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HEADER HYDROLASE 01-MAR-18 6CL4
TITLE LIPC12 - LIPASE FROM METAGENOMICS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE C12;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.1.3;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: UNCULTURED BACTERIUM;
SOURCE 3 ORGANISM_TAXID: 77133;
SOURCE 4 GENE: LIPC12;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS LIPASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.IULEK,V.P.MARTINI,N.KRIEGER,A.GLOGAUER,E.M.SOUZA
REVDAT 1 13-MAR-19 6CL4 0
JRNL AUTH V.P.MARTINI,N.KRIEGER,A.GLOGAUER,E.M.SOUZA,J.IULEK
JRNL TITL STRUCTURE SOLUTION AND ANALYSES OF THE FIRST TRUE LIPASE
JRNL TITL 2 OBTAINED FROM METAGENOMICS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.64 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
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) : 2.64
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.18
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 10487
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 : 0.251
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 503
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 48.1830 - 4.1901 0.99 2638 127 0.1757 0.2374
REMARK 3 2 4.1901 - 3.3260 1.00 2504 120 0.1761 0.2306
REMARK 3 3 3.3260 - 2.9057 1.00 2419 144 0.2160 0.2757
REMARK 3 4 2.9057 - 2.6400 0.99 2423 112 0.2400 0.2830
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.30
REMARK 3 SHRINKAGE RADIUS : 1.00
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.290
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.630
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 2250
REMARK 3 ANGLE : 0.447 3058
REMARK 3 CHIRALITY : 0.018 345
REMARK 3 PLANARITY : 0.002 400
REMARK 3 DIHEDRAL : 9.172 807
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A
REMARK 3 ORIGIN FOR THE GROUP (A): 4.5125 21.2000 22.0314
REMARK 3 T TENSOR
REMARK 3 T11: 0.1718 T22: 0.2189
REMARK 3 T33: 0.1874 T12: 0.0669
REMARK 3 T13: 0.0072 T23: 0.0056
REMARK 3 L TENSOR
REMARK 3 L11: 0.7649 L22: 1.2731
REMARK 3 L33: 3.0022 L12: 0.6386
REMARK 3 L13: 0.9212 L23: 1.0468
REMARK 3 S TENSOR
REMARK 3 S11: 0.0214 S12: -0.0749 S13: -0.0352
REMARK 3 S21: -0.0523 S22: -0.0010 S23: -0.0416
REMARK 3 S31: -0.0453 S32: -0.0924 S33: -0.0238
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 6CL4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-MAR-18.
REMARK 100 THE DEPOSITION ID IS D_1000230955.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-JUL-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS VERSION DECEMBER 28, 2009
REMARK 200 DATA SCALING SOFTWARE : XSCALE VERSION JANUARY 30, 2009
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 10489
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.640
REMARK 200 RESOLUTION RANGE LOW (A) : 58.500
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.5
REMARK 200 DATA REDUNDANCY : 8.820
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 18.9100
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.64
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.72
