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HEADER HYDROLASE 03-NOV-21 7SPR
TITLE CRYSTAL STRUCTURE OF SMG1 MUTANT
TITLE 2 (G28C/P206C/Q34P/A37P/M176V/G177A/M294R/F278N)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIP1, SECRETORY LIPASE (FAMILY 3);
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MALASSEZIA GLOBOSA (STRAIN ATCC MYA-4612 / CBS
SOURCE 3 7966);
SOURCE 4 ORGANISM_COMMON: DANDRUFF-ASSOCIATED FUNGUS;
SOURCE 5 ORGANISM_TAXID: 425265;
SOURCE 6 STRAIN: ATCC MYA-4612 / CBS 7966;
SOURCE 7 GENE: MGL_0797;
SOURCE 8 EXPRESSION_SYSTEM: KOMAGATAELLA PHAFFII;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 460519
KEYWDS SMG1, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.L.LI,Y.H.WANG
REVDAT 1 10-MAY-23 7SPR 0
JRNL AUTH L.L.LI,Y.H.WANG
JRNL TITL LIPASE SMG1 THERMOSTABILITY OPTIMIZING THROUGH PROTEIN
JRNL TITL 2 DESIGN APPROACH
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.79 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.19.2_4158
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 : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.79
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.14
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.370
REMARK 3 COMPLETENESS FOR RANGE (%) : 79.9
REMARK 3 NUMBER OF REFLECTIONS : 37769
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.158
REMARK 3 R VALUE (WORKING SET) : 0.157
REMARK 3 FREE R VALUE : 0.183
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.020
REMARK 3 FREE R VALUE TEST SET COUNT : 1897
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 25.1400 - 4.3200 0.96 3082 152 0.1559 0.1804
REMARK 3 2 4.3200 - 3.4300 0.96 3098 153 0.1382 0.1478
REMARK 3 3 3.4300 - 3.0000 0.97 3102 165 0.1585 0.2032
REMARK 3 4 3.0000 - 2.7200 0.99 3179 170 0.1597 0.1636
REMARK 3 5 2.7200 - 2.5300 0.99 3172 184 0.1542 0.1686
REMARK 3 6 2.5300 - 2.3800 0.94 3019 160 0.1575 0.2220
REMARK 3 7 2.3800 - 2.2600 0.91 2932 157 0.1585 0.1925
REMARK 3 8 2.2600 - 2.1600 0.81 2581 141 0.1458 0.1495
REMARK 3 9 2.1600 - 2.0800 0.72 2319 116 0.1651 0.2104
REMARK 3 10 2.0800 - 2.0100 0.64 2030 116 0.1744 0.2200
REMARK 3 11 2.0100 - 1.9400 0.61 1972 97 0.1787 0.2143
REMARK 3 12 1.9400 - 1.8900 0.59 1904 103 0.1780 0.2034
REMARK 3 13 1.8900 - 1.8400 0.57 1840 94 0.1936 0.2292
REMARK 3 14 1.8400 - 1.7900 0.51 1642 89 0.2111 0.2614
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) : 0.152
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.995
