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HEADER HYDROLASE 29-AUG-24 9JCA
TITLE CALA-LIKE LIPASE FROM USTILAGO TRICHOPHORA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.1.3;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: USTILAGO TRICHOPHORA;
SOURCE 3 ORGANISM_TAXID: 86804;
SOURCE 4 STRAIN: USTILAGO TRICHOPHORA;
SOURCE 5 GENE: UTRI_04204_B;
SOURCE 6 EXPRESSION_SYSTEM: KOMAGATAELLA PASTORIS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: GS115;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PFAI2
KEYWDS ALPHA/BETA-HYDROLASES, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR B.XUE,L.H.LING,X.JIA,W.S.YEW
REVDAT 1 02-APR-25 9JCA 0
JRNL AUTH L.H.LING,E.T.CHUA,B.XUE,X.JIA,J.Y.CHOW,R.L.YANG,Y.P.LIM,
JRNL AUTH 2 P.HAN,H.XIE,C.H.TAN,G.K.T.NGUYEN,W.S.YEW
JRNL TITL SUSTAINABLE BIOSYNTHESIS OF DIVERSE FATTY ACID ESTERS OF
JRNL TITL 2 HYDROXY FATTY ACIDS (FAHFAS) FOR INDUSTRIAL PRODUCTION
JRNL REF ACS SUSTAIN CHEM ENG V. 13 2830 2025
JRNL REFN ESSN 2168-0485
JRNL DOI 10.1021/ACSSUSCHEMENG.4C08793
REMARK 2
REMARK 2 RESOLUTION. 3.33 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.20.1_4487
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) : 3.33
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.37
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 8936
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.225
REMARK 3 R VALUE (WORKING SET) : 0.221
REMARK 3 FREE R VALUE : 0.297
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.810
REMARK 3 FREE R VALUE TEST SET COUNT : 430
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 48.3700 - 4.8000 1.00 2991 150 0.1821 0.2494
REMARK 3 2 4.8000 - 3.8100 1.00 2802 137 0.2343 0.3236
REMARK 3 3 3.8100 - 3.3300 0.99 2713 143 0.3196 0.4047
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
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) : 0.580
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.290
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 95.49
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 88.09
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 : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
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 9JCA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-SEP-24.
REMARK 100 THE DEPOSITION ID IS D_1300050875.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-DEC-22
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.95372
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 X 9M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.7.8
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 8996
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.330
REMARK 200 RESOLUTION RANGE LOW (A) : 48.370
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 37.30
REMARK 200 R MERGE (I) : 0.21600
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 15.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.33
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.3
REMARK 200 DATA REDUNDANCY IN SHELL : 37.90
REMARK 200 R MERGE FOR SHELL (I) : 1.26800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.8.3
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.52
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M AMMONIUM ACETATE, 0.1M SODIUM
REMARK 280 CITRATE TRIBASIC DIHYDRATE PH 5.5, 24% V/V PEG 400, EVAPORATION,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
REMARK 290 7555 Y,X,-Z+1/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+2/3
