HEADER TRANSFERASE 24-MAR-13 4BGA
TITLE NUCLEOTIDE-BOUND OPEN FORM OF A PUTATIVE SUGAR KINASE MK0840 FROM
TITLE 2 METHANOPYRUS KANDLERI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PREDICTED MOLECULAR CHAPERONE DISTANTLY RELATED TO HSP70-F
COMPND 3 OLD METALLOPROTEASES;
COMPND 4 CHAIN: A, B, C, D;
COMPND 5 FRAGMENT: RESIDUES 37-358;
COMPND 6 SYNONYM: PUTATIVE SUGAR KINASE MK0840;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: METHANOPYRUS KANDLERI;
SOURCE 3 ORGANISM_TAXID: 190192;
SOURCE 4 STRAIN: AV19;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PET28A;
SOURCE 10 OTHER_DETAILS: DSM6324
KEYWDS TRANSFERASE, ASKHA SUPERFAMILY, PHOSPHOTRANSFER, PSEUDOMUREIN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.SCHACHERL,U.BAUMANN
REVDAT 4 20-DEC-23 4BGA 1 HETSYN
REVDAT 3 29-JUL-20 4BGA 1 COMPND REMARK HET HETNAM
REVDAT 3 2 1 FORMUL LINK SITE ATOM
REVDAT 2 18-DEC-13 4BGA 1 JRNL
REVDAT 1 27-NOV-13 4BGA 0
JRNL AUTH M.SCHACHERL,S.M.WALTERSPERGER,U.BAUMANN
JRNL TITL STRUCTURAL CHARACTERIZATION OF THE RIBONUCLEASE H-LIKE TYPE
JRNL TITL 2 ASKHA SUPERFAMILY KINASE MK0840 FROM METHANOPYRUS KANDLERI
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 69 2440 2013
JRNL REFN ISSN 0907-4449
JRNL PMID 24311585
JRNL DOI 10.1107/S0907444913022683
REMARK 2
REMARK 2 RESOLUTION. 2.60 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) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 73.57
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 2.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 43757
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.157
REMARK 3 R VALUE (WORKING SET) : 0.154
REMARK 3 FREE R VALUE : 0.208
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2188
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 73.5972 - 6.5501 1.00 2660 140 0.1654 0.1946
REMARK 3 2 6.5501 - 5.1995 1.00 2622 138 0.1567 0.2065
REMARK 3 3 5.1995 - 4.5423 1.00 2617 138 0.1202 0.1513
REMARK 3 4 4.5423 - 4.1271 1.00 2595 137 0.1153 0.1551
REMARK 3 5 4.1271 - 3.8313 1.00 2600 137 0.1326 0.1653
REMARK 3 6 3.8313 - 3.6054 1.00 2602 137 0.1423 0.2056
REMARK 3 7 3.6054 - 3.4248 1.00 2602 137 0.1517 0.2235
REMARK 3 8 3.4248 - 3.2757 1.00 2585 136 0.1606 0.1963
REMARK 3 9 3.2757 - 3.1496 1.00 2592 136 0.1762 0.2406
REMARK 3 10 3.1496 - 3.0410 1.00 2592 136 0.1822 0.2889
REMARK 3 11 3.0410 - 2.9459 1.00 2569 136 0.1903 0.2511
REMARK 3 12 2.9459 - 2.8617 1.00 2590 136 0.1784 0.2774
REMARK 3 13 2.8617 - 2.7863 1.00 2589 136 0.1842 0.2335
REMARK 3 14 2.7863 - 2.7183 1.00 2567 135 0.1772 0.2887
REMARK 3 15 2.7183 - 2.6565 1.00 2605 137 0.1780 0.2466
REMARK 3 16 2.6565 - 2.6000 1.00 2582 136 0.1773 0.2496
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 : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.290
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.530
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 33.99
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.44
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 : 0.006 10011
REMARK 3 ANGLE : 1.181 13642
REMARK 3 CHIRALITY : 0.065 1561
REMARK 3 PLANARITY : 0.005 1799
REMARK 3 DIHEDRAL : 20.379 3816
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: FIRST 36 AMINO ACIDS OF THE PROTEIN ARE
REMARK 3 MISSING.GSH OVERHANG FROM THROMBIN-DIGESTED 6X-HIS TAG.
REMARK 4
REMARK 4 4BGA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-MAR-13.