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.7
REMARK 200 DATA REDUNDANCY IN SHELL : 8.38
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 4.290
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: 1EX9
REMARK 200
REMARK 200 REMARK: NEEDLES
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.0 M SODIUM FORMATE AND 0.1 M BIS
REMARK 280 -TRIS PROPANE, PH 7.0 USING A PROTEIN CONCENTRATION OF 10 MG /
REMARK 280 ML. CRYSTALS GROWN FOR TEN WEEKS, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 2 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,X,Z+1/4
REMARK 290 4555 Y,-X,Z+3/4
REMARK 290 5555 -X,Y,-Z
REMARK 290 6555 X,-Y,-Z+1/2
REMARK 290 7555 Y,X,-Z+3/4
REMARK 290 8555 -Y,-X,-Z+1/4
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 96.35000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 48.17500
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 144.52500
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 96.35000
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 144.52500
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 48.17500
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 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 MET A -19
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 SER A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 LEU A -6
REMARK 465 VAL A -5
REMARK 465 PRO A -4
REMARK 465 ARG A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 SER A 2
REMARK 465 ALA A 3
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 LYS A 42 NZ
REMARK 470 GLU A 71 CD OE1 OE2
REMARK 470 LYS A 175 NZ
REMARK 470 LYS A 250 NZ
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 ILE A 25 -31.69 -133.52
REMARK 500 SER A 83 -104.91 57.84
REMARK 500 PRO A 125 96.05 -64.50
REMARK 500 ALA A 213 43.82 -149.23
REMARK 500 GLN A 236 78.40 -159.89
REMARK 500 LEU A 240 -33.26 -138.07
REMARK 500
REMARK 500 REMARK: NULL
DBREF 6CL4 A 1 293 UNP G1APT8 G1APT8_9BACT 1 293
SEQADV 6CL4 MET A -19 UNP G1APT8 EXPRESSION TAG
SEQADV 6CL4 GLY A -18 UNP G1APT8 EXPRESSION TAG
SEQADV 6CL4 SER A -17 UNP G1APT8 EXPRESSION TAG
SEQADV 6CL4 SER A -16 UNP G1APT8 EXPRESSION TAG
SEQADV 6CL4 HIS A -15 UNP G1APT8 EXPRESSION TAG
SEQADV 6CL4 HIS A -14 UNP G1APT8 EXPRESSION TAG
SEQADV 6CL4 HIS A -13 UNP G1APT8 EXPRESSION TAG
SEQADV 6CL4 HIS A -12 UNP G1APT8 EXPRESSION TAG
SEQADV 6CL4 HIS A -11 UNP G1APT8 EXPRESSION TAG
SEQADV 6CL4 HIS A -10 UNP G1APT8 EXPRESSION TAG
SEQADV 6CL4 SER A -9 UNP G1APT8 EXPRESSION TAG
SEQADV 6CL4 SER A -8 UNP G1APT8 EXPRESSION TAG
SEQADV 6CL4 GLY A -7 UNP G1APT8 EXPRESSION TAG
SEQADV 6CL4 LEU A -6 UNP G1APT8 EXPRESSION TAG
SEQADV 6CL4 VAL A -5 UNP G1APT8 EXPRESSION TAG
SEQADV 6CL4 PRO A -4 UNP G1APT8 EXPRESSION TAG
SEQADV 6CL4 ARG A -3 UNP G1APT8 EXPRESSION TAG
SEQADV 6CL4 GLY A -2 UNP G1APT8 EXPRESSION TAG
SEQADV 6CL4 SER A -1 UNP G1APT8 EXPRESSION TAG
SEQADV 6CL4 HIS A 0 UNP G1APT8 EXPRESSION TAG
SEQRES 1 A 313 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 313 LEU VAL PRO ARG GLY SER HIS MET SER ALA SER SER LEU
SEQRES 3 A 313 LYS PHE PRO ILE VAL LEU VAL HIS GLY LEU LEU GLY PHE