REMARK 290 10555 -Y,-X,-Z+5/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/6
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 69.13233
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 138.26467
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 103.69850
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 172.83083
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 34.56617
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 69.13233
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 138.26467
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 172.83083
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 103.69850
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 34.56617
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: 5980 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 29750 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -48.0 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 0.00000
REMARK 350 BIOMT2 2 -0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -34.56617
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 VAL A 13
REMARK 465 MET A 14
REMARK 465 HIS A 15
REMARK 465 HIS A 16
REMARK 465 HIS A 17
REMARK 465 HIS A 18
REMARK 465 HIS A 19
REMARK 465 HIS A 20
REMARK 465 VAL A 21
REMARK 465 PRO A 22
REMARK 465 MET A 23
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 56 146.98 -170.23
REMARK 500 LYS A 82 61.22 60.98
REMARK 500 CYS A 117 3.31 -67.76
REMARK 500 LEU A 137 -100.10 -72.03
REMARK 500 GLN A 148 -6.11 -58.46
REMARK 500 ASP A 157 87.16 -64.67
REMARK 500 ASN A 187 51.19 32.82
REMARK 500 SER A 200 -117.73 40.38
REMARK 500 ALA A 207 -36.04 -35.79
REMARK 500 TYR A 227 148.16 -172.70
REMARK 500 GLU A 269 -50.12 -28.26
REMARK 500 LEU A 311 -67.16 62.03
REMARK 500 SER A 332 33.93 -84.14
REMARK 500 PHE A 340 159.29 -45.41
REMARK 500 HIS A 346 126.14 -171.66
REMARK 500 PRO A 349 40.57 -93.68
REMARK 500 ASP A 350 98.83 -61.75
REMARK 500 ASN A 371 74.08 -119.52
REMARK 500 PHE A 388 -72.85 -43.66
REMARK 500 ALA A 416 106.11 -55.06
REMARK 500 ASN A 421 12.82 -161.57
REMARK 500 PRO A 423 158.98 -49.28
REMARK 500 PRO A 456 172.01 -54.32
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 162 0.26 SIDE CHAIN
REMARK 500 ARG A 180 0.25 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF1 9JCA A 21 458 UNP A0A5C3EAQ1_9BASI
DBREF2 9JCA A A0A5C3EAQ1 21 458
SEQADV 9JCA VAL A 13 UNP A0A5C3EAQ EXPRESSION TAG
SEQADV 9JCA MET A 14 UNP A0A5C3EAQ EXPRESSION TAG
SEQADV 9JCA HIS A 15 UNP A0A5C3EAQ EXPRESSION TAG
SEQADV 9JCA HIS A 16 UNP A0A5C3EAQ EXPRESSION TAG
SEQADV 9JCA HIS A 17 UNP A0A5C3EAQ EXPRESSION TAG
SEQADV 9JCA HIS A 18 UNP A0A5C3EAQ EXPRESSION TAG
SEQADV 9JCA HIS A 19 UNP A0A5C3EAQ EXPRESSION TAG
SEQADV 9JCA HIS A 20 UNP A0A5C3EAQ EXPRESSION TAG
SEQRES 1 A 446 VAL MET HIS HIS HIS HIS HIS HIS VAL PRO MET GLU ARG
SEQRES 2 A 446 ARG ALA PRO PHE PRO ASP PRO ASN ASP ASP PRO PHE TYR
SEQRES 3 A 446 LYS THR PRO SER ASN ILE GLY THR TYR ALA ASN GLY GLN
SEQRES 4 A 446 VAL ILE GLN SER ARG LYS ALA PRO THR ASP ILE GLY ASN
SEQRES 5 A 446 GLN ASN GLY ALA ASP SER PHE GLN LEU SER TYR ARG THR
SEQRES 6 A 446 THR ASN THR GLN LYS GLU ALA GLN ALA ASN VAL ALA THR
SEQRES 7 A 446 VAL PHE ILE PRO SER LYS PRO ALA SER PRO PRO LYS ILE
SEQRES 8 A 446 PHE SER TYR GLN VAL TYR GLU ASP SER THR GLN LEU ASN
SEQRES 9 A 446 CYS ALA PRO SER TYR SER TYR LEU THR GLY PHE ASP GLU
SEQRES 10 A 446 PRO ASN LYS VAL THR THR VAL LEU ASP THR PRO ILE ILE
