELIX 16 16 ILE A 315 PRO A 317 5 3
HELIX 17 17 ASP A 318 ALA A 325 1 8
HELIX 18 18 ALA A 325 HIS A 332 1 8
HELIX 19 19 ASP A 360 ILE A 383 1 24
HELIX 20 20 GLY A 393 GLU A 397 5 5
HELIX 21 21 ALA A 398 ARG A 409 1 12
HELIX 22 22 SER A 424 GLY A 426 5 3
HELIX 23 23 ALA A 427 ASP A 432 1 6
HELIX 24 24 ASP A 454 GLU A 467 1 14
HELIX 25 25 ASP B 47 SER B 60 1 14
HELIX 26 26 ARG B 61 ALA B 63 5 3
HELIX 27 27 PRO B 99 SER B 108 1 10
HELIX 28 28 PRO B 112 GLY B 117 1 6
HELIX 29 29 ASN B 126 HIS B 138 1 13
HELIX 30 30 HIS B 138 ASN B 144 1 7
HELIX 31 31 TRP B 150 GLY B 160 1 11
HELIX 32 32 GLU B 165 GLY B 170 1 6
HELIX 33 33 SER B 184 LEU B 190 1 7
HELIX 34 34 TRP B 192 PHE B 196 5 5
HELIX 35 35 LEU B 210 GLY B 218 1 9
HELIX 36 36 ASP B 231 ARG B 240 1 10
HELIX 37 37 PRO B 275 ARG B 278 5 4
HELIX 38 38 MSE B 297 GLU B 307 1 11
HELIX 39 39 ILE B 308 ARG B 312 5 5
HELIX 40 40 ILE B 315 PRO B 317 5 3
HELIX 41 41 ASP B 318 HIS B 332 1 15
HELIX 42 42 ASP B 360 ILE B 383 1 24
HELIX 43 43 GLY B 393 GLU B 397 5 5
HELIX 44 44 ALA B 398 ARG B 409 1 12
HELIX 45 45 SER B 424 GLY B 426 5 3
HELIX 46 46 ALA B 427 ASP B 432 1 6
HELIX 47 47 ASP B 454 LYS B 470 1 17
SHEET 1 A 6 MSE A 27 PRO A 34 0
SHEET 2 A 6 LEU A 15 TRP A 21 -1 N LEU A 20 O LEU A 28
SHEET 3 A 6 ILE A 7 LEU A 11 -1 N ASP A 10 O LYS A 17
SHEET 4 A 6 THR A 69 GLY A 74 1 O VAL A 73 N ILE A 9
SHEET 5 A 6 GLN A 224 LEU A 226 1 O GLN A 224 N ILE A 70
SHEET 6 A 6 THR A 205 ALA A 208 -1 N GLY A 207 O VAL A 225
SHEET 1 B 5 MSE A 27 PRO A 34 0
SHEET 2 B 5 LEU A 15 TRP A 21 -1 N LEU A 20 O LEU A 28
SHEET 3 B 5 ILE A 7 LEU A 11 -1 N ASP A 10 O LYS A 17
SHEET 4 B 5 THR A 69 GLY A 74 1 O VAL A 73 N ILE A 9
SHEET 5 B 5 LEU A 229 HIS A 230 1 O LEU A 229 N GLY A 74
SHEET 1 C 2 LEU A 38 GLU A 39 0
SHEET 2 C 2 ARG A 44 ARG A 45 -1 O ARG A 45 N LEU A 38
SHEET 1 D 3 ARG A 86 LEU A 87 0
SHEET 2 D 3 ILE A 79 THR A 83 -1 N THR A 83 O ARG A 86
SHEET 3 D 3 THR A 146 PRO A 149 -1 O LEU A 148 N ALA A 80
SHEET 1 E 2 SER A 164 GLU A 165 0
SHEET 2 E 2 ILE A 199 VAL A 200 1 O VAL A 200 N SER A 164
SHEET 1 F 2 TRP A 176 ASP A 177 0
SHEET 2 F 2 ASP A 182 PHE A 183 -1 O ASP A 182 N ASP A 177
SHEET 1 G 7 CYS A 280 VAL A 284 0
SHEET 2 G 7 PRO A 290 PHE A 296 -1 O VAL A 291 N ASN A 283
SHEET 3 G 7 PHE A 259 LEU A 264 -1 N ALA A 261 O ALA A 294
SHEET 4 G 7 ALA A 250 SER A 254 -1 N ALA A 250 O LEU A 264
SHEET 5 G 7 ARG A 388 GLU A 392 1 O LEU A 390 N LEU A 253
SHEET 6 G 7 ALA A 413 ALA A 417 1 O TYR A 415 N ILE A 389
SHEET 7 G 7 LEU A 441 ARG A 443 -1 O VAL A 442 N THR A 416
SHEET 1 H 2 MSE A 335 LEU A 337 0
SHEET 2 H 2 ALA A 353 ILE A 355 -1 O ALA A 353 N LEU A 337
SHEET 1 I 6 MSE B 27 PRO B 34 0
SHEET 2 I 6 LEU B 15 ASP B 22 -1 N LEU B 20 O LEU B 28
SHEET 3 I 6 GLY B 4 LEU B 11 -1 N ASP B 10 O LYS B 17
SHEET 4 I 6 THR B 69 GLY B 74 1 O THR B 69 N ILE B 7
SHEET 5 I 6 GLN B 224 LEU B 226 1 O GLN B 224 N ILE B 70
