| content |
HEADER HYDROLASE 07-JAN-19 6NKG
TITLE CRYSTAL STRUCTURE OF THE LIPASE LIP_VUT5 FROM GOAT RUMEN METAGENOME.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIP_VUT5, C4L;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: METAGENOME;
SOURCE 3 ORGANISM_TAXID: 256318;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS LIPASE, GOAT RUMEN METAGENOMICS, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.KIM,L.WELK,G.MUKENDI,G.NKHI,T.MOTLOI,R.JEDRZEJCZAK,N.FETO,
AUTHOR 2 A.JOACHIMIAK
REVDAT 1 22-JAN-20 6NKG 0
JRNL AUTH Y.KIM,L.WELK,R.JEDRZEJCZAK,N.FETO,A.JOACHIMIAK
JRNL TITL CRYSTAL STRUCTURE OF THE LIPASE LIP_VUT5 FROM GOAT RUMEN
JRNL TITL 2 METAGENOME.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.15 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.13_2998
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 56.67
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 17706
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.197
REMARK 3 R VALUE (WORKING SET) : 0.195
REMARK 3 FREE R VALUE : 0.235
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.280
REMARK 3 FREE R VALUE TEST SET COUNT : 935
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 56.6875 - 4.1125 1.00 2604 136 0.1602 0.1754
REMARK 3 2 4.1125 - 3.2643 1.00 2409 155 0.1814 0.2697
REMARK 3 3 3.2643 - 2.8517 1.00 2385 128 0.2354 0.2568
REMARK 3 4 2.8517 - 2.5909 1.00 2375 138 0.2271 0.2381
REMARK 3 5 2.5909 - 2.4052 1.00 2308 132 0.2295 0.3003
REMARK 3 6 2.4052 - 2.2634 0.99 2369 131 0.2404 0.2652
REMARK 3 7 2.2634 - 2.1501 0.99 2321 115 0.2624 0.2932
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.240
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.580
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 38.97
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 52.00
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 : 0.002 2087
REMARK 3 ANGLE : 0.404 2825
REMARK 3 CHIRALITY : 0.037 296
REMARK 3 PLANARITY : 0.004 367
REMARK 3 DIHEDRAL : 14.982 1248
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 41 THROUGH 140 )
REMARK 3 ORIGIN FOR THE GROUP (A): -0.2994 28.1297 27.9200
REMARK 3 T TENSOR
REMARK 3 T11: 0.3401 T22: 0.3344
REMARK 3 T33: 0.3586 T12: 0.0141
REMARK 3 T13: -0.0124 T23: 0.0600
REMARK 3 L TENSOR
REMARK 3 L11: 1.0016 L22: 0.9148
REMARK 3 L33: 4.2242 L12: 0.0239
REMARK 3 L13: -0.3922 L23: 0.6143
REMARK 3 S TENSOR
REMARK 3 S11: -0.0263 S12: 0.0320 S13: 0.0463
REMARK 3 S21: 0.2210 S22: -0.0171 S23: 0.0091
REMARK 3 S31: 0.1050 S32: 0.2650 S33: 0.0265
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 141 THROUGH 157 )
REMARK 3 ORIGIN FOR THE GROUP (A): -11.0380 47.7677 42.4257
REMARK 3 T TENSOR
REMARK 3 T11: 0.6340 T22: 0.3522
REMARK 3 T33: 0.4215 T12: 0.0713
REMARK 3 T13: -0.0466 T23: -0.0063
REMARK 3 L TENSOR
REMARK 3 L11: 2.9351 L22: 2.7543
REMARK 3 L33: 5.1226 L12: -1.1461