REMARK 100 THE DEPOSITION ID IS D_1290047194.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-OCT-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06DA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 54893
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 73.600
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 4.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.600
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 21.9500
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.76
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.69
REMARK 200 R MERGE FOR SHELL (I) : 0.36000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.980
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 4BG8 CHAIN A
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.24
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MIXED WITH 5 MM ADP, 10 MM MACL2,
REMARK 280 CRYSTALLIZED IN 0.2 M POTASSIUM SODIUM TARTRATE AND 20% PEG 3350,
REMARK 280 PH 7.5
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 55.83500
REMARK 290 SMTRY3 2 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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1410 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31970 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.1 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, E
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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6740 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24220 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -45.9 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D, F
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 GLY A 34
REMARK 465 SER A 35
REMARK 465 HIS A 36
REMARK 465 GLY A 351
REMARK 465 THR A 352
REMARK 465 GLY A 353
REMARK 465 ARG A 354
REMARK 465 GLY A 355
REMARK 465 GLY A 356
REMARK 465 LYS A 357
REMARK 465 THR A 358
REMARK 465 GLY B 34
REMARK 465 SER B 35
REMARK 465 HIS B 36
REMARK 465 GLY B 351
REMARK 465 THR B 352
REMARK 465 GLY B 353
REMARK 465 ARG B 354
REMARK 465 GLY B 355
REMARK 465 GLY B 356
REMARK 465 LYS B 357
REMARK 465 THR B 358
REMARK 465 GLY C 34
REMARK 465 SER C 35
REMARK 465 HIS C 36
REMARK 465 GLY D 34
REMARK 465 SER D 35
REMARK 465 HIS D 36
REMARK 465 GLY D 351
REMARK 465 THR D 352
REMARK 465 GLY D 353
REMARK 465 ARG D 354
REMARK 465 GLY D 355
REMARK 465 GLY D 356
REMARK 465 LYS D 357
REMARK 465 THR D 358
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 OE2 GLU A 62 NH1 ARG C 101 2.12
REMARK 500 NH2 ARG A 179 OE1 GLU A 341 2.15
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 PHE A 320 79.56 -112.65
REMARK 500 SER B 75 149.83 -171.23
REMARK 500 ASP C 261 36.72 -89.06
REMARK 500 PHE C 320 73.83 -119.49
REMARK 500 SER D 75 145.49 -170.15
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 A2027 DISTANCE = 6.69 ANGSTROMS
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 SUCROSE (SUC): CRYOPROTECTANT
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A1351 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 114 OD2
REMARK 620 2 ASP A 138 O 103.9
REMARK 620 3 GLY A 141 O 165.4 67.1
REMARK 620 4 PRO A 143 O 82.9 83.6 84.6
REMARK 620 5 ASP A 144 OD1 96.0 147.3 87.5 73.3
REMARK 620 6 ASP A 144 OD2 71.7 173.9 118.1 99.8 38.7
REMARK 620 7 HOH A2014 O 82.8 86.6 107.4 160.2 121.8 88.6
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A1352 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 138 OD2
