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HEADER HYDROLASE 04-OCT-21 7SFM
TITLE MYCOBACTERIUM TUBERCULOSIS HIP1 CRYSTAL STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HIP1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PROTEASE;
COMPND 5 EC: 3.4.-.-,3.4.14.-;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 1773;
SOURCE 4 GENE: TAP;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS MTB, AEBSF, TB, TUBERCULOSIS, SERINE HYDROLASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.A.OSTROV,D.LI
REVDAT 1 24-AUG-22 7SFM 0
JRNL AUTH D.A.OSTROV,D.LI,N.GOLDFARB
JRNL TITL MYCOBACTERIUM TUBERCULOSIS HIP1 CRYSTAL STRUCTURE
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.46
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 44549
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.176
REMARK 3 R VALUE (WORKING SET) : 0.175
REMARK 3 FREE R VALUE : 0.205
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.480
REMARK 3 FREE R VALUE TEST SET COUNT : 1996
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 29.4600 - 5.1713 1.00 3222 151 0.1900 0.1971
REMARK 3 2 5.1713 - 4.1081 1.00 3116 143 0.1572 0.1970
REMARK 3 3 4.1081 - 3.5899 1.00 3069 148 0.1538 0.1656
REMARK 3 4 3.5899 - 3.2621 1.00 3059 140 0.1645 0.1721
REMARK 3 5 3.2621 - 3.0285 1.00 3047 143 0.1778 0.1976
REMARK 3 6 3.0285 - 2.8501 1.00 3021 144 0.1776 0.2165
REMARK 3 7 2.8501 - 2.7075 0.99 3024 144 0.1796 0.2362
REMARK 3 8 2.7075 - 2.5897 0.99 3022 142 0.1760 0.2058
REMARK 3 9 2.5897 - 2.4901 0.99 3013 143 0.1802 0.2211
REMARK 3 10 2.4901 - 2.4042 0.99 3007 139 0.1787 0.2347
REMARK 3 11 2.4042 - 2.3290 0.99 2962 139 0.1887 0.2372
REMARK 3 12 2.3290 - 2.2625 0.99 3009 137 0.1920 0.2361
REMARK 3 13 2.2625 - 2.2030 0.99 2996 141 0.1892 0.2547
REMARK 3 14 2.2030 - 2.1492 0.99 2986 142 0.2035 0.2525
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) : 0.190
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.490
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.75
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 7SFM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-OCT-21.
REMARK 100 THE DEPOSITION ID IS D_1000259306.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-OCT-14
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 : NSLS
REMARK 200 BEAMLINE : X6A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9436
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 44555
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.149
REMARK 200 RESOLUTION RANGE LOW (A) : 29.464
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 1.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 17.0000
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) : 2.23
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: 5UGQ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 68.86
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.95
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 3350, 0.1M SODIUM ACETATE PH
REMARK 280 5.6, 0.2 M AMMONIUM SULFATE AND 10% GLYCEROL, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 42.60067
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 85.20133
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 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 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 85.20133
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 42.60067
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 SER A 29
REMARK 465 SER A 30
REMARK 465 ASN A 31
REMARK 465 PRO A 32
REMARK 465 GLN A 33
REMARK 465 VAL A 34
REMARK 465 LYS A 35
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 ALA A 19 67.50 -29.96
REMARK 500 ALA A 117 -114.37 53.45
REMARK 500 CYS A 125 -53.13 -122.44
REMARK 500 SER A 200 -109.01 41.49
REMARK 500 ARG A 290 74.07 -118.33
REMARK 500 THR A 463 162.43 74.59
REMARK 500 VAL A 464 -19.57 -155.17
REMARK 500
REMARK 500 REMARK: NULL
DBREF1 7SFM A 20 492 UNP A0A654TLU9_MYCTX
DBREF2 7SFM A A0A654TLU9 46 518
SEQADV 7SFM ALA A 14 UNP A0A654TLU EXPRESSION TAG
SEQADV 7SFM ALA A 15 UNP A0A654TLU EXPRESSION TAG
SEQADV 7SFM ALA A 16 UNP A0A654TLU EXPRESSION TAG
SEQADV 7SFM ALA A 17 UNP A0A654TLU EXPRESSION TAG
SEQADV 7SFM LEU A 