SHEET 6 I 6 THR B 205 ALA B 208 -1 N GLY B 207 O VAL B 225
SHEET 1 J 5 MSE B 27 PRO B 34 0
SHEET 2 J 5 LEU B 15 ASP B 22 -1 N LEU B 20 O LEU B 28
SHEET 3 J 5 GLY B 4 LEU B 11 -1 N ASP B 10 O LYS B 17
SHEET 4 J 5 THR B 69 GLY B 74 1 O THR B 69 N ILE B 7
SHEET 5 J 5 LEU B 229 HIS B 230 1 O LEU B 229 N GLY B 74
SHEET 1 K 2 LEU B 38 ILE B 40 0
SHEET 2 K 2 ILE B 43 ARG B 45 -1 O ARG B 45 N LEU B 38
SHEET 1 L 3 ARG B 86 LEU B 87 0
SHEET 2 L 3 ILE B 79 THR B 83 -1 N THR B 83 O ARG B 86
SHEET 3 L 3 THR B 146 PRO B 149 -1 O LEU B 148 N ALA B 80
SHEET 1 M 2 TRP B 176 ASP B 177 0
SHEET 2 M 2 ASP B 182 PHE B 183 -1 O ASP B 182 N ASP B 177
SHEET 1 N 7 CYS B 280 VAL B 284 0
SHEET 2 N 7 PRO B 290 PHE B 296 -1 O VAL B 291 N ASN B 283
SHEET 3 N 7 PHE B 259 LEU B 264 -1 N PHE B 259 O PHE B 296
SHEET 4 N 7 ALA B 250 SER B 254 -1 N ALA B 250 O LEU B 264
SHEET 5 N 7 ARG B 388 VAL B 391 1 O LEU B 390 N LEU B 253
SHEET 6 N 7 ALA B 413 THR B 416 1 O TYR B 415 N ILE B 389
SHEET 7 N 7 VAL B 442 ARG B 443 -1 O VAL B 442 N THR B 416
SHEET 1 O 2 MSE B 335 LEU B 337 0
SHEET 2 O 2 ALA B 353 ILE B 355 -1 O ALA B 353 N LEU B 337
LINK C ARG A 26 N MSE A 27 1555 1555 1.33
LINK C MSE A 27 N LEU A 28 1555 1555 1.33
LINK C VAL A 102 N MSE A 103 1555 1555 1.33
LINK C MSE A 103 N ALA A 104 1555 1555 1.33
LINK C VAL A 141 N MSE A 142 1555 1555 1.33
LINK C MSE A 142 N ALA A 143 1555 1555 1.33
LINK C PRO A 185 N MSE A 186 1555 1555 1.33
LINK C MSE A 186 N ALA A 187 1555 1555 1.33
LINK C ALA A 261 N MSE A 262 1555 1555 1.33
LINK C MSE A 262 N ARG A 263 1555 1555 1.33
LINK C PHE A 296 N MSE A 297 1555 1555 1.33
LINK C MSE A 297 N GLY A 298 1555 1555 1.33
LINK C ARG A 334 N MSE A 335 1555 1555 1.33
LINK C MSE A 335 N ILE A 336 1555 1555 1.33
LINK C LEU A 340 N MSE A 341 1555 1555 1.33
LINK C MSE A 341 N ARG A 342 1555 1555 1.33
LINK C ARG B 26 N MSE B 27 1555 1555 1.33
LINK C MSE B 27 N LEU B 28 1555 1555 1.33
LINK C VAL B 102 N MSE B 103 1555 1555 1.33
LINK C MSE B 103 N ALA B 104 1555 1555 1.33
LINK C VAL B 141 N MSE B 142 1555 1555 1.33
LINK C MSE B 142 N ALA B 143 1555 1555 1.33
LINK C PRO B 185 N MSE B 186 1555 1555 1.33
LINK C MSE B 186 N ALA B 187 1555 1555 1.33
LINK C ALA B 261 N MSE B 262 1555 1555 1.33
LINK C MSE B 262 N ARG B 263 1555 1555 1.33
LINK C PHE B 296 N MSE B 297 1555 1555 1.33
LINK C MSE B 297 N GLY B 298 1555 1555 1.33
LINK C ARG B 334 N MSE B 335 1555 1555 1.33
LINK C MSE B 335 N ILE B 336 1555 1555 1.33
LINK C LEU B 340 N MSE B 341 1555 1555 1.33
LINK C MSE B 341 N ARG B 342 1555 1555 1.33
CISPEP 1 PRO A 338 THR A 339 0 1.11
CISPEP 2 PRO B 338 THR B 339 0 -3.04
CISPEP 3 ASN B 418 ALA B 419 0 -3.46
CRYST1 52.614 81.198 229.134 90.00 90.00 90.00 P 21 21 21 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 0.019006 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012316 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004364 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
