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HEADER HYDROLASE 20-AUG-21 7V6D
TITLE STRUCTURE OF LIPASE B FROM LASIODIPLODIA THEOBROMAE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE B;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LASIODIPLODIA THEOBROMAE;
SOURCE 3 ORGANISM_TAXID: 45133;
SOURCE 4 GENE: LIPB, DBV05_G2145;
SOURCE 5 EXPRESSION_SYSTEM: KOMAGATAELLA PASTORIS;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: GS115;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: GENOME INTEGRATED LINEARIZED VECTOR;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PPIC9K
KEYWDS ALPHA/BETA-HYDROLASES, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR B.XUE,H.F.ZHANG,G.K.T.NGUYEN,W.S.YEW
REVDAT 1 13-OCT-21 7V6D 0
JRNL AUTH A.M.J.NG,R.L.YANG,H.F.ZHANG,B.XUE,W.S.YEW,G.K.T.NGUYEN
JRNL TITL A NOVEL LIPASE FROM LASIODIPLODIA THEOBROMAE EFFICIENTLY
JRNL TITL 2 HYDROLYSES C8-C10 METHYL ESTERS FOR THE PREPARATION OF
JRNL TITL 3 MEDIUM-CHAIN TRIGLYCERIDES PRECURSORS
JRNL REF INT J MOL SCI V. 22 2021
JRNL REFN ESSN 1422-0067
JRNL DOI 10.3390/IJMS221910339
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.19.1_4122
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) : 29.70
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 31217
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.195
REMARK 3 R VALUE (WORKING SET) : 0.192
REMARK 3 FREE R VALUE : 0.243
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.980
REMARK 3 FREE R VALUE TEST SET COUNT : 1554
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 29.7000 - 5.5500 1.00 2871 131 0.1919 0.2300
REMARK 3 2 5.5500 - 4.4100 1.00 2757 137 0.1791 0.2111
REMARK 3 3 4.4100 - 3.8500 1.00 2703 145 0.1588 0.1950
REMARK 3 4 3.8500 - 3.5000 1.00 2731 119 0.1746 0.2275
REMARK 3 5 3.5000 - 3.2500 1.00 2658 141 0.1863 0.2170
REMARK 3 6 3.2500 - 3.0600 1.00 2687 151 0.2047 0.2436
REMARK 3 7 3.0600 - 2.9100 1.00 2656 149 0.2159 0.2885
REMARK 3 8 2.9100 - 2.7800 1.00 2661 140 0.2138 0.2962
REMARK 3 9 2.7800 - 2.6700 1.00 2647 141 0.2346 0.3288
REMARK 3 10 2.6700 - 2.5800 1.00 2643 150 0.2413 0.3756
REMARK 3 11 2.5800 - 2.5000 1.00 2649 150 0.2423 0.2947
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) : 0.280
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.230
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 37.48
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.73
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 7V6D COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-AUG-21.
