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HEADER HYDROLASE 18-JUL-09 3ICW
TITLE STRUCTURE OF A CIRCULAR PERMUTATION ON LIPASE B FROM CANDIDA
TITLE 2 ANTARTICA WITH BOUND SUICIDE INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE B;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CALB;
COMPND 5 EC: 3.1.1.3;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CANDIDA ANTARCTICA;
SOURCE 3 ORGANISM_COMMON: YEAST;
SOURCE 4 ORGANISM_TAXID: 34362;
SOURCE 5 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 4922
KEYWDS CIRCULAR PERMUTATION, SUICIDE INHIBITION, HYDROLASE,
KEYWDS 2 CLEAVAGE ON PAIR OF BASIC RESIDUES, DISULFIDE BOND,
KEYWDS 3 GLYCOPROTEIN, LIPID DEGRADATION, ZYMOGEN
EXPDTA X-RAY DIFFRACTION
AUTHOR J.R.HORTON,Z.QIAN,D.JIA,S.A.LUTZ,X.CHENG
REVDAT 1 06-OCT-09 3ICW 0
JRNL AUTH Z.QIAN,J.R.HORTON,X.CHENG,S.LUTZ
JRNL TITL STRUCTURAL REDESIGN OF LIPASE B FROM CANDIDA
JRNL TITL 2 ANTARCTICA BY CIRCULAR PERMUTATION AND INCREMENTAL
JRNL TITL 3 TRUNCATION.
JRNL REF J.MOL.BIOL. 2009
JRNL REFN ESSN 1089-8638
JRNL PMID 19683009
JRNL DOI 10.1016/J.JMB.2009.08.008
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.69 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.69
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.80
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.4
REMARK 3 NUMBER OF REFLECTIONS : 42309
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 SET) : 0.180
REMARK 3 FREE R VALUE : 0.199
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 2125
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.69
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.75
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 87.30
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2380
REMARK 3 BIN FREE R VALUE : 0.2590
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 199
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.018
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2197
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 45
REMARK 3 SOLVENT ATOMS : 338
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 25.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -4.66000
REMARK 3 B22 (A**2) : -4.66000
REMARK 3 B33 (A**2) : 9.32000
REMARK 3 B12 (A**2) : -2.08000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.18
REMARK 3 ESD FROM SIGMAA (A) : 0.14
REMARK 3 LOW RESOLUTION CUTOFF (A) : 27.80
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.20
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.15
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.50
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.90
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.96
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ISOTROPIC
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3ICW COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-JUL-09.
REMARK 100 THE RCSB ID CODE IS RCSB054253.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-OCT-06
REMARK 200 TEMPERATURE (KELVIN) : 173.0
REMARK 200 PH : 4.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 44608
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.690
REMARK 200 RESOLUTION RANGE LOW (A) : 27.800
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 12.800
REMARK 200 R MERGE (I) : 0.12100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.69
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.75
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 11.50
REMARK 200 R MERGE FOR SHELL (I) : 0.47300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 4.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: GLRF
REMARK 200 STARTING MODEL: PDB CODE 1LBT
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.03
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350, 0.2M SODIUM
REMARK 280 DIHYDROGEN PHOSPHATE, PH 4.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 36.53733
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 18.26867
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 18.26867
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 36.53733
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4920 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22240 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.0 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 350 BIOMT1 2 -0.500000 -0.866025 0.000000 167.61900
REMARK 350 BIOMT2 2 -0.866025 0.500000 0.000000 96.77487
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 91.34333
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A1094 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A1155 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A1184 LIES ON A SPECIAL POSITION.