REMARK 3 L13: 3.8669 L23: -1.2558
REMARK 3 S TENSOR
REMARK 3 S11: -0.3916 S12: -0.2012 S13: -0.0123
REMARK 3 S21: 0.8995 S22: 0.0404 S23: -0.2391
REMARK 3 S31: -0.2808 S32: -0.2510 S33: 0.1982
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 158 THROUGH 248 )
REMARK 3 ORIGIN FOR THE GROUP (A): 7.2788 30.5503 17.5612
REMARK 3 T TENSOR
REMARK 3 T11: 0.3226 T22: 0.4902
REMARK 3 T33: 0.3927 T12: -0.0303
REMARK 3 T13: -0.0072 T23: 0.0533
REMARK 3 L TENSOR
REMARK 3 L11: 1.6012 L22: 0.7202
REMARK 3 L33: 5.1962 L12: -0.5059
REMARK 3 L13: -0.5494 L23: 0.9291
REMARK 3 S TENSOR
REMARK 3 S11: -0.0004 S12: 0.1701 S13: 0.0886
REMARK 3 S21: 0.0653 S22: -0.0228 S23: -0.1670
REMARK 3 S31: -0.1587 S32: 0.9726 S33: 0.0264
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 4 THROUGH 40 )
REMARK 3 ORIGIN FOR THE GROUP (A): -9.2754 27.0589 19.4881
REMARK 3 T TENSOR
REMARK 3 T11: 0.2412 T22: 0.4498
REMARK 3 T33: 0.4213 T12: -0.0040
REMARK 3 T13: -0.0028 T23: -0.0076
REMARK 3 L TENSOR
REMARK 3 L11: 1.6145 L22: 2.8804
REMARK 3 L33: 4.1858 L12: 1.3590
REMARK 3 L13: 0.6857 L23: 0.9331
REMARK 3 S TENSOR
REMARK 3 S11: 0.1048 S12: -0.0085 S13: 0.1992
REMARK 3 S21: -0.0188 S22: -0.2518 S23: 0.4702
REMARK 3 S31: 0.0298 S32: -0.9621 S33: 0.2045
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 6NKG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-JAN-19.
REMARK 100 THE DEPOSITION ID IS D_1000238903.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-NOV-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.9
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9796
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 X 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17833
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.150
REMARK 200 RESOLUTION RANGE LOW (A) : 56.700
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 15.90
REMARK 200 R MERGE (I) : 0.11500
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 13.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.19
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 12.70
REMARK 200 R MERGE FOR SHELL (I) : 0.98100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: HKL-3000, MLPHARE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.08
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.62
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M MAGNESIUM ACETATE, 20 % PEG3350,
REMARK 280 PH 7.9, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 84.94900
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 30.05500
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 30.05500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 42.47450
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 30.05500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 30.05500
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 127.42350