REMARK 100 THE DEPOSITION ID IS D_1300024175.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-JUN-20
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.6
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) : 0.95373
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 9M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.7.4
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31233
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 29.700
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 13.60
REMARK 200 R MERGE (I) : 0.19100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.9000
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) : 2.60
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 14.00
REMARK 200 R MERGE FOR SHELL (I) : 1.20200
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
REMARK 200 STARTING MODEL: 6IDY
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.98
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 60% MPD, 100 MM NAOAC, PH 4.6, 10 MM
REMARK 280 CACL2, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
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,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z+1/2
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 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
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 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 32.71400
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 81.31950
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 83.33700
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 32.71400
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 81.31950
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 83.33700
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 32.71400
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 81.31950
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 83.33700
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 32.71400
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 81.31950
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 83.33700
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 620 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13810 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 90 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13660 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL
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 ALA A 19
REMARK 465 PRO A 20
REMARK 465 ALA A 21
REMARK 465 PRO A 22
REMARK 465 VAL A 23
REMARK 465 PRO A 24
REMARK 465 GLU A 25
REMARK 465 ASN A 26
REMARK 465 GLY A 27
REMARK 465 LEU A 28
REMARK 465 GLU A 29
REMARK 465 LYS A 30
REMARK 465 ARG A 31
REMARK 465 GLN A 32
REMARK 465 SER A 33
REMARK 465 LEU A 34
REMARK 465 SER A 35
REMARK 465 SER A 36
REMARK 465 VAL A 37
REMARK 465 LEU A 38
REMARK 465 SER A 39
REMARK 465 ALA A 40
REMARK 465 LEU A 41