REMARK 620 2 ALA A 142 O 85.6
REMARK 620 3 PHE A 182 O 91.8 88.9
REMARK 620 4 GLY A 183 O 93.8 165.3 76.4
REMARK 620 5 ALA A 185 O 173.7 90.7 93.3 91.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K B1351 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 114 OD2
REMARK 620 2 ASP B 138 O 104.2
REMARK 620 3 GLY B 141 O 164.2 72.7
REMARK 620 4 PRO B 143 O 82.7 84.5 81.6
REMARK 620 5 ASP B 144 OD2 70.4 174.0 113.3 97.2
REMARK 620 6 HOH B2019 O 98.4 81.4 96.4 165.6 96.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K B1352 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 138 OD2
REMARK 620 2 ALA B 142 O 88.1
REMARK 620 3 PHE B 182 O 93.5 88.5
REMARK 620 4 GLY B 183 O 90.0 166.5 78.3
REMARK 620 5 ALA B 185 O 171.9 90.6 94.5 93.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B1354 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ADP B1355 O2A
REMARK 620 2 ADP B1355 O1B 65.9
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K C1359 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 114 OD2
REMARK 620 2 ASP C 138 O 103.8
REMARK 620 3 GLY C 141 O 151.9 70.3
REMARK 620 4 PRO C 143 O 77.3 80.7 74.6
REMARK 620 5 ASP C 144 OD2 70.4 169.5 110.5 89.5
REMARK 620 6 HOH C2016 O 106.5 93.8 101.4 174.0 96.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K C1360 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 138 OD2
REMARK 620 2 ALA C 142 O 92.8
REMARK 620 3 PHE C 182 O 91.3 90.7
REMARK 620 4 GLY C 183 O 89.8 169.0 78.5
REMARK 620 5 ALA C 185 O 172.8 89.9 95.3 88.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K D1352 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 114 OD2
REMARK 620 2 ASP D 138 O 99.5
REMARK 620 3 GLY D 141 O 163.5 65.0
REMARK 620 4 PRO D 143 O 88.1 86.7 85.4
REMARK 620 5 ASP D 144 OD2 76.5 169.1 119.8 103.2
REMARK 620 6 ASP D 144 OD1 102.4 151.6 90.8 76.3 38.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K D1351 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 138 OD2
REMARK 620 2 ALA D 142 O 88.6
REMARK 620 3 PHE D 182 O 92.3 91.8
REMARK 620 4 GLY D 183 O 93.8 168.8 77.2
REMARK 620 5 ALA D 185 O 171.0 87.7 96.1 91.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D1355 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ADP D1356 O1B
REMARK 620 2 ADP D1356 O2A 67.4
REMARK 620 N 1
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4BG8 RELATED DB: PDB
REMARK 900 APO FORM OF A PUTATIVE SUGAR KINASE MK0840 FROM METHANOPYRUS
REMARK 900 KANDLERI (MONOCLINIC SPACE GROUP)
REMARK 900 RELATED ID: 4BG9 RELATED DB: PDB
REMARK 900 APO FORM OF A PUTATIVE SUGAR KINASE MK0840 FROM METHANOPYRUS
REMARK 900 KANDLERI (ORTHORHOMBIC SPACE GROUP)
REMARK 900 RELATED ID: 4BGB RELATED DB: PDB
REMARK 900 NUCLEOTIDE-BOUND CLOSED FORM OF A PUTATIVE SUGAR KINASE MK0840 FROM
REMARK 900 METHANOPYRUS KANDLERI
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 TRUNCATED CONSTRUCT LACKING THE FIRST 36 AMINO ACIDS
DBREF 4BGA A 37 358 UNP Q8TX37 Q8TX37_METKA 37 358
DBREF 4BGA B 37 358 UNP Q8TX37 Q8TX37_METKA 37 358
DBREF 4BGA C 37 358 UNP Q8TX37 Q8TX37_METKA 37 358
DBREF 4BGA D 37 358 UNP Q8TX37 Q8TX37_METKA 37 358
SEQADV 4BGA GLY A 34 UNP Q8TX37 EXPRESSION TAG
SEQADV 4BGA SER A 35 UNP Q8TX37 EXPRESSION TAG
SEQADV 4BGA HIS A 36 UNP Q8TX37 EXPRESSION TAG
SEQADV 4BGA GLY B 34 UNP Q8TX37 EXPRESSION TAG
SEQADV 4BGA SER B 35 UNP Q8TX37 EXPRESSION TAG
SEQADV 4BGA HIS B 36 UNP Q8TX37 EXPRESSION TAG
SEQADV 4BGA GLY C 34 UNP Q8TX37 EXPRESSION TAG