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 30.05500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 30.05500
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 42.47450
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 30.05500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 30.05500
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 127.42350
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 84.94900
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 MSE A 1
REMARK 465 LYS A 2
REMARK 465 ILE A 3
REMARK 465 HIS A 249
REMARK 465 HIS A 250
REMARK 465 HIS A 251
REMARK 465 HIS A 252
REMARK 465 HIS A 253
REMARK 465 HIS A 254
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 SER A 93 -110.80 58.33
REMARK 500 ASP A 178 5.35 -69.02
REMARK 500 ASP A 178 3.97 -69.02
REMARK 500 HIS A 191 57.22 -101.16
REMARK 500 GLU A 208 40.33 -109.21
REMARK 500 GLN A 247 -57.75 60.34
REMARK 500 GLN A 247 -57.65 59.65
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 EDO A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACY A 303
DBREF 6NKG A 1 248 UNP Q65EQ1 Q65EQ1_BACLD 1 248
SEQADV 6NKG HIS A 249 UNP Q65EQ1 EXPRESSION TAG
SEQADV 6NKG HIS A 250 UNP Q65EQ1 EXPRESSION TAG
SEQADV 6NKG HIS A 251 UNP Q65EQ1 EXPRESSION TAG
SEQADV 6NKG HIS A 252 UNP Q65EQ1 EXPRESSION TAG
SEQADV 6NKG HIS A 253 UNP Q65EQ1 EXPRESSION TAG
SEQADV 6NKG HIS A 254 UNP Q65EQ1 EXPRESSION TAG
SEQRES 1 A 254 MSE LYS ILE VAL LYS PRO GLN PRO PHE THR PHE LYS GLY
SEQRES 2 A 254 GLY LYS LYS ALA VAL LEU LEU LEU HIS GLY PHE THR GLY
SEQRES 3 A 254 ASN THR ALA ASP VAL ARG MSE LEU GLY ARG TYR LEU ASN
SEQRES 4 A 254 GLU LYS GLY TYR THR CYS HIS ALA PRO GLN TYR LYS GLY
SEQRES 5 A 254 HIS GLY VAL PRO PRO GLU GLU LEU LEU SER THR GLY PRO
SEQRES 6 A 254 GLU ASP TRP TRP LYS ASP VAL MSE ASP GLY TYR GLU TYR
SEQRES 7 A 254 LEU LYS SER GLU GLY TYR GLU GLN ILE ALA ALA CYS GLY
SEQRES 8 A 254 LEU SER LEU GLY GLY VAL PHE SER LEU LYS LEU GLY TYR
SEQRES 9 A 254 THR VAL PRO ILE LYS GLY ILE VAL PRO MSE CYS ALA PRO
SEQRES 10 A 254 MSE TYR ILE LYS SER GLU GLU THR MSE TYR GLU GLY VAL
SEQRES 11 A 254 LEU ASP TYR ALA ARG ASN TYR LYS LYS PHE GLU GLY LYS
SEQRES 12 A 254 THR ALA GLU GLN ILE ASN ALA GLU MSE GLU GLU PHE LYS
SEQRES 13 A 254 LYS THR PRO MSE ASN THR LEU LYS ALA LEU GLN ASP LEU
SEQRES 14 A 254 ILE ALA ASP VAL ARG GLU HIS VAL ASP MSE ILE TYR SER
SEQRES 15 A 254 PRO THR PHE VAL VAL GLN ALA ARG HIS ASP HIS MSE ILE
SEQRES 16 A 254 ASN THR ASP SER ALA ASN ILE ILE TYR ASN GLU VAL GLU
SEQRES 17 A 254 THR ASP ASP LYS GLN LEU LYS TRP TYR GLU GLU SER GLY
SEQRES 18 A 254 HIS ALA ILE THR LEU ASP LYS GLU ARG GLU THR LEU HIS
SEQRES 19 A 254 LYS ASP VAL TYR GLN PHE LEU GLU THR LEU ASP TRP GLN
SEQRES 20 A 254 THR HIS HIS HIS HIS HIS HIS
MODRES 6NKG MSE A 33 MET MODIFIED RESIDUE
MODRES 6NKG MSE A 73 MET MODIFIED RESIDUE
MODRES 6NKG MSE A 114 MET MODIFIED RESIDUE