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 17.82
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.07
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 : 0.008 2265
REMARK 3 ANGLE : 0.927 3080
REMARK 3 CHIRALITY : 0.060 333
REMARK 3 PLANARITY : 0.008 404
REMARK 3 DIHEDRAL : 7.341 320
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 28 THROUGH 56 )
REMARK 3 ORIGIN FOR THE GROUP (A): 23.7776 1.9013 -16.1065
REMARK 3 T TENSOR
REMARK 3 T11: 0.1648 T22: 0.0929
REMARK 3 T33: 0.1031 T12: -0.0164
REMARK 3 T13: -0.0054 T23: -0.0158
REMARK 3 L TENSOR
REMARK 3 L11: 3.8437 L22: 1.9913
REMARK 3 L33: 1.3052 L12: -0.0746
REMARK 3 L13: -0.0289 L23: -0.6728
REMARK 3 S TENSOR
REMARK 3 S11: 0.0508 S12: -0.1607 S13: 0.2052
REMARK 3 S21: 0.0967 S22: -0.0682 S23: -0.1029
REMARK 3 S31: -0.1143 S32: -0.0182 S33: 0.0227
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 57 THROUGH 89 )
REMARK 3 ORIGIN FOR THE GROUP (A): 3.2036 4.0730 -12.4902
REMARK 3 T TENSOR
REMARK 3 T11: 0.2521 T22: 0.3427
REMARK 3 T33: 0.2903 T12: 0.0792
REMARK 3 T13: 0.0681 T23: 0.0230
REMARK 3 L TENSOR
REMARK 3 L11: 5.1697 L22: 5.6290
REMARK 3 L33: 5.2645 L12: 0.5899
REMARK 3 L13: 0.1272 L23: 0.1908
REMARK 3 S TENSOR
REMARK 3 S11: -0.0572 S12: -0.6982 S13: 0.4806
REMARK 3 S21: 0.6466 S22: 0.4071 S23: 0.6450
REMARK 3 S31: -0.0719 S32: -0.7752 S33: -0.2362
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 90 THROUGH 164 )
REMARK 3 ORIGIN FOR THE GROUP (A): 9.9766 -11.3579 -16.9248
REMARK 3 T TENSOR
REMARK 3 T11: 0.1350 T22: 0.1639
REMARK 3 T33: 0.0903 T12: -0.0166
REMARK 3 T13: 0.0114 T23: 0.0456
REMARK 3 L TENSOR
REMARK 3 L11: 3.8512 L22: 3.4870
REMARK 3 L33: 1.6836 L12: -0.0498
REMARK 3 L13: -0.5252 L23: -1.0129
REMARK 3 S TENSOR
REMARK 3 S11: 0.0016 S12: -0.3623 S13: -0.4013
REMARK 3 S21: 0.3470 S22: -0.0064 S23: 0.2988
REMARK 3 S31: 0.0190 S32: -0.1404 S33: -0.0471
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 165 THROUGH 304 )
REMARK 3 ORIGIN FOR THE GROUP (A): 22.4860 -3.7681 -13.3908
REMARK 3 T TENSOR
REMARK 3 T11: 0.1389 T22: 0.1307
REMARK 3 T33: 0.0660 T12: -0.0073
REMARK 3 T13: -0.0028 T23: 0.0165
REMARK 3 L TENSOR
REMARK 3 L11: 3.6609 L22: 1.6282
REMARK 3 L33: 1.3623 L12: -0.0023
REMARK 3 L13: -0.5067 L23: -0.3430
REMARK 3 S TENSOR
REMARK 3 S11: 0.0441 S12: -0.5668 S13: 0.0877
REMARK 3 S21: 0.2385 S22: -0.0276 S23: -0.0724
REMARK 3 S31: -0.1129 S32: 0.0814 S33: -0.0101
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 7SPR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-NOV-21.