SEQADV 4BGA SER C 35 UNP Q8TX37 EXPRESSION TAG
SEQADV 4BGA HIS C 36 UNP Q8TX37 EXPRESSION TAG
SEQADV 4BGA GLY D 34 UNP Q8TX37 EXPRESSION TAG
SEQADV 4BGA SER D 35 UNP Q8TX37 EXPRESSION TAG
SEQADV 4BGA HIS D 36 UNP Q8TX37 EXPRESSION TAG
SEQRES 1 A 325 GLY SER HIS LEU THR ARG VAL LEU GLY ILE GLN LEU GLY
SEQRES 2 A 325 ASN THR GLY THR ASP TYR CYS VAL MET ASN GLU ASP GLY
SEQRES 3 A 325 ASP TRP GLU ILE VAL ALA ARG GLU GLU GLY VAL PHE GLY
SEQRES 4 A 325 LYS ILE SER CYS VAL PHE THR LEU GLU GLU SER ARG ARG
SEQRES 5 A 325 ALA LEU ARG GLU GLU ILE ALA PRO ARG VAL ILE GLU ARG
SEQRES 6 A 325 VAL ARG ARG VAL ASN PRO ASP LEU ALA VAL VAL GLY THR
SEQRES 7 A 325 ILE VAL ASP GLU LEU GLY LEU ILE LEU GLY PRO MET ILE
SEQRES 8 A 325 HIS GLU LYS THR GLY VAL PRO THR LEU ALA VAL TYR GLY
SEQRES 9 A 325 ASP PRO TRP GLY ALA PRO ASP GLY ASP ALA VAL GLY ALA
SEQRES 10 A 325 PRO TYR CYS VAL ALA GLU GLU TYR PRO ASN CYS VAL HIS
SEQRES 11 A 325 VAL ASP VAL GLY ALA MET ALA VAL VAL THR PRO ILE ARG
SEQRES 12 A 325 ASP GLY ARG PRO ASP PHE GLY ASP ALA VAL VAL SER VAL
SEQRES 13 A 325 GLY THR PHE PRO LEU ASP LEU ALA ALA ARG GLU LEU LEU
SEQRES 14 A 325 GLY LYS GLU TYR ASP GLU GLY GLY LYS LYS ALA ALA GLU
SEQRES 15 A 325 GLY GLU VAL ASP GLU ASN PHE ARG ARG GLU LEU ARG SER
SEQRES 16 A 325 VAL ASP VAL ASP GLY LYS PRO VAL PHE GLY ARG VAL ARG
SEQRES 17 A 325 GLY SER LEU ALA PRO VAL PRO PRO GLU GLN GLU ARG VAL
SEQRES 18 A 325 LEU ARG ASP HIS ILE ARG ASP ALA GLY ALA PRO ALA GLU
SEQRES 19 A 325 ASP VAL LEU ARG THR LEU VAL GLU LEU VAL ALA GLU THR
SEQRES 20 A 325 ILE VAL ILE ASN ALA ALA GLN TYR ASP MET ASP LEU LEU
SEQRES 21 A 325 VAL LEU SER GLY GLY GLY VAL LYS ASN GLU LEU LEU LYS
SEQRES 22 A 325 ARG ARG VAL SER GLU LEU TRP GLU GLY ASP VAL SER ILE
SEQRES 23 A 325 PHE ALA GLY GLU GLU LEU GLU ALA ARG GLY LEU CYS LEU
SEQRES 24 A 325 LEU GLY LEU ARG TYR LEU GLU GLY GLU PRO VAL PRO ALA
SEQRES 25 A 325 LEU PRO CYS GLU GLY GLY THR GLY ARG GLY GLY LYS THR
SEQRES 1 B 325 GLY SER HIS LEU THR ARG VAL LEU GLY ILE GLN LEU GLY
SEQRES 2 B 325 ASN THR GLY THR ASP TYR CYS VAL MET ASN GLU ASP GLY
SEQRES 3 B 325 ASP TRP GLU ILE VAL ALA ARG GLU GLU GLY VAL PHE GLY
SEQRES 4 B 325 LYS ILE SER CYS VAL PHE THR LEU GLU GLU SER ARG ARG
SEQRES 5 B 325 ALA LEU ARG GLU GLU ILE ALA PRO ARG VAL ILE GLU ARG
SEQRES 6 B 325 VAL ARG ARG VAL ASN PRO ASP LEU ALA VAL VAL GLY THR
SEQRES 7 B 325 ILE VAL ASP GLU LEU GLY LEU ILE LEU GLY PRO MET ILE
SEQRES 8 B 325 HIS GLU LYS THR GLY VAL PRO THR LEU ALA VAL TYR GLY
SEQRES 9 B 325 ASP PRO TRP GLY ALA PRO ASP GLY ASP ALA VAL GLY ALA
SEQRES 10 B 325 PRO TYR CYS VAL ALA GLU GLU TYR PRO ASN CYS VAL HIS
SEQRES 11 B 325 VAL ASP VAL GLY ALA MET ALA VAL VAL THR PRO ILE ARG
SEQRES 12 B 325 ASP GLY ARG PRO ASP PHE GLY ASP ALA VAL VAL SER VAL
SEQRES 13 B 325 GLY THR PHE PRO LEU ASP LEU ALA ALA ARG GLU LEU LEU
SEQRES 14 B 325 GLY LYS GLU TYR ASP GLU GLY GLY LYS LYS ALA ALA GLU
SEQRES 15 B 325 GLY GLU VAL ASP GLU ASN PHE ARG ARG GLU LEU ARG SER
SEQRES 16 B 325 VAL ASP VAL ASP GLY LYS PRO VAL PHE GLY ARG VAL ARG
SEQRES 17 B 325 GLY SER LEU ALA PRO VAL PRO PRO GLU GLN GLU ARG VAL
SEQRES 18 B 325 LEU ARG ASP HIS ILE ARG ASP ALA GLY ALA PRO ALA GLU
SEQRES 19 B 325 ASP VAL LEU ARG THR LEU VAL GLU LEU VAL ALA GLU THR
SEQRES 20 B 325 ILE VAL ILE ASN ALA ALA GLN TYR ASP MET ASP LEU LEU
SEQRES 21 B 325 VAL LEU SER GLY GLY GLY VAL LYS ASN GLU LEU LEU LYS
SEQRES 22 B 325 ARG ARG VAL SER GLU LEU TRP GLU GLY ASP VAL SER ILE
SEQRES 23 B 325 PHE ALA GLY GLU GLU LEU GLU ALA ARG GLY LEU CYS LEU