MODRES 6NKG MSE A 118 MET MODIFIED RESIDUE
MODRES 6NKG MSE A 126 MET MODIFIED RESIDUE
MODRES 6NKG MSE A 152 MET MODIFIED RESIDUE
MODRES 6NKG MSE A 160 MET MODIFIED RESIDUE
MODRES 6NKG MSE A 179 MET MODIFIED RESIDUE
MODRES 6NKG MSE A 194 MET MODIFIED RESIDUE
HET MSE A 33 16
HET MSE A 73 8
HET MSE A 114 8
HET MSE A 118 8
HET MSE A 126 8
HET MSE A 152 8
HET MSE A 160 8
HET MSE A 179 16
HET MSE A 194 8
HET EDO A 301 4
HET EDO A 302 4
HET ACY A 303 4
HETNAM MSE SELENOMETHIONINE
HETNAM EDO 1,2-ETHANEDIOL
HETNAM ACY ACETIC ACID
HETSYN EDO ETHYLENE GLYCOL
FORMUL 1 MSE 9(C5 H11 N O2 SE)
FORMUL 2 EDO 2(C2 H6 O2)
FORMUL 4 ACY C2 H4 O2
FORMUL 5 HOH *67(H2 O)
HELIX 1 AA1 ASN A 27 ASP A 30 5 4
HELIX 2 AA2 VAL A 31 LYS A 41 1 11
HELIX 3 AA3 PRO A 56 LEU A 61 1 6
HELIX 4 AA4 GLY A 64 GLU A 82 1 19
HELIX 5 AA5 SER A 93 TYR A 104 1 12
HELIX 6 AA6 SER A 122 GLU A 141 1 20
HELIX 7 AA7 THR A 144 LYS A 156 1 13
HELIX 8 AA8 THR A 162 GLU A 175 1 14
HELIX 9 AA9 HIS A 176 ILE A 180 5 5
HELIX 10 AB1 ASP A 198 VAL A 207 1 10
HELIX 11 AB2 GLU A 229 GLU A 242 1 14
SHEET 1 AA1 5 PHE A 9 PHE A 11 0
SHEET 2 AA1 5 THR A 44 ALA A 47 -1 O CYS A 45 N PHE A 11
SHEET 3 AA1 5 ALA A 17 LEU A 21 1 N VAL A 18 O THR A 44
SHEET 4 AA1 5 ILE A 87 LEU A 92 1 O ALA A 88 N LEU A 19
SHEET 5 AA1 5 ILE A 111 MSE A 114 1 O MSE A 114 N GLY A 91
SHEET 1 AA2 2 THR A 184 ALA A 189 0
SHEET 2 AA2 2 LYS A 212 TYR A 217 1 O GLN A 213 N VAL A 186
LINK C ARG A 32 N AMSE A 33 1555 1555 1.33
LINK C ARG A 32 N BMSE A 33 1555 1555 1.33
LINK C AMSE A 33 N LEU A 34 1555 1555 1.33
LINK C BMSE A 33 N LEU A 34 1555 1555 1.33
LINK C VAL A 72 N MSE A 73 1555 1555 1.33
LINK C MSE A 73 N ASP A 74 1555 1555 1.34
LINK C PRO A 113 N MSE A 114 1555 1555 1.33
LINK C MSE A 114 N CYS A 115 1555 1555 1.33
LINK C PRO A 117 N MSE A 118 1555 1555 1.33
LINK C MSE A 118 N TYR A 119 1555 1555 1.33
LINK C THR A 125 N MSE A 126 1555 1555 1.33
LINK C MSE A 126 N TYR A 127 1555 1555 1.34
LINK C GLU A 151 N MSE A 152 1555 1555 1.33
LINK C MSE A 152 N GLU A 153 1555 1555 1.34
LINK C PRO A 159 N MSE A 160 1555 1555 1.33
LINK C MSE A 160 N ASN A 161 1555 1555 1.33
LINK C ASP A 178 N AMSE A 179 1555 1555 1.33
LINK C ASP A 178 N BMSE A 179 1555 1555 1.33
LINK C AMSE A 179 N ILE A 180 1555 1555 1.33
LINK C BMSE A 179 N ILE A 180 1555 1555 1.33
LINK C HIS A 193 N MSE A 194 1555 1555 1.33
LINK C MSE A 194 N ILE A 195 1555 1555 1.33
SITE 1 AC1 5 PRO A 8 HIS A 46 ASP A 74 GLY A 75
SITE 2 AC1 5 EDO A 302
SITE 1 AC2 6 PRO A 48 GLN A 49 ASP A 71 ASP A 74
SITE 2 AC2 6 GLY A 75 EDO A 301
SITE 1 AC3 2 SER A 93 HOH A 413
CRYST1 60.110 60.110 169.898 90.00 90.00 90.00 P 41 21 2 8
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 0.016636 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016636 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005886 0.00000
TER 2024 THR A 248
MASTER 324 0 12 11 7 0 5 6 2051 1 118 20
END |