SEQRES 11 A 446 ILE SER TRP ALA LEU GLN GLN GLY TYR TYR VAL VAL SER
SEQRES 12 A 446 SER ASP HIS GLU GLY PRO ARG SER ALA PHE ILE ALA GLY
SEQRES 13 A 446 TYR GLU GLU GLY MET ALA ILE LEU ASP GLY ILE ARG ALA
SEQRES 14 A 446 PHE LYS ASN PHE LYS ASN LEU PRO GLU ASP ILE GLY VAL
SEQRES 15 A 446 GLY PHE TYR GLY TYR SER GLY GLY ALA HIS ALA THR ALA
SEQRES 16 A 446 TRP ALA VAL SER LEU ALA GLU GLY TYR ALA PRO GLU ILE
SEQRES 17 A 446 LYS ILE ASP GLY ALA ALA TYR GLY GLY THR PRO ALA SER
SEQRES 18 A 446 ALA LYS ASP THR PHE THR PHE LEU ASN LYS GLY PHE PHE
SEQRES 19 A 446 ALA GLY PHE ALA VAL ALA GLY VAL SER GLY LEU ALA LEU
SEQRES 20 A 446 ALA HIS PRO ASP MET GLU ALA PHE LEU GLU PRO ARG LEU
SEQRES 21 A 446 ASN ALA LYS GLY LYS GLN VAL PHE GLU GLN ILE ARG SER
SEQRES 22 A 446 ARG GLY PHE CYS LEU PRO SER VAL VAL LEU HIS ASN ASN
SEQRES 23 A 446 PHE VAL ASP VAL PHE SER LEU VAL ASN ASP THR ASN LEU
SEQRES 24 A 446 LEU ILE GLU GLU PRO ILE ALA GLY ILE LEU LYS GLN GLU
SEQRES 25 A 446 THR LEU VAL GLN ALA GLU ALA SER TYR THR VAL PRO VAL
SEQRES 26 A 446 PRO LYS PHE PRO ARG PHE MET TRP HIS ALA LEU PRO ASP
SEQRES 27 A 446 GLU ILE VAL PRO PHE GLN PRO ALA ALA ASN TYR VAL LYS
SEQRES 28 A 446 GLU GLN CYS GLN LYS GLY ALA ASN ILE ASN TRP ASN VAL
SEQRES 29 A 446 TYR PRO ILE ALA GLU HIS VAL THR ALA GLU ILE PHE GLY
SEQRES 30 A 446 LEU VAL PRO GLY LEU ASP PHE LEU SER LYS ALA PHE LYS
SEQRES 31 A 446 GLY GLN THR PRO LYS VAL ALA CYS GLY SER GLY VAL PRO
SEQRES 32 A 446 ALA ILE PRO GLY ILE ASN SER PRO SER THR GLN ASN VAL
SEQRES 33 A 446 LEU GLY SER ASP LEU ALA ASN GLN LEU ASN SER LEU LYS
SEQRES 34 A 446 GLY GLN GLN SER ALA PHE GLY LYS PRO PHE GLY SER VAL
SEQRES 35 A 446 SER PRO PRO LEU
HET NAG A 501 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
FORMUL 2 NAG C8 H15 N O6
HELIX 1 AA1 THR A 60 ASN A 66 1 7
HELIX 2 AA2 ALA A 118 LEU A 124 1 7
HELIX 3 AA3 ASN A 131 LEU A 137 1 7
HELIX 4 AA4 LEU A 137 GLN A 149 1 13
HELIX 5 AA5 ALA A 167 LYS A 186 1 20
HELIX 6 AA6 SER A 200 ALA A 217 1 18
HELIX 7 AA7 SER A 233 ASN A 242 1 10
HELIX 8 AA8 PHE A 246 HIS A 261 1 16
HELIX 9 AA9 HIS A 261 LEU A 272 1 12
HELIX 10 AB1 ASN A 273 ARG A 284 1 12
HELIX 11 AB2 CYS A 289 HIS A 296 1 8
HELIX 12 AB3 ASP A 301 VAL A 306 1 6
HELIX 13 AB4 PRO A 316 GLU A 324 1 9
HELIX 14 AB5 PRO A 354 LYS A 368 1 15
HELIX 15 AB6 GLU A 381 GLY A 389 1 9
HELIX 16 AB7 LEU A 390 LYS A 402 1 13
HELIX 17 AB8 SER A 424 GLY A 430 1 7
HELIX 18 AB9 GLY A 430 LEU A 440 1 11
SHEET 1 AA1 9 VAL A 52 LYS A 57 0
SHEET 2 AA1 9 ASP A 69 THR A 78 -1 O GLN A 72 N ARG A 56
SHEET 3 AA1 9 ALA A 84 ILE A 93 -1 O ASN A 87 N TYR A 75
SHEET 4 AA1 9 TYR A 152 SER A 156 -1 O SER A 155 N THR A 90
SHEET 5 AA1 9 LYS A 102 GLN A 107 1 N PHE A 104 O TYR A 152
SHEET 6 AA1 9 GLY A 193 GLY A 198 1 O GLY A 193 N ILE A 103
SHEET 7 AA1 9 ILE A 222 GLY A 228 1 O ALA A 226 N PHE A 196
SHEET 8 AA1 9 PRO A 341 ALA A 347 1 O PHE A 343 N TYR A 227
SHEET 9 AA1 9 ASN A 371 TYR A 377 1 O ASN A 371 N ARG A 342
SSBOND 1 CYS A 117 CYS A 289 1555 1555 2.02
SSBOND 2 CYS A 366 CYS A 410 1555 1555 2.02
LINK ND2 ASN A 307 C1 NAG A 501 1555 1555 1.44
CISPEP 1 SER A 99 PRO A 100 0 8.79
CISPEP 2 GLU A 315 PRO A 316 0 17.75
CRYST1 96.730 96.730 207.397 90.00 90.00 120.00 P 61 2 2 12
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 0.010338 0.005969 0.000000 0.00000
SCALE2 0.000000 0.011937 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004822 0.00000
TER 3324 LEU A 458
MASTER 305 0 1 18 9 0 0 6 3337 1 19 35
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