SEQRES 24 B 325 LEU GLY LEU ARG TYR LEU GLU GLY GLU PRO VAL PRO ALA
SEQRES 25 B 325 LEU PRO CYS GLU GLY GLY THR GLY ARG GLY GLY LYS THR
SEQRES 1 C 325 GLY SER HIS LEU THR ARG VAL LEU GLY ILE GLN LEU GLY
SEQRES 2 C 325 ASN THR GLY THR ASP TYR CYS VAL MET ASN GLU ASP GLY
SEQRES 3 C 325 ASP TRP GLU ILE VAL ALA ARG GLU GLU GLY VAL PHE GLY
SEQRES 4 C 325 LYS ILE SER CYS VAL PHE THR LEU GLU GLU SER ARG ARG
SEQRES 5 C 325 ALA LEU ARG GLU GLU ILE ALA PRO ARG VAL ILE GLU ARG
SEQRES 6 C 325 VAL ARG ARG VAL ASN PRO ASP LEU ALA VAL VAL GLY THR
SEQRES 7 C 325 ILE VAL ASP GLU LEU GLY LEU ILE LEU GLY PRO MET ILE
SEQRES 8 C 325 HIS GLU LYS THR GLY VAL PRO THR LEU ALA VAL TYR GLY
SEQRES 9 C 325 ASP PRO TRP GLY ALA PRO ASP GLY ASP ALA VAL GLY ALA
SEQRES 10 C 325 PRO TYR CYS VAL ALA GLU GLU TYR PRO ASN CYS VAL HIS
SEQRES 11 C 325 VAL ASP VAL GLY ALA MET ALA VAL VAL THR PRO ILE ARG
SEQRES 12 C 325 ASP GLY ARG PRO ASP PHE GLY ASP ALA VAL VAL SER VAL
SEQRES 13 C 325 GLY THR PHE PRO LEU ASP LEU ALA ALA ARG GLU LEU LEU
SEQRES 14 C 325 GLY LYS GLU TYR ASP GLU GLY GLY LYS LYS ALA ALA GLU
SEQRES 15 C 325 GLY GLU VAL ASP GLU ASN PHE ARG ARG GLU LEU ARG SER
SEQRES 16 C 325 VAL ASP VAL ASP GLY LYS PRO VAL PHE GLY ARG VAL ARG
SEQRES 17 C 325 GLY SER LEU ALA PRO VAL PRO PRO GLU GLN GLU ARG VAL
SEQRES 18 C 325 LEU ARG ASP HIS ILE ARG ASP ALA GLY ALA PRO ALA GLU
SEQRES 19 C 325 ASP VAL LEU ARG THR LEU VAL GLU LEU VAL ALA GLU THR
SEQRES 20 C 325 ILE VAL ILE ASN ALA ALA GLN TYR ASP MET ASP LEU LEU
SEQRES 21 C 325 VAL LEU SER GLY GLY GLY VAL LYS ASN GLU LEU LEU LYS
SEQRES 22 C 325 ARG ARG VAL SER GLU LEU TRP GLU GLY ASP VAL SER ILE
SEQRES 23 C 325 PHE ALA GLY GLU GLU LEU GLU ALA ARG GLY LEU CYS LEU
SEQRES 24 C 325 LEU GLY LEU ARG TYR LEU GLU GLY GLU PRO VAL PRO ALA
SEQRES 25 C 325 LEU PRO CYS GLU GLY GLY THR GLY ARG GLY GLY LYS THR
SEQRES 1 D 325 GLY SER HIS LEU THR ARG VAL LEU GLY ILE GLN LEU GLY
SEQRES 2 D 325 ASN THR GLY THR ASP TYR CYS VAL MET ASN GLU ASP GLY
SEQRES 3 D 325 ASP TRP GLU ILE VAL ALA ARG GLU GLU GLY VAL PHE GLY
SEQRES 4 D 325 LYS ILE SER CYS VAL PHE THR LEU GLU GLU SER ARG ARG
SEQRES 5 D 325 ALA LEU ARG GLU GLU ILE ALA PRO ARG VAL ILE GLU ARG
SEQRES 6 D 325 VAL ARG ARG VAL ASN PRO ASP LEU ALA VAL VAL GLY THR
SEQRES 7 D 325 ILE VAL ASP GLU LEU GLY LEU ILE LEU GLY PRO MET ILE
SEQRES 8 D 325 HIS GLU LYS THR GLY VAL PRO THR LEU ALA VAL TYR GLY
SEQRES 9 D 325 ASP PRO TRP GLY ALA PRO ASP GLY ASP ALA VAL GLY ALA
SEQRES 10 D 325 PRO TYR CYS VAL ALA GLU GLU TYR PRO ASN CYS VAL HIS
SEQRES 11 D 325 VAL ASP VAL GLY ALA MET ALA VAL VAL THR PRO ILE ARG
SEQRES 12 D 325 ASP GLY ARG PRO ASP PHE GLY ASP ALA VAL VAL SER VAL
SEQRES 13 D 325 GLY THR PHE PRO LEU ASP LEU ALA ALA ARG GLU LEU LEU
SEQRES 14 D 325 GLY LYS GLU TYR ASP GLU GLY GLY LYS LYS ALA ALA GLU
SEQRES 15 D 325 GLY GLU VAL ASP GLU ASN PHE ARG ARG GLU LEU ARG SER
SEQRES 16 D 325 VAL ASP VAL ASP GLY LYS PRO VAL PHE GLY ARG VAL ARG
SEQRES 17 D 325 GLY SER LEU ALA PRO VAL PRO PRO GLU GLN GLU ARG VAL
SEQRES 18 D 325 LEU ARG ASP HIS ILE ARG ASP ALA GLY ALA PRO ALA GLU
SEQRES 19 D 325 ASP VAL LEU ARG THR LEU VAL GLU LEU VAL ALA GLU THR
SEQRES 20 D 325 ILE VAL ILE ASN ALA ALA GLN TYR ASP MET ASP LEU LEU
SEQRES 21 D 325 VAL LEU SER GLY GLY GLY VAL LYS ASN GLU LEU LEU LYS
SEQRES 22 D 325 ARG ARG VAL SER GLU LEU TRP GLU GLY ASP VAL SER ILE
SEQRES 23 D 325 PHE ALA GLY GLU GLU LEU GLU ALA ARG GLY LEU CYS LEU
SEQRES 24 D 325 LEU GLY LEU ARG TYR LEU GLU GLY GLU PRO VAL PRO ALA
