HEADER HYDROLASE 27-JAN-16 5FUI
TITLE CRYSTAL STRUCTURE OF THE C-TERMINAL CBM6 OF LAMC A MARINE LAMINARIANSE
TITLE 2 FROM ZOBELLIA GALACTANIVORANS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENDO-1,3-BETA-GLUCANASE, FAMILY GH16;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CARBOHYDRATE BINDING MODULE, RESIDUES 262-385;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ZOBELLIA GALACTANIVORANS;
SOURCE 3 ORGANISM_TAXID: 63186;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PFO4;
SOURCE 9 OTHER_DETAILS: GERMAN COLLECTION OF MICROORGANISMS (DSM)
KEYWDS HYDROLASE, CARBOHYDRATE BINDING MODULE, CBM6, POLYSACCHARIDE
KEYWDS 2 FIXATION, MARINE BACTERIAL LAMINARINASE, ZOBELLIA GALACTANIVORANS
EXPDTA X-RAY DIFFRACTION
AUTHOR A.LABOUREL,M.JAM,L.LEGENTIL,B.SYLLA,J.H.HEHEMANN,E.FICKO-BLEAN,
AUTHOR 2 V.FERRIERES,M.CZJZEK,G.MICHEL
REVDAT 4 10-JAN-24 5FUI 1 REMARK LINK
REVDAT 3 08-JUN-16 5FUI 1 JRNL
REVDAT 2 23-MAR-16 5FUI 1 JRNL
REVDAT 1 02-MAR-16 5FUI 0
SPRSDE 02-MAR-16 5FUI 4CRR
JRNL AUTH M.JAM,E.FICKO-BLEAN,A.LABOUREL,R.LAROCQUE,M.CZJZEK,G.MICHEL
JRNL TITL UNRAVELING THE MULTIVALENT BINDING OF A MARINE FAMILY 6
JRNL TITL 2 CARBOHYDRATE-BINDING MODULE WITH ITS NATIVE LAMINARIN
JRNL TITL 3 LIGAND.
JRNL REF FEBS J. V. 283 1863 2016
JRNL REFN ISSN 1742-464X
JRNL PMID 26959085
JRNL DOI 10.1111/FEBS.13707
REMARK 2
REMARK 2 RESOLUTION. 1.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.71
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.6
REMARK 3 NUMBER OF REFLECTIONS : 18751
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.128
REMARK 3 R VALUE (WORKING SET) : 0.126
REMARK 3 FREE R VALUE : 0.127
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1014
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.43
REMARK 3 REFLECTION IN BIN (WORKING SET) : 862
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 58.83
REMARK 3 BIN R VALUE (WORKING SET) : 0.2130
REMARK 3 BIN FREE R VALUE SET COUNT : 54
REMARK 3 BIN FREE R VALUE : 0.3140
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 956
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 23
REMARK 3 SOLVENT ATOMS : 143
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.24000
REMARK 3 B22 (A**2) : -0.30000
REMARK 3 B33 (A**2) : 0.69000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.16000
REMARK 3 B23 (A**2) : 0.23000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.067
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.061
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.041
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.346
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.980
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.968
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1022 ; 0.024 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1394 ; 2.064 ; 1.939
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 131 ; 6.673 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 47 ;39.211 ;25.319
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 151 ;10.912 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 3 ;17.694 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 147 ; 0.163 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 800 ; 0.013 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 1022 ; 9.525 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 34 ;20.128 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 1107 ; 8.907 ; 5.000
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS. U VALUES REFINED INDIVIDUALLY.
REMARK 4
REMARK 4 5FUI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-JAN-16.
REMARK 100 THE DEPOSITION ID IS D_1290066109.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-JUL-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19499
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.400
REMARK 200 RESOLUTION RANGE LOW (A) : 46.700
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.100
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.0
REMARK 200 DATA REDUNDANCY : 2.800
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.43
REMARK 200 COMPLETENESS FOR SHELL (%) : 65.3
REMARK 200 DATA REDUNDANCY IN SHELL : 2.80
REMARK 200 R MERGE FOR SHELL (I) : 0.36000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1UXZ
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.13
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM HEPES PH 7.2, 10 MM MGCL2 AND
REMARK 280 27 % POLYACRYLIC ACID. MICROSEEDING WAS ESSENTIAL