SEQRES 4 A 313 ASP LYS ILE GLY GLY ILE TYR PRO TYR PHE TYR GLY ILE
SEQRES 5 A 313 LYS GLU ALA LEU GLU LYS ALA GLY ALA LYS VAL TYR ILE
SEQRES 6 A 313 ALA THR LEU SER ALA LEU ASN SER ASN GLU LEU ARG GLY
SEQRES 7 A 313 GLU GLN LEU LEU GLU PHE VAL ARG LYS VAL GLN ALA GLU
SEQRES 8 A 313 THR GLY ALA ALA LYS VAL ASN LEU ILE GLY HIS SER GLN
SEQRES 9 A 313 GLY PRO LEU ALA CYS ARG TYR VAL ALA ALA THR HIS PRO
SEQRES 10 A 313 GLU LEU ILE ALA SER VAL THR SER VAL ASN GLY VAL ASN
SEQRES 11 A 313 HIS GLY SER GLU VAL ALA ASP LEU VAL ARG LEU ALA LEU
SEQRES 12 A 313 THR PRO GLY ARG LEU PRO GLU SER ILE ALA ASN ALA ALA
SEQRES 13 A 313 MET SER ALA PHE GLY GLN LEU LEU SER ALA LEU ALA GLY
SEQRES 14 A 313 SER PRO ARG LEU PRO GLN SER GLY ILE GLU ALA LEU GLU
SEQRES 15 A 313 ALA LEU THR SER GLU GLY VAL ALA ALA PHE ASN ASN LYS
SEQRES 16 A 313 TYR PRO GLN GLY LEU PRO ALA GLU TRP GLY GLY GLU GLY
SEQRES 17 A 313 LYS GLU LEU VAL ASN GLY VAL TYR TYR TYR SER TRP SER
SEQRES 18 A 313 GLY VAL ILE ASP TYR ASN PRO LEU HIS GLN GLY ALA ASN
SEQRES 19 A 313 ASN LEU ASP PRO LEU HIS VAL ALA MET LEU ALA PHE SER
SEQRES 20 A 313 ILE LEU PHE THR ASN GLU ARG PHE GLN ASN ASP GLY LEU
SEQRES 21 A 313 VAL GLY ARG TYR SER SER HIS LEU GLY LYS VAL ILE GLY
SEQRES 22 A 313 SER ASP TYR SER MET ASP HIS VAL ASP ALA ILE ASN GLN
SEQRES 23 A 313 LEU ALA GLY VAL VAL ALA ASN ASN THR ASP PRO VAL GLN
SEQRES 24 A 313 LEU PHE VAL GLU HIS VAL ALA ARG LEU LYS SER LYS GLY
SEQRES 25 A 313 LEU
FORMUL 2 HOH *150(H2 O)
HELIX 1 AA1 GLY A 31 ALA A 39 1 9
HELIX 2 AA2 SER A 53 GLY A 73 1 21
HELIX 3 AA3 GLN A 84 HIS A 96 1 13
HELIX 4 AA4 SER A 113 ARG A 120 1 8
HELIX 5 AA5 LEU A 121 THR A 124 5 4
HELIX 6 AA6 PRO A 129 GLY A 149 1 21
HELIX 7 AA7 LEU A 153 SER A 156 5 4
HELIX 8 AA8 GLY A 157 GLU A 162 1 6
HELIX 9 AA9 THR A 165 ASN A 174 1 10
HELIX 10 AB1 ASP A 217 LEU A 229 1 13
HELIX 11 AB2 ARG A 243 HIS A 247 5 5
HELIX 12 AB3 VAL A 261 ASN A 265 5 5
HELIX 13 AB4 ASP A 276 LYS A 291 1 16
SHEET 1 AA1 6 VAL A 43 ILE A 45 0
SHEET 2 AA1 6 ILE A 10 VAL A 13 1 N ILE A 10 O TYR A 44
SHEET 3 AA1 6 VAL A 77 HIS A 82 1 O ILE A 80 N VAL A 13
SHEET 4 AA1 6 ILE A 100 VAL A 106 1 O THR A 104 N LEU A 79
SHEET 5 AA1 6 VAL A 195 VAL A 203 1 O TYR A 196 N VAL A 103
SHEET 6 AA1 6 LEU A 191 VAL A 192 -1 N VAL A 192 O VAL A 195
SHEET 1 AA2 6 VAL A 43 ILE A 45 0
SHEET 2 AA2 6 ILE A 10 VAL A 13 1 N ILE A 10 O TYR A 44
SHEET 3 AA2 6 VAL A 77 HIS A 82 1 O ILE A 80 N VAL A 13
SHEET 4 AA2 6 ILE A 100 VAL A 106 1 O THR A 104 N LEU A 79
SHEET 5 AA2 6 VAL A 195 VAL A 203 1 O TYR A 196 N VAL A 103
SHEET 6 AA2 6 LYS A 250 SER A 257 1 O TYR A 256 N VAL A 203
SHEET 1 AA3 2 LYS A 21 ILE A 22 0
SHEET 2 AA3 2 TYR A 26 PRO A 27 -1 O TYR A 26 N ILE A 22
CISPEP 1 GLN A 266 LEU A 267 0 3.39
CRYST1 58.500 58.500 192.700 90.00 90.00 90.00 P 41 2 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 0.017094 0.000000 0.000000 0.00000
SCALE2 0.000000 0.017094 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005189 0.00000
TER 2204 LEU A 293
MASTER 286 0 0 13 14 0 0 6 2331 1 0 25
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