SEQRES 25 D 325 LEU PRO CYS GLU GLY GLY THR GLY ARG GLY GLY LYS THR
HET GLC E 1 11
HET FRU E 2 12
HET GLC F 1 11
HET FRU F 2 12
HET K A1351 1
HET K A1352 1
HET BGC A1353 12
HET ADP A1354 27
HET K B1351 1
HET K B1352 1
HET BGC B1353 12
HET MG B1354 1
HET ADP B1355 27
HET K C1359 1
HET K C1360 1
HET BGC C1361 12
HET MG C1363 1
HET ADP C1364 27
HET K D1351 1
HET K D1352 1
HET BGC D1353 12
HET MG D1355 1
HET ADP D1356 27
HETNAM GLC ALPHA-D-GLUCOPYRANOSE
HETNAM FRU BETA-D-FRUCTOFURANOSE
HETNAM K POTASSIUM ION
HETNAM BGC BETA-D-GLUCOPYRANOSE
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
HETNAM MG MAGNESIUM ION
HETSYN GLC ALPHA-D-GLUCOSE; D-GLUCOSE; GLUCOSE
HETSYN FRU BETA-D-FRUCTOSE; D-FRUCTOSE; FRUCTOSE
HETSYN BGC BETA-D-GLUCOSE; D-GLUCOSE; GLUCOSE
FORMUL 5 GLC 2(C6 H12 O6)
FORMUL 5 FRU 2(C6 H12 O6)
FORMUL 7 K 8(K 1+)
FORMUL 9 BGC 4(C6 H12 O6)
FORMUL 10 ADP 4(C10 H15 N5 O10 P2)
FORMUL 14 MG 3(MG 2+)
FORMUL 26 HOH *222(H2 O)
HELIX 1 1 THR A 79 GLU A 90 1 12
HELIX 2 2 GLU A 90 ASN A 103 1 14
HELIX 3 3 VAL A 113 GLY A 129 1 17
HELIX 4 4 ASP A 144 ALA A 147 5 4
HELIX 5 5 VAL A 148 TYR A 158 1 11
HELIX 6 6 THR A 191 GLY A 203 1 13
HELIX 7 7 ASP A 207 LYS A 211 5 5
HELIX 8 8 LYS A 212 GLY A 216 5 5
HELIX 9 9 ASP A 219 SER A 228 1 10
HELIX 10 10 VAL A 247 ASP A 261 1 15
HELIX 11 11 PRO A 265 ALA A 286 1 22
HELIX 12 12 GLN A 287 ASP A 289 5 3
HELIX 13 13 GLY A 297 LYS A 301 5 5
HELIX 14 14 ASN A 302 TRP A 313 1 12
HELIX 15 15 GLU A 324 GLU A 339 1 16
HELIX 16 16 THR B 79 GLU B 90 1 12
HELIX 17 17 GLU B 90 ASN B 103 1 14
HELIX 18 18 VAL B 113 GLY B 129 1 17
HELIX 19 19 ASP B 144 ALA B 147 5 4
HELIX 20 20 VAL B 148 TYR B 158 1 11
HELIX 21 21 THR B 191 GLY B 203 1 13
HELIX 22 22 ASP B 207 LYS B 211 5 5
HELIX 23 23 LYS B 212 GLY B 216 5 5
HELIX 24 24 ASP B 219 SER B 228 1 10
HELIX 25 25 VAL B 247 ALA B 262 1 16
HELIX 26 26 PRO B 265 ALA B 286 1 22
HELIX 27 27 GLN B 287 ASP B 289 5 3
HELIX 28 28 GLY B 297 LYS B 301 5 5
HELIX 29 29 ASN B 302 TRP B 313 1 12
HELIX 30 30 GLU B 324 GLU B 339 1 16
HELIX 31 31 THR C 79 GLU C 90 1 12
HELIX 32 32 GLU C 90 ASN C 103 1 14
HELIX 33 33 VAL C 113 GLY C 129 1 17
HELIX 34 34 ASP C 144 ALA C 147 5 4
HELIX 35 35 VAL C 148 GLU C 156 1 9
HELIX 36 36 THR C 191 LEU C 202 1 12
HELIX 37 37 ASP C 207 LYS C 211 5 5
HELIX 38 38 LYS C 212 GLY C 216 5 5
HELIX 39 39 ASP C 219 SER C 228 1 10
HELIX 40 40 VAL C 247 ASP C 261 1 15
HELIX 41 41 PRO C 265 ALA C 286 1 22
HELIX 42 42 GLY C 297 LYS C 301 5 5
HELIX 43 43 ASN C 302 TRP C 313 1 12
HELIX 44 44 GLU C 324 GLU C 339 1 16
HELIX 45 45 THR D 79 GLU D 90 1 12
HELIX 46 46 GLU D 90 ASN D 103 1 14
HELIX 47 47 VAL D 113 GLY D 129 1 17
HELIX 48 48 ASP D 144 ALA D 147 5 4
HELIX 49 49 VAL D 148 TYR D 158 1 11
HELIX 50 50 THR D 191 GLY D 203 1 13
HELIX 51 51 ASP D 207 LYS D 211 5 5
HELIX 52 52 LYS D 212 GLY D 216 5 5
HELIX 53 53 ASP D 219 SER D 228 1 10
HELIX 54 54 VAL D 247 ASP D 261 1 15
HELIX 55 55 PRO D 265 ALA D 286 1 22
HELIX 56 56 GLN D 287 ASP D 289 5 3
HELIX 57 57 GLY D 297 LYS D 301 5 5
HELIX 58 58 ASN D 302 TRP D 313 1 12
HELIX 59 59 GLU D 324 GLU D 339 1 16
SHEET 1 AA12 ALA A 345 CYS A 348 0
SHEET 2 AA12 THR A 132 VAL A 135 -1 O THR A 132 N CYS A 348
SHEET 3 AA12 LEU A 106 THR A 111 1 O ALA A 107 N LEU A 133
SHEET 4 AA12 ARG A 39 LEU A 45 1 O LEU A 41 N VAL A 108
SHEET 5 AA12 GLY A 49 ASN A 56 -1 O ASP A 51 N GLN A 44
SHEET 6 AA12 TRP A 61 GLU A 68 -1 O GLU A 62 N VAL A 54
SHEET 7 AA12 TRP C 61 GLU C 68 -1 O VAL C 64 N ILE A 63