REMARK 100 THE DEPOSITION ID IS D_1000260861.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-JUN-21
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL18U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 37769
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.790
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 12.60
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 19.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.79
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.84
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: PHENIX
REMARK 200 STARTING MODEL: 3UUE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.73
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 150 MM POTASSIUM BROMIDE, 30% PEG 2000
REMARK 280 MME, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 24.02650
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 55.40200
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 24.49800
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 55.40200
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.02650
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 24.49800
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, 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 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 GLU A 77 CG CD OE1 OE2
REMARK 470 TYR A 79 CG CD1 CD2 CE1 CE2 CZ OH
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 OD1 ASP A 189 O HOH A 401 1.88
REMARK 500 O HOH A 548 O HOH A 582 1.89
REMARK 500 O HOH A 578 O HOH A 617 1.89
REMARK 500 OE1 GLU A 159 O HOH A 402 1.96
REMARK 500 O HOH A 516 O HOH A 569 1.96
REMARK 500 O HOH A 604 O HOH A 605 2.00
REMARK 500 O HOH A 533 O HOH A 581 2.09
REMARK 500 O HOH A 574 O HOH A 580 2.13
REMARK 500 O HOH A 496 O HOH A 549 2.16
REMARK 500 O HOH A 525 O HOH A 597 2.17
REMARK 500
REMARK 500 REMARK: NULL
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 601 O HOH A 616 3554 2.05
REMARK 500 O HOH A 437 O HOH A 461 1455 2.08
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 GLU A 77 -51.77 -143.20
REMARK 500 ALA A 80 -56.30 62.11
REMARK 500 TYR A 124 10.63 -140.74
REMARK 500 SER A 171 -133.52 65.31
REMARK 500 ASP A 245 136.58 81.05
REMARK 500 GLN A 282 40.58 -101.98
REMARK 500 ILE A 290 71.38 -106.68
REMARK 500 ALA A 292 -146.09 67.86
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 A 625 DISTANCE = 7.19 ANGSTROMS
DBREF 7SPR A 28 304 UNP A8PUY1 A8PUY1_MALGO 28 304
SEQADV 7SPR CYS A 28 UNP A8PUY1 GLY 28 ENGINEERED MUTATION
SEQADV 7SPR PRO A 34 UNP A8PUY1 GLN 34 ENGINEERED MUTATION
SEQADV 7SPR PRO A 37 UNP A8PUY1 ALA 37 ENGINEERED MUTATION
SEQADV 7SPR VAL A 176 UNP A8PUY1 MET 176 ENGINEERED MUTATION
SEQADV 7SPR ALA A 177 UNP A8PUY1 GLY 177 ENGINEERED MUTATION
SEQADV 7SPR CYS A 206 UNP A8PUY1 PRO 206 ENGINEERED MUTATION
SEQADV 7SPR ASN A 278 UNP A8PUY1 PHE 278 ENGINEERED MUTATION
SEQADV 7SPR ARG A 294 UNP A8PUY1 MET 294 ENGINEERED MUTATION
SEQRES 1 A 277 CYS GLY SER SER THR ASP PRO PRO VAL PRO ASN PRO TYR
SEQRES 2 A 277 ASN THR LYS GLU ILE SER LEU ALA ALA GLY LEU VAL GLN
SEQRES 3 A 277 GLN THR TYR CYS ASP SER THR GLU ASN GLY LEU LYS ILE