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 176
REMARK 465 PRO A 177
REMARK 465 LEU A 178
REMARK 465 ASP A 179
REMARK 465 ALA A 180
REMARK 465 LEU A 181
REMARK 465 ALA A 182
REMARK 465 VAL A 183
REMARK 465 LEU A 300
REMARK 465 THR A 301
REMARK 465 PRO A 302
REMARK 465 GLU A 303
REMARK 465 GLN A 304
REMARK 465 LYS A 305
REMARK 465 VAL A 306
REMARK 465 ALA A 307
REMARK 465 ALA A 308
REMARK 465 ALA A 309
REMARK 465 ALA A 310
REMARK 465 LEU A 311
REMARK 465 LEU A 312
REMARK 465 ALA A 313
REMARK 465 PRO A 314
REMARK 465 ALA A 315
REMARK 465 ALA A 316
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 ILE A 3 CG1 CG2 CD1
REMARK 470 LYS A 8 CG CD CE NZ
REMARK 470 ASP A 299 CG OD1 OD2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 1185 O HOH A 1185 5796 2.00
REMARK 500 O HOH A 1164 O HOH A 1164 6766 2.16
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 ILE A 3 139.87 -22.04
REMARK 500 VAL A 4 -1.92 -157.47
REMARK 500 PRO A 7 99.05 -25.67
REMARK 500 SER A 63 85.27 -151.97
REMARK 500 ASN A 85 -94.33 -138.81
REMARK 500 ASP A 109 115.80 -31.53
REMARK 500 SER A 139 -123.13 52.03
REMARK 500 ASP A 168 67.51 -106.74
REMARK 500 ASN A 240 -2.62 75.47
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 401
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 402
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 403
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MHH A 900
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3ICV RELATED DB: PDB
REMARK 900 STRUCTURAL CONSEQUENCES OF A CIRCULAR PERMUTATION ON LIPASE
REMARK 900 B FROM CANDIDA ANTARTICA
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE RECOMBINANT PROTEIN IS A "CIRCULAR PERMUTATION" OF LIPASE B
REMARK 999 IN WHICH THE C-TERMINAL SEQUENCE
REMARK 999 AAIVAGPKQNCEPDLMPYARPFAVGKRTCSGIVTP HAS BEEN MOVED TO THE N-
REMARK 999 TERMINUS WITH THE TP REPLACED WITH G. ALA82 AND THR114 REPRESENT
REMARK 999 VARIATIONS FROM THE PUBLISHED WILD TYPE SEQUENCE AND THEIR
REMARK 999 ACCURACY WAS CONFIRMED INDEPENDENTLY BY DNA SEQUENCING
DBREF 3ICW A 1 33 UNP P41365 LIPB_CANAR 308 340
DBREF 3ICW A 35 316 UNP P41365 LIPB_CANAR 26 307
SEQADV 3ICW ALA A 91 UNP P41365 THR 82 SEE REMARK 999
SEQADV 3ICW THR A 123 UNP P41365 ALA 114 SEE REMARK 999
SEQRES 1 A 316 ALA ALA ILE VAL ALA GLY PRO LYS GLN ASN CYS GLU PRO
SEQRES 2 A 316 ASP LEU MET PRO TYR ALA ARG PRO PHE ALA VAL GLY LYS
SEQRES 3 A 316 ARG THR CYS SER GLY ILE VAL GLY LEU PRO SER GLY SER
SEQRES 4 A 316 ASP PRO ALA PHE SER GLN PRO LYS SER VAL LEU ASP ALA
SEQRES 5 A 316 GLY LEU THR CYS GLN GLY ALA SER PRO SER SER VAL SER
SEQRES 6 A 316 LYS PRO ILE LEU LEU VAL PRO GLY THR GLY THR THR GLY
SEQRES 7 A 316 PRO GLN SER PHE ASP SER ASN TRP ILE PRO LEU SER ALA
SEQRES 8 A 316 GLN LEU GLY TYR THR PRO CYS TRP ILE SER PRO PRO PRO
SEQRES 9 A 316 PHE MET LEU ASN ASP THR GLN VAL ASN THR GLU TYR MET
SEQRES 10 A 316 VAL ASN ALA ILE THR THR LEU TYR ALA GLY SER GLY ASN
SEQRES 11 A 316 ASN LYS LEU PRO VAL LEU THR TRP SER GLN GLY GLY LEU