SHEET 8 AA12 GLY C 49 ASN C 56 -1 O THR C 50 N GLU C 67
SHEET 9 AA12 ARG C 39 LEU C 45 -1 O VAL C 40 N MET C 55
SHEET 10 AA12 LEU C 106 THR C 111 1 O LEU C 106 N LEU C 41
SHEET 11 AA12 THR C 132 VAL C 135 1 O LEU C 133 N VAL C 109
SHEET 12 AA12 ALA C 345 CYS C 348 -1 O LEU C 346 N ALA C 134
SHEET 1 AB 2 ARG A 179 PRO A 180 0
SHEET 2 AB 2 MET A 169 ARG A 176 1 O ARG A 176 N ARG A 179
SHEET 1 AC 2 VAL A 186 VAL A 189 0
SHEET 2 AC 2 MET A 169 ARG A 176 -1 O ALA A 170 N SER A 188
SHEET 1 AD 5 VAL A 317 ILE A 319 0
SHEET 2 AD 5 LEU A 293 SER A 296 1 O LEU A 293 N SER A 318
SHEET 3 AD 5 CYS A 161 VAL A 166 1 O VAL A 162 N VAL A 294
SHEET 4 AD 5 MET A 169 ARG A 176 -1 O VAL A 171 N ASP A 165
SHEET 5 AD 5 ARG A 179 PRO A 180 1 O ARG A 179 N ARG A 176
SHEET 1 AE 5 VAL A 317 ILE A 319 0
SHEET 2 AE 5 LEU A 293 SER A 296 1 O LEU A 293 N SER A 318
SHEET 3 AE 5 CYS A 161 VAL A 166 1 O VAL A 162 N VAL A 294
SHEET 4 AE 5 MET A 169 ARG A 176 -1 O VAL A 171 N ASP A 165
SHEET 5 AE 5 VAL A 186 VAL A 189 -1 O VAL A 186 N VAL A 172
SHEET 1 AF 2 ASP A 230 VAL A 231 0
SHEET 2 AF 2 LYS A 234 PRO A 235 -1 O LYS A 234 N VAL A 231
SHEET 1 BA 6 TRP B 61 GLU B 68 0
SHEET 2 BA 6 GLY B 49 ASN B 56 -1 O THR B 50 N GLU B 67
SHEET 3 BA 6 ARG B 39 LEU B 45 -1 O VAL B 40 N MET B 55
SHEET 4 BA 6 LEU B 106 THR B 111 1 O LEU B 106 N LEU B 41
SHEET 5 BA 6 THR B 132 VAL B 135 1 O LEU B 133 N VAL B 109
SHEET 6 BA 6 ALA B 345 CYS B 348 -1 O LEU B 346 N ALA B 134
SHEET 1 BB 2 ARG B 179 PRO B 180 0
SHEET 2 BB 2 MET B 169 ARG B 176 1 O ARG B 176 N ARG B 179
SHEET 1 BC 2 VAL B 186 VAL B 189 0
SHEET 2 BC 2 MET B 169 ARG B 176 -1 O ALA B 170 N SER B 188
SHEET 1 BD 5 ASP B 316 ILE B 319 0
SHEET 2 BD 5 LEU B 292 SER B 296 1 O LEU B 293 N SER B 318
SHEET 3 BD 5 CYS B 161 VAL B 166 1 O VAL B 162 N VAL B 294
SHEET 4 BD 5 MET B 169 ARG B 176 -1 O VAL B 171 N ASP B 165
SHEET 5 BD 5 ARG B 179 PRO B 180 1 O ARG B 179 N ARG B 176
SHEET 1 BE 5 ASP B 316 ILE B 319 0
SHEET 2 BE 5 LEU B 292 SER B 296 1 O LEU B 293 N SER B 318
SHEET 3 BE 5 CYS B 161 VAL B 166 1 O VAL B 162 N VAL B 294
SHEET 4 BE 5 MET B 169 ARG B 176 -1 O VAL B 171 N ASP B 165
SHEET 5 BE 5 VAL B 186 VAL B 189 -1 O VAL B 186 N VAL B 172
SHEET 1 BF 2 ASP B 230 VAL B 231 0
SHEET 2 BF 2 LYS B 234 PRO B 235 -1 O LYS B 234 N VAL B 231
SHEET 1 CA 2 ARG C 179 PRO C 180 0
SHEET 2 CA 2 MET C 169 ARG C 176 1 O ARG C 176 N ARG C 179
SHEET 1 CB 2 VAL C 186 VAL C 189 0
SHEET 2 CB 2 MET C 169 ARG C 176 -1 O ALA C 170 N SER C 188
SHEET 1 CC 5 ASP C 316 ILE C 319 0
SHEET 2 CC 5 LEU C 292 SER C 296 1 O LEU C 293 N SER C 318
SHEET 3 CC 5 CYS C 161 VAL C 166 1 O VAL C 162 N VAL C 294
SHEET 4 CC 5 MET C 169 ARG C 176 -1 O VAL C 171 N ASP C 165
SHEET 5 CC 5 ARG C 179 PRO C 180 1 O ARG C 179 N ARG C 176
SHEET 1 CD 5 ASP C 316 ILE C 319 0
SHEET 2 CD 5 LEU C 292 SER C 296 1 O LEU C 293 N SER C 318
SHEET 3 CD 5 CYS C 161 VAL C 166 1 O VAL C 162 N VAL C 294
SHEET 4 CD 5 MET C 169 ARG C 176 -1 O VAL C 171 N ASP C 165
SHEET 5 CD 5 VAL C 186 VAL C 189 -1 O VAL C 186 N VAL C 172
SHEET 1 CE 2 ASP C 230 VAL C 231 0
SHEET 2 CE 2 LYS C 234 PRO C 235 -1 O LYS C 234 N VAL C 231
SHEET 1 DA 6 TRP D 61 GLU D 68 0
SHEET 2 DA 6 GLY D 49 ASN D 56 -1 O THR D 50 N GLU D 67
SHEET 3 DA 6 ARG D 39 LEU D 45 -1 O VAL D 40 N MET D 55
SHEET 4 DA 6 LEU D 106 THR D 111 1 O LEU D 106 N LEU D 41
SHEET 5 DA 6 THR D 132 VAL D 135 1 O LEU D 133 N VAL D 109
SHEET 6 DA 6 ALA D 345 CYS D 348 -1 O LEU D 346 N ALA D 134
SHEET 1 DB 2 ARG D 179 PRO D 180 0