REMARK 465 SER A 42
REMARK 465 GLY A 43
REMARK 465 LEU A 44
REMARK 465 THR A 45
REMARK 465 GLU A 46
REMARK 465 PRO A 47
REMARK 465 THR A 48
REMARK 465 ALA A 49
REMARK 465 ILE A 50
REMARK 465 LEU A 51
REMARK 465 SER A 52
REMARK 465 GLN A 53
REMARK 465 LEU A 54
REMARK 465 GLU A 55
REMARK 465 ALA A 56
REMARK 465 VAL A 57
REMARK 465 GLU A 58
REMARK 465 ALA A 59
REMARK 465 THR A 60
REMARK 465 SER A 61
REMARK 465 THR A 62
REMARK 465 PRO A 63
REMARK 465 THR A 64
REMARK 465 SER A 65
REMARK 465 VAL A 66
REMARK 465 GLU A 67
REMARK 465 GLN A 68
REMARK 465 ALA A 69
REMARK 465 GLN A 70
REMARK 465 GLU A 71
REMARK 465 GLN A 72
REMARK 465 LEU A 73
REMARK 465 GLU A 74
REMARK 465 ALA A 75
REMARK 465 ILE A 76
REMARK 465 TYR A 77
REMARK 465 GLY A 78
REMARK 465 THR A 79
REMARK 465 THR A 80
REMARK 465 PRO A 81
REMARK 465 THR A 82
REMARK 465 ALA B 19
REMARK 465 PRO B 20
REMARK 465 ALA B 21
REMARK 465 PRO B 22
REMARK 465 VAL B 23
REMARK 465 PRO B 24
REMARK 465 GLU B 25
REMARK 465 ASN B 26
REMARK 465 GLY B 27
REMARK 465 LEU B 28
REMARK 465 GLU B 29
REMARK 465 LYS B 30
REMARK 465 ARG B 31
REMARK 465 GLN B 32
REMARK 465 SER B 33
REMARK 465 LEU B 34
REMARK 465 SER B 35
REMARK 465 SER B 36
REMARK 465 VAL B 37
REMARK 465 LEU B 38
REMARK 465 SER B 39
REMARK 465 ALA B 40
REMARK 465 LEU B 41
REMARK 465 SER B 42
REMARK 465 GLY B 43
REMARK 465 LEU B 44
REMARK 465 THR B 45
REMARK 465 GLU B 46
REMARK 465 PRO B 47
REMARK 465 THR B 48
REMARK 465 ALA B 49
REMARK 465 ILE B 50
REMARK 465 LEU B 51
REMARK 465 SER B 52
REMARK 465 GLN B 53
REMARK 465 LEU B 54
REMARK 465 GLU B 55
REMARK 465 ALA B 56
REMARK 465 VAL B 57
REMARK 465 GLU B 58
REMARK 465 ALA B 59
REMARK 465 THR B 60
REMARK 465 SER B 61
REMARK 465 THR B 62
REMARK 465 PRO B 63
REMARK 465 THR B 64
REMARK 465 SER B 65
REMARK 465 VAL B 66
REMARK 465 GLU B 67
REMARK 465 GLN B 68
REMARK 465 ALA B 69
REMARK 465 GLN B 70
REMARK 465 GLU B 71
REMARK 465 GLN B 72
REMARK 465 LEU B 73
REMARK 465 GLU B 74
REMARK 465 ALA B 75
REMARK 465 ILE B 76
REMARK 465 TYR B 77
REMARK 465 GLY B 78
REMARK 465 THR B 79
REMARK 465 THR B 80
REMARK 465 PRO B 81
REMARK 465 THR B 82
REMARK 465 ASN B 83
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 ASN A 180 -117.05 -134.23
REMARK 500 SER A 235 -128.02 61.99
REMARK 500 TRP A 248 77.93 -112.21
REMARK 500 ASP A 264 75.27 -119.71
REMARK 500 GLN A 332 42.19 -153.30
REMARK 500 ASN B 180 -118.68 -133.49
REMARK 500 SER B 235 -124.81 58.17
REMARK 500 TRP B 248 79.08 -117.44
REMARK 500 PHE B 324 100.87 -164.67
REMARK 500 GLN B 332 45.49 -145.71
REMARK 500 ASP B 343 48.46 -145.54
REMARK 500 CYS B 404 3.85 -68.63
REMARK 500 MET B 445 153.80 -49.06
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 CA A 501 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 257 OD1
REMARK 620 2 ASP A 257 OD2 52.1
REMARK 620 3 ALA A 386 O 81.4 77.2
REMARK 620 4 HIS A 389 O 153.1 146.7 86.2