SEQRES 12 A 316 VAL ALA GLN TRP GLY LEU THR PHE PHE PRO SER ILE ARG
SEQRES 13 A 316 SER LYS VAL ASP ARG LEU MET ALA PHE ALA PRO ASP TYR
SEQRES 14 A 316 LYS GLY THR VAL LEU ALA GLY PRO LEU ASP ALA LEU ALA
SEQRES 15 A 316 VAL SER ALA PRO SER VAL TRP GLN GLN THR THR GLY SER
SEQRES 16 A 316 ALA LEU THR THR ALA LEU ARG ASN ALA GLY GLY LEU THR
SEQRES 17 A 316 GLN ILE VAL PRO THR THR ASN LEU TYR SER ALA THR ASP
SEQRES 18 A 316 GLU ILE VAL GLN PRO GLN VAL SER ASN SER PRO LEU ASP
SEQRES 19 A 316 SER SER TYR LEU PHE ASN GLY LYS ASN VAL GLN ALA GLN
SEQRES 20 A 316 ALA VAL CYS GLY PRO LEU PHE VAL ILE ASP HIS ALA GLY
SEQRES 21 A 316 SER LEU THR SER GLN PHE SER TYR VAL VAL GLY ARG SER
SEQRES 22 A 316 ALA LEU ARG SER THR THR GLY GLN ALA ARG SER ALA ASP
SEQRES 23 A 316 TYR GLY ILE THR ASP CYS ASN PRO LEU PRO ALA ASN ASP
SEQRES 24 A 316 LEU THR PRO GLU GLN LYS VAL ALA ALA ALA ALA LEU LEU
SEQRES 25 A 316 ALA PRO ALA ALA
HET NAG A 401 15
HET NAG A 402 15
HET PO4 A 403 5
HET MHH A 900 10
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM PO4 PHOSPHATE ION
HETNAM MHH METHYL HYDROGEN (R)-HEXYLPHOSPHONATE
HETSYN NAG NAG
FORMUL 2 NAG 2(C8 H15 N O6)
FORMUL 4 PO4 O4 P 3-
FORMUL 5 MHH C7 H17 O3 P
FORMUL 6 HOH *338(H2 O)
HELIX 1 1 ALA A 19 ALA A 23 5 5
HELIX 2 2 PRO A 46 ALA A 52 1 7
HELIX 3 3 THR A 77 ASP A 83 1 7
HELIX 4 4 ASN A 85 LEU A 93 1 9
HELIX 5 5 ASP A 109 SER A 128 1 20
HELIX 6 6 SER A 139 PHE A 152 1 14
HELIX 7 7 PRO A 153 ARG A 156 5 4
HELIX 8 8 ALA A 185 GLN A 191 1 7
HELIX 9 9 SER A 195 ALA A 204 1 10
HELIX 10 10 ALA A 246 GLY A 251 1 6
HELIX 11 11 ALA A 259 SER A 264 1 6
HELIX 12 12 SER A 264 SER A 277 1 14
HELIX 13 13 ARG A 283 TYR A 287 5 5
HELIX 14 14 GLY A 288 CYS A 292 5 5
SHEET 1 A 2 ARG A 27 THR A 28 0
SHEET 2 A 2 GLY A 31 ILE A 32 -1 O GLY A 31 N THR A 28
SHEET 1 B 7 LEU A 54 CYS A 56 0
SHEET 2 B 7 THR A 96 ILE A 100 -1 O TRP A 99 N THR A 55
SHEET 3 B 7 PRO A 67 VAL A 71 1 N LEU A 70 O CYS A 98
SHEET 4 B 7 LEU A 133 TRP A 138 1 O LEU A 136 N LEU A 69
SHEET 5 B 7 VAL A 159 PHE A 165 1 O PHE A 165 N THR A 137
SHEET 6 B 7 THR A 213 TYR A 217 1 O THR A 214 N ALA A 164
SHEET 7 B 7 LYS A 242 GLN A 245 1 O VAL A 244 N ASN A 215
SSBOND 1 CYS A 11 CYS A 29 1555 1555 2.04
SSBOND 2 CYS A 56 CYS A 98 1555 1555 2.04
SSBOND 3 CYS A 250 CYS A 292 1555 1555 2.03
LINK OG SER A 139 P MHH A 900 1555 1555 1.76
CISPEP 1 PRO A 103 PRO A 104 0 -0.51
CISPEP 2 GLN A 225 PRO A 226 0 0.11
SITE 1 AC1 3 VAL A 228 SER A 229 LEU A 233
SITE 1 AC2 6 PRO A 103 PRO A 104 ASN A 108 HOH A1181
SITE 2 AC2 6 HOH A1183 HOH A1224
SITE 1 AC3 5 LYS A 242 ARG A 283 SER A 284 HOH A 953
SITE 2 AC3 5 HOH A1069
SITE 1 AC4 5 THR A 74 SER A 139 GLN A 140 GLN A 191
SITE 2 AC4 5 HIS A 258
CRYST1 111.746 111.746 54.806 90.00 90.00 120.00 P 32 2 1 6
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 0.008949 0.005166 0.000000 0.00000
SCALE2 0.000000 0.010333 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018246 0.00000
TER 2198 ASP A 299
MASTER 350 0 4 14 9 0 7 6 2580 1 52 25
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