longtext: 6nkg-pdb

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