REMARK 620 5 GLY A 391 O 75.4 126.7 106.2 85.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 501 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 257 OD1
REMARK 620 2 ASP B 257 OD2 48.2
REMARK 620 3 ALA B 386 O 79.0 66.3
REMARK 620 4 HIS B 389 O 161.0 137.2 87.9
REMARK 620 5 GLY B 391 O 80.2 127.8 101.7 89.2
REMARK 620 N 1 2 3 4
DBREF1 7V6D A 19 449 UNP A0A5N5DNA6_9PEZI
DBREF2 7V6D A A0A5N5DNA6 19 449
DBREF1 7V6D B 19 449 UNP A0A5N5DNA6_9PEZI
DBREF2 7V6D B A0A5N5DNA6 19 449
SEQRES 1 A 431 ALA PRO ALA PRO VAL PRO GLU ASN GLY LEU GLU LYS ARG
SEQRES 2 A 431 GLN SER LEU SER SER VAL LEU SER ALA LEU SER GLY LEU
SEQRES 3 A 431 THR GLU PRO THR ALA ILE LEU SER GLN LEU GLU ALA VAL
SEQRES 4 A 431 GLU ALA THR SER THR PRO THR SER VAL GLU GLN ALA GLN
SEQRES 5 A 431 GLU GLN LEU GLU ALA ILE TYR GLY THR THR PRO THR ASN
SEQRES 6 A 431 ILE PHE GLU ASN ILE ALA GLN GLN ILE ALA ASP GLY LEU
SEQRES 7 A 431 SER THR LEU THR ILE VAL GLN ALA LEU GLY PHE SER PRO
SEQRES 8 A 431 SER GLY GLU ASN SER GLU THR ASN SER ASN THR ARG GLU
SEQRES 9 A 431 PRO SER THR THR ILE TYR PRO LYS LYS SER SER SER ASP
SEQRES 10 A 431 ALA PRO TYR SER ILE THR GLU GLU GLU LEU ARG GLN ALA
SEQRES 11 A 431 ILE TYR ILE PRO SER ASP PHE THR TYR GLY ASP LYS PRO
SEQRES 12 A 431 PRO VAL ILE PHE VAL PRO GLY THR GLY SER TYR GLY GLY
SEQRES 13 A 431 ILE SER PHE GLY SER ASN LEU ARG LYS LEU LEU THR GLY
SEQRES 14 A 431 VAL SER TYR ALA ASP PRO VAL TRP LEU ASN VAL PRO ASP
SEQRES 15 A 431 ALA LEU LEU ARG ASP ALA GLN THR ASN GLY GLU PHE VAL
SEQRES 16 A 431 ALA TYR ALA ILE ASN TYR ILE SER GLY ILE SER GLY ASP
SEQRES 17 A 431 ALA ASN VAL SER VAL VAL SER TRP SER GLN GLY GLY LEU
SEQRES 18 A 431 ASP THR GLN TRP ALA PHE THR TYR TRP PRO SER THR ARG
SEQRES 19 A 431 ALA LEU VAL SER ASP PHE VAL PRO VAL SER PRO ASP PHE
SEQRES 20 A 431 HIS GLY THR VAL LEU ALA ASN VAL ILE CYS LEU ASN PRO
SEQRES 21 A 431 GLY ALA GLY GLY VAL GLY LEU GLY PRO CYS ALA PRO ALA
SEQRES 22 A 431 VAL LEU GLN GLN GLU TYR ASN SER ASN PHE VAL THR ALA
SEQRES 23 A 431 LEU ARG ALA ALA GLY GLY ALA ASP ALA TYR VAL PRO THR
SEQRES 24 A 431 THR SER VAL PHE SER GLY PHE LEU ASP GLU ILE VAL GLN
SEQRES 25 A 431 PRO GLN SER GLY THR GLY ALA SER ALA TYR ILE ASN ASP
SEQRES 26 A 431 ALA ARG GLY VAL GLY THR THR ASN ALA GLU VAL GLN VAL
SEQRES 27 A 431 VAL CYS LYS GLY LYS GLY PRO ALA GLY GLY PHE TYR THR
SEQRES 28 A 431 HIS GLU SER LEU LEU VAL ASN PRO LEU THR TYR ALA LEU
SEQRES 29 A 431 LEU VAL ASP ALA LEU THR HIS ASP GLY PRO GLY SER VAL
SEQRES 30 A 431 ASP ARG LEU ASP LEU ASP THR VAL CYS SER THR VAL VAL
SEQRES 31 A 431 ALA PRO GLY LEU GLY LEU ASP ALA LEU LEU GLU ILE GLU
SEQRES 32 A 431 GLY VAL ASN VAL LEU ALA ALA VAL ASN LEU LEU THR TYR
SEQRES 33 A 431 SER ASP ARG ARG LEU ALA GLU PRO ALA LEU MET SER TYR
SEQRES 34 A 431 ALA ALA
SEQRES 1 B 431 ALA PRO ALA PRO VAL PRO GLU ASN GLY LEU GLU LYS ARG
SEQRES 2 B 431 GLN SER LEU SER SER VAL LEU SER ALA LEU SER GLY LEU
SEQRES 3 B 431 THR GLU PRO THR ALA ILE LEU SER GLN LEU GLU ALA VAL