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 39.02800
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 14.76150
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 39.02800
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 14.76150
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 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 HIS A 254
REMARK 465 HIS A 255
REMARK 465 HIS A 256
REMARK 465 HIS A 257
REMARK 465 HIS A 258
REMARK 465 HIS A 259
REMARK 465 SER A 260
REMARK 465 GLY A 261
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 CG2 VAL A 358 O HOH A 2131 2.05
REMARK 500 CG1 VAL A 336 O HOH A 2084 2.15
REMARK 500 O HOH A 2105 O HOH A 2107 2.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 GLU A 331 OE1 - CD - OE2 ANGL. DEV. = -7.4 DEGREES
REMARK 500 ARG A 382 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
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 MG A1386 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 267 OE1
REMARK 620 2 GLU A 269 OE1 97.0
REMARK 620 3 GLU A 287 O 153.8 81.9
REMARK 620 4 ASN A 379 OD1 94.9 164.3 91.8
REMARK 620 5 ASN A 379 O 85.2 93.3 121.0 77.5
REMARK 620 6 HOH A2015 O 65.8 96.7 88.2 97.5 150.2
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 131
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE APY A 132
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE APY A 133
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1386
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE CRYSTAL STRUCTURE CONTAINS THE CENTRAL CBM6 MODULE
REMARK 999 ONLY
DBREF 5FUI A 262 385 UNP GOL2L9 G0L2L9_ZOBGA 262 385
SEQADV 5FUI HIS A 254 UNP GOL2L9 EXPRESSION TAG
SEQADV 5FUI HIS A 255 UNP GOL2L9 EXPRESSION TAG
SEQADV 5FUI HIS A 256 UNP GOL2L9 EXPRESSION TAG
SEQADV 5FUI HIS A 257 UNP GOL2L9 EXPRESSION TAG
SEQADV 5FUI HIS A 258 UNP GOL2L9 EXPRESSION TAG
SEQADV 5FUI HIS A 259 UNP GOL2L9 EXPRESSION TAG
SEQADV 5FUI SER A 260 UNP GOL2L9 EXPRESSION TAG
SEQADV 5FUI GLY A 261 UNP GOL2L9 EXPRESSION TAG
SEQRES 1 A 132 HIS HIS HIS HIS HIS HIS SER GLY ASN THR LEU LYS ILE
SEQRES 2 A 132 GLU ALA GLU SER TYR LEU TYR SER ASN ASP VAL GLN LYS
SEQRES 3 A 132 GLU PRO CYS SER GLU GLY GLY GLU ASN VAL GLY TYR ILE
SEQRES 4 A 132 ASN ASN GLY SER TRP MET SER TYR PRO GLY ILE ASN PHE
SEQRES 5 A 132 PRO SER SER GLY ASN TYR LEU ILE GLU TYR ARG VAL ALA
SEQRES 6 A 132 SER ALA VAL ASP GLY GLY ARG PHE SER SER ASP LEU GLU
SEQRES 7 A 132 ALA GLY GLU THR VAL LEU GLY GLU LEU SER VAL PRO ASN
SEQRES 8 A 132 THR GLY GLY TRP GLN ASN TRP THR THR VAL SER GLN THR
SEQRES 9 A 132 VAL ASN VAL SER ALA GLY THR TYR GLN PHE GLY LEU TYR
SEQRES 10 A 132 SER ILE SER GLY GLY TRP ASN ILE ASN TRP ILE ARG ILE
SEQRES 11 A 132 THR LYS
HET GOL A 131 6
HET APY A 132 8
HET APY A 133 8
HET MG A1386 1
HETNAM GOL GLYCEROL
HETNAM APY 2-AMINOMETHYL-PYRIDINE
HETNAM MG MAGNESIUM ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 GOL C3 H8 O3
FORMUL 3 APY 2(C6 H8 N2)
FORMUL 5 MG MG 2+
FORMUL 6 HOH *143(H2 O)
HELIX 1 1 GLU A 269 TYR A 271 5 3
SHEET 1 AA 4 THR A 263 GLU A 267 0
SHEET 2 AA 4 ASN A 377 THR A 384 -1 O ILE A 381 N ILE A 266
SHEET 3 AA 4 GLY A 309 ALA A 318 -1 O LEU A 312 N THR A 384
SHEET 4 AA 4 THR A 352 VAL A 360 -1 O THR A 352 N VAL A 317
SHEET 1 AB 5 TYR A 273 ASN A 275 0
SHEET 2 AB 5 TRP A 297 PHE A 305 -1 O TRP A 297 N ASN A 275
SHEET 3 AB 5 GLY A 363 SER A 373 -1 O GLY A 363 N PHE A 305
SHEET 4 AB 5 ARG A 325 LEU A 330 -1 O ARG A 325 N SER A 373
SHEET 5 AB 5 THR A 335 SER A 341 -1 O THR A 335 N LEU A 330
SHEET 1 AC 2 GLN A 278 PRO A 281 0
SHEET 2 AC 2 GLU A 287 GLY A 290 -1 O ASN A 288 N GLU A 280
LINK OE1 GLU A 267 MG MG A1386 1555 1555 2.54
LINK OE1 GLU A 269 MG MG A1386 1555 1555 2.40
LINK O GLU A 287 MG MG A1386 1555 1555 2.26
LINK OD1 ASN A 379 MG MG A1386 1555 1555 2.36
LINK O ASN A 379 MG MG A1386 1555 1555 2.38
LINK MG MG A1386 O HOH A2015 1555 1555 2.34
SITE 1 AC1 7 GLU A 280 GLY A 290 TYR A 291 TRP A 348
SITE 2 AC1 7 ASN A 377 HOH A2001 HOH A2003
SITE 1 AC2 5 GLU A 284 ASP A 329 GLY A 368 TYR A 370
SITE 2 AC2 5 HOH A2005
SITE 1 AC3 5 TYR A 291 ILE A 292 ASN A 293 GLY A 375
SITE 2 AC3 5 HOH A2003
SITE 1 AC4 5 GLU A 267 GLU A 269 GLU A 287 ASN A 379
SITE 2 AC4 5 HOH A2015
CRYST1 78.056 29.523 51.872 90.00 115.79 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 0.012811 0.000000 0.006190 0.00000
SCALE2 0.000000 0.033872 0.000000 0.00000
SCALE3 0.000000 0.000000 0.021411 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