SEQRES 4 A 277 GLY ASP SER GLU LEU LEU TYR THR MET GLY GLU GLY TYR
SEQRES 5 A 277 ALA ARG GLN ARG VAL ASN ILE TYR HIS SER PRO SER LEU
SEQRES 6 A 277 GLY ILE ALA VAL ALA ILE GLU GLY THR ASN LEU PHE SER
SEQRES 7 A 277 LEU ASN SER ASP LEU HIS ASP ALA LYS PHE TRP GLN GLU
SEQRES 8 A 277 ASP PRO ASN GLU ARG TYR ILE GLN TYR TYR PRO LYS GLY
SEQRES 9 A 277 THR LYS LEU MET HIS GLY PHE GLN GLN ALA TYR ASN ASP
SEQRES 10 A 277 LEU MET ASP ASP ILE PHE THR ALA VAL LYS LYS TYR LYS
SEQRES 11 A 277 LYS GLU LYS ASN GLU LYS ARG VAL THR VAL ILE GLY HIS
SEQRES 12 A 277 SER LEU GLY ALA ALA VAL ALA LEU LEU CYS ALA MET ASP
SEQRES 13 A 277 ILE GLU LEU ARG MET ASP GLY GLY LEU TYR LYS THR TYR
SEQRES 14 A 277 LEU PHE GLY LEU PRO ARG LEU GLY ASN CYS THR PHE ALA
SEQRES 15 A 277 SER PHE VAL ASP GLN LYS ILE GLY ASP LYS PHE HIS SER
SEQRES 16 A 277 ILE ILE ASN GLY ARG ASP TRP VAL PRO THR VAL PRO PRO
SEQRES 17 A 277 ARG ALA LEU GLY TYR GLN HIS PRO SER ASP TYR VAL TRP
SEQRES 18 A 277 ILE TYR PRO GLY ASN SER THR SER ALA LYS LEU TYR PRO
SEQRES 19 A 277 GLY GLN GLU ASN VAL HIS GLY ILE LEU THR VAL ALA ARG
SEQRES 20 A 277 GLU PHE ASN ASN ASP ASP HIS GLN GLY ILE TYR PHE HIS
SEQRES 21 A 277 THR GLN ILE GLY ALA VAL ARG GLY GLU CYS PRO ALA GLN
SEQRES 22 A 277 VAL GLY ALA HIS
HET NAG B 1 14
HET NAG B 2 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 2(C8 H15 N O6)
FORMUL 3 HOH *225(H2 O)
HELIX 1 AA1 ASN A 41 GLN A 54 1 14
HELIX 2 AA2 THR A 55 CYS A 57 5 3
HELIX 3 AA3 ASP A 112 PHE A 115 5 4
HELIX 4 AA4 TYR A 124 TYR A 128 5 5
HELIX 5 AA5 HIS A 136 ASP A 144 1 9
HELIX 6 AA6 LEU A 145 ASN A 161 1 17
HELIX 7 AA7 SER A 171 MET A 188 1 18
HELIX 8 AA8 ASN A 205 GLY A 217 1 13
HELIX 9 AA9 TRP A 229 VAL A 233 5 5
HELIX 10 AB1 PRO A 235 GLY A 239 5 5
HELIX 11 AB2 GLY A 268 VAL A 272 5 5
HELIX 12 AB3 GLY A 291 GLY A 295 5 5
SHEET 1 AA110 VAL A 36 PRO A 37 0
SHEET 2 AA110 ALA A 257 TYR A 260 -1 O LEU A 259 N VAL A 36
SHEET 3 AA110 TYR A 246 ILE A 249 -1 N TYR A 246 O TYR A 260
SHEET 4 AA110 PHE A 220 ASN A 225 1 N ILE A 224 O ILE A 249
SHEET 5 AA110 LYS A 194 PHE A 198 1 N LEU A 197 O ILE A 223
SHEET 6 AA110 VAL A 165 HIS A 170 1 N GLY A 169 O PHE A 198
SHEET 7 AA110 GLY A 93 ILE A 98 1 N VAL A 96 O ILE A 168
SHEET 8 AA110 VAL A 84 SER A 89 -1 N ASN A 85 O ALA A 97
SHEET 9 AA110 SER A 69 MET A 75 -1 N LEU A 72 O ILE A 86
SHEET 10 AA110 LYS A 65 ILE A 66 -1 N ILE A 66 O SER A 69
SHEET 1 AA2 2 GLN A 117 GLU A 118 0
SHEET 2 AA2 2 LEU A 134 MET A 135 -1 O LEU A 134 N GLU A 118
SHEET 1 AA3 2 ILE A 284 TYR A 285 0
SHEET 2 AA3 2 THR A 288 GLN A 289 -1 O THR A 288 N TYR A 285
SSBOND 1 CYS A 28 CYS A 206 1555 1555 2.04
SSBOND 2 CYS A 57 CYS A 297 1555 1555 2.03
LINK ND2 ASN A 253 C1 NAG B 1 1555 1555 1.44
LINK O4 NAG B 1 C1 NAG B 2 1555 1555 1.43
CISPEP 1 VAL A 233 PRO A 234 0 -10.50
CISPEP 2 TYR A 250 PRO A 251 0 -0.23
CISPEP 3 CYS A 297 PRO A 298 0 -1.81
CRYST1 48.053 48.996 110.804 90.00 90.00 90.00 P 21 21 21 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 0.020810 0.000000 0.000000 0.00000
SCALE2 0.000000 0.020410 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009025 0.00000
TER 2179 HIS A 304
MASTER 347 0 2 12 14 0 0 6 2419 1 35 22
END |