SEQRES 4 B 431 GLU ALA THR SER THR PRO THR SER VAL GLU GLN ALA GLN
SEQRES 5 B 431 GLU GLN LEU GLU ALA ILE TYR GLY THR THR PRO THR ASN
SEQRES 6 B 431 ILE PHE GLU ASN ILE ALA GLN GLN ILE ALA ASP GLY LEU
SEQRES 7 B 431 SER THR LEU THR ILE VAL GLN ALA LEU GLY PHE SER PRO
SEQRES 8 B 431 SER GLY GLU ASN SER GLU THR ASN SER ASN THR ARG GLU
SEQRES 9 B 431 PRO SER THR THR ILE TYR PRO LYS LYS SER SER SER ASP
SEQRES 10 B 431 ALA PRO TYR SER ILE THR GLU GLU GLU LEU ARG GLN ALA
SEQRES 11 B 431 ILE TYR ILE PRO SER ASP PHE THR TYR GLY ASP LYS PRO
SEQRES 12 B 431 PRO VAL ILE PHE VAL PRO GLY THR GLY SER TYR GLY GLY
SEQRES 13 B 431 ILE SER PHE GLY SER ASN LEU ARG LYS LEU LEU THR GLY
SEQRES 14 B 431 VAL SER TYR ALA ASP PRO VAL TRP LEU ASN VAL PRO ASP
SEQRES 15 B 431 ALA LEU LEU ARG ASP ALA GLN THR ASN GLY GLU PHE VAL
SEQRES 16 B 431 ALA TYR ALA ILE ASN TYR ILE SER GLY ILE SER GLY ASP
SEQRES 17 B 431 ALA ASN VAL SER VAL VAL SER TRP SER GLN GLY GLY LEU
SEQRES 18 B 431 ASP THR GLN TRP ALA PHE THR TYR TRP PRO SER THR ARG
SEQRES 19 B 431 ALA LEU VAL SER ASP PHE VAL PRO VAL SER PRO ASP PHE
SEQRES 20 B 431 HIS GLY THR VAL LEU ALA ASN VAL ILE CYS LEU ASN PRO
SEQRES 21 B 431 GLY ALA GLY GLY VAL GLY LEU GLY PRO CYS ALA PRO ALA
SEQRES 22 B 431 VAL LEU GLN GLN GLU TYR ASN SER ASN PHE VAL THR ALA
SEQRES 23 B 431 LEU ARG ALA ALA GLY GLY ALA ASP ALA TYR VAL PRO THR
SEQRES 24 B 431 THR SER VAL PHE SER GLY PHE LEU ASP GLU ILE VAL GLN
SEQRES 25 B 431 PRO GLN SER GLY THR GLY ALA SER ALA TYR ILE ASN ASP
SEQRES 26 B 431 ALA ARG GLY VAL GLY THR THR ASN ALA GLU VAL GLN VAL
SEQRES 27 B 431 VAL CYS LYS GLY LYS GLY PRO ALA GLY GLY PHE TYR THR
SEQRES 28 B 431 HIS GLU SER LEU LEU VAL ASN PRO LEU THR TYR ALA LEU
SEQRES 29 B 431 LEU VAL ASP ALA LEU THR HIS ASP GLY PRO GLY SER VAL
SEQRES 30 B 431 ASP ARG LEU ASP LEU ASP THR VAL CYS SER THR VAL VAL
SEQRES 31 B 431 ALA PRO GLY LEU GLY LEU ASP ALA LEU LEU GLU ILE GLU
SEQRES 32 B 431 GLY VAL ASN VAL LEU ALA ALA VAL ASN LEU LEU THR TYR
SEQRES 33 B 431 SER ASP ARG ARG LEU ALA GLU PRO ALA LEU MET SER TYR
SEQRES 34 B 431 ALA ALA
HET NAG C 1 14
HET NAG C 2 14
HET CA A 501 1
HET CA B 501 1
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM CA CALCIUM ION
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 3 NAG 2(C8 H15 N O6)
FORMUL 4 CA 2(CA 2+)
FORMUL 6 HOH *118(H2 O)
HELIX 1 AA1 ASN A 83 SER A 97 1 15
HELIX 2 AA2 LEU A 99 LEU A 105 1 7
HELIX 3 AA3 SER A 110 SER A 114 5 5
HELIX 4 AA4 THR A 141 ALA A 148 1 8
HELIX 5 AA5 TYR A 172 GLY A 178 1 7
HELIX 6 AA6 ASN A 180 LEU A 185 1 6
HELIX 7 AA7 ASP A 205 ILE A 223 1 19
HELIX 8 AA8 SER A 235 TRP A 248 1 14
HELIX 9 AA9 PRO A 249 ALA A 253 5 5
HELIX 10 AB1 THR A 268 CYS A 275 1 8
HELIX 11 AB2 ALA A 289 GLN A 295 1 7
HELIX 12 AB3 SER A 299 ALA A 308 1 10
HELIX 13 AB4 SER A 333 ALA A 337 5 5
HELIX 14 AB5 VAL A 354 CYS A 358 1 5
HELIX 15 AB6 GLY A 362 GLY A 366 5 5
HELIX 16 AB7 GLU A 371 VAL A 375 5 5