SHEET 2 DB 2 MET D 169 ARG D 176 1 O ARG D 176 N ARG D 179
SHEET 1 DC 2 VAL D 186 VAL D 189 0
SHEET 2 DC 2 MET D 169 ARG D 176 -1 O ALA D 170 N SER D 188
SHEET 1 DD 5 VAL D 317 ILE D 319 0
SHEET 2 DD 5 LEU D 293 SER D 296 1 O LEU D 293 N SER D 318
SHEET 3 DD 5 CYS D 161 VAL D 166 1 O VAL D 162 N VAL D 294
SHEET 4 DD 5 MET D 169 ARG D 176 -1 O VAL D 171 N ASP D 165
SHEET 5 DD 5 ARG D 179 PRO D 180 1 O ARG D 179 N ARG D 176
SHEET 1 DE 5 VAL D 317 ILE D 319 0
SHEET 2 DE 5 LEU D 293 SER D 296 1 O LEU D 293 N SER D 318
SHEET 3 DE 5 CYS D 161 VAL D 166 1 O VAL D 162 N VAL D 294
SHEET 4 DE 5 MET D 169 ARG D 176 -1 O VAL D 171 N ASP D 165
SHEET 5 DE 5 VAL D 186 VAL D 189 -1 O VAL D 186 N VAL D 172
SHEET 1 DF 2 ASP D 230 VAL D 231 0
SHEET 2 DF 2 LYS D 234 PRO D 235 -1 O LYS D 234 N VAL D 231
LINK C1 GLC E 1 O2 FRU E 2 1555 1555 1.41
LINK C1 GLC F 1 O2 FRU F 2 1555 1555 1.41
LINK OD2 ASP A 114 K K A1351 1555 1555 3.13
LINK O ASP A 138 K K A1351 1555 1555 2.81
LINK OD2 ASP A 138 K K A1352 1555 1555 2.98
LINK O GLY A 141 K K A1351 1555 1555 2.88
LINK O ALA A 142 K K A1352 1555 1555 2.71
LINK O PRO A 143 K K A1351 1555 1555 3.08
LINK OD1 ASP A 144 K K A1351 1555 1555 3.42
LINK OD2 ASP A 144 K K A1351 1555 1555 3.15
LINK O PHE A 182 K K A1352 1555 1555 2.87
LINK O GLY A 183 K K A1352 1555 1555 2.94
LINK O ALA A 185 K K A1352 1555 1555 2.85
LINK K K A1351 O HOH A2014 1555 1555 3.26
LINK OD2 ASP B 114 K K B1351 1555 1555 3.05
LINK O ASP B 138 K K B1351 1555 1555 2.78
LINK OD2 ASP B 138 K K B1352 1555 1555 3.04
LINK O GLY B 141 K K B1351 1555 1555 2.74
LINK O ALA B 142 K K B1352 1555 1555 2.73
LINK O PRO B 143 K K B1351 1555 1555 3.12
LINK OD2 ASP B 144 K K B1351 1555 1555 3.21
LINK O PHE B 182 K K B1352 1555 1555 2.86
LINK O GLY B 183 K K B1352 1555 1555 3.07
LINK O ALA B 185 K K B1352 1555 1555 2.71
LINK K K B1351 O HOH B2019 1555 1555 3.12
LINK MG MG B1354 O2A ADP B1355 1555 1555 2.76
LINK MG MG B1354 O1B ADP B1355 1555 1555 2.31
LINK OD2 ASP C 114 K K C1359 1555 1555 3.02
LINK O ASP C 138 K K C1359 1555 1555 2.80
LINK OD2 ASP C 138 K K C1360 1555 1555 2.98
LINK O GLY C 141 K K C1359 1555 1555 2.79
LINK O ALA C 142 K K C1360 1555 1555 2.70
LINK O PRO C 143 K K C1359 1555 1555 3.44
LINK OD2 ASP C 144 K K C1359 1555 1555 3.23
LINK O PHE C 182 K K C1360 1555 1555 2.85
LINK O GLY C 183 K K C1360 1555 1555 3.05
LINK O ALA C 185 K K C1360 1555 1555 2.78
LINK K K C1359 O HOH C2016 1555 1555 3.35
LINK MG MG C1363 O1A ADP C1364 1555 1555 2.42
LINK OD2 ASP D 114 K K D1352 1555 1555 2.91
LINK OD2 ASP D 138 K K D1351 1555 1555 3.05
LINK O ASP D 138 K K D1352 1555 1555 2.96
LINK O GLY D 141 K K D1352 1555 1555 2.84
LINK O ALA D 142 K K D1351 1555 1555 2.87
LINK O PRO D 143 K K D1352 1555 1555 2.90
LINK OD2 ASP D 144 K K D1352 1555 1555 3.16
LINK OD1 ASP D 144 K K D1352 1555 1555 3.47
LINK O PHE D 182 K K D1351 1555 1555 2.84
LINK O GLY D 183 K K D1351 1555 1555 3.12
LINK O ALA D 185 K K D1351 1555 1555 2.73
LINK MG MG D1355 O1B ADP D1356 1555 1555 2.38
LINK MG MG D1355 O2A ADP D1356 1555 1555 2.76
CISPEP 1 ALA A 142 PRO A 143 0 10.11
CISPEP 2 ALA B 142 PRO B 143 0 8.70
CISPEP 3 ALA C 142 PRO C 143 0 9.49
CISPEP 4 ALA D 142 PRO D 143 0 10.60
CRYST1 73.570 111.670 87.880 90.00 89.55 90.00 P 1 21 1 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 0.013592 0.000000 -0.000107 0.00000
SCALE2 0.000000 0.008955 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011380 0.00000
(ATOM LINES ARE NOT SHOWN.)
END