HELIX 17 AB8 ASN A 376 THR A 388 1 13
HELIX 18 AB9 ASP A 399 CYS A 404 1 6
HELIX 19 AC1 GLY A 413 TYR A 434 1 22
HELIX 20 AC2 PHE B 85 SER B 97 1 13
HELIX 21 AC3 LEU B 99 LEU B 105 1 7
HELIX 22 AC4 SER B 110 SER B 114 5 5
HELIX 23 AC5 THR B 141 ALA B 148 1 8
HELIX 24 AC6 TYR B 172 GLY B 178 1 7
HELIX 25 AC7 ASN B 180 LEU B 185 1 6
HELIX 26 AC8 VAL B 198 LEU B 203 5 6
HELIX 27 AC9 ASP B 205 ILE B 223 1 19
HELIX 28 AD1 SER B 235 TRP B 248 1 14
HELIX 29 AD2 PRO B 249 ALA B 253 5 5
HELIX 30 AD3 THR B 268 CYS B 275 1 8
HELIX 31 AD4 ALA B 289 GLN B 295 1 7
HELIX 32 AD5 SER B 299 ALA B 308 1 10
HELIX 33 AD6 VAL B 354 CYS B 358 1 5
HELIX 34 AD7 GLY B 362 GLY B 366 5 5
HELIX 35 AD8 GLU B 371 VAL B 375 5 5
HELIX 36 AD9 ASN B 376 THR B 388 1 13
HELIX 37 AE1 ASP B 399 CYS B 404 1 6
HELIX 38 AE2 LEU B 414 TYR B 434 1 21
HELIX 39 AE3 MET B 445 ALA B 449 5 5
SHEET 1 AA1 5 ILE A 149 TYR A 150 0
SHEET 2 AA1 5 ASP A 192 LEU A 196 -1 O TRP A 195 N TYR A 150
SHEET 3 AA1 5 PRO A 162 VAL A 166 1 N PHE A 165 O VAL A 194
SHEET 4 AA1 5 VAL A 229 TRP A 234 1 O SER A 230 N ILE A 164
SHEET 5 AA1 5 VAL A 255 VAL A 261 1 O VAL A 261 N SER A 233
SHEET 1 AA2 2 THR A 317 PHE A 321 0
SHEET 2 AA2 2 THR A 349 GLU A 353 1 O ALA A 352 N SER A 319
SHEET 1 AA3 5 ILE B 149 TYR B 150 0
SHEET 2 AA3 5 ASP B 192 LEU B 196 -1 O TRP B 195 N TYR B 150
SHEET 3 AA3 5 PRO B 162 VAL B 166 1 N VAL B 163 O VAL B 194
SHEET 4 AA3 5 VAL B 229 TRP B 234 1 O SER B 230 N ILE B 164
SHEET 5 AA3 5 VAL B 255 VAL B 261 1 O VAL B 261 N SER B 233
SHEET 1 AA4 2 THR B 317 PHE B 321 0
SHEET 2 AA4 2 THR B 349 GLU B 353 1 O ALA B 352 N SER B 319
SSBOND 1 CYS A 275 CYS A 288 1555 1555 2.04
SSBOND 2 CYS A 358 CYS A 404 1555 1555 2.04
SSBOND 3 CYS B 275 CYS B 288 1555 1555 2.03
SSBOND 4 CYS B 358 CYS B 404 1555 1555 2.03
LINK ND2 ASN A 228 C1 NAG C 1 1555 1555 1.46
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.44
LINK OD1 ASP A 257 CA CA A 501 1555 1555 2.60
LINK OD2 ASP A 257 CA CA A 501 1555 1555 2.43
LINK O ALA A 386 CA CA A 501 1555 1555 2.30
LINK O HIS A 389 CA CA A 501 1555 1555 2.33
LINK O GLY A 391 CA CA A 501 1555 1555 2.35
LINK OD1 ASP B 257 CA CA B 501 1555 1555 2.45
LINK OD2 ASP B 257 CA CA B 501 1555 1555 2.88
LINK O ALA B 386 CA CA B 501 1555 1555 2.28
LINK O HIS B 389 CA CA B 501 1555 1555 2.31
LINK O GLY B 391 CA CA B 501 1555 1555 2.41
CISPEP 1 TYR A 128 PRO A 129 0 6.19
CISPEP 2 PHE A 324 LEU A 325 0 -26.94
CISPEP 3 GLN A 330 PRO A 331 0 -2.49
CISPEP 4 TYR B 128 PRO B 129 0 7.33
CISPEP 5 PHE B 324 LEU B 325 0 0.18
CISPEP 6 GLN B 330 PRO B 331 0 -5.82
CRYST1 65.428 162.639 166.674 90.00 90.00 90.00 I 2 2 2 16
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 0.015284 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006149 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006000 0.00000
TER 2716 ALA A 449
TER 5424 ALA B 449
MASTER 420 0 4 39 14 0 0 6 5570 2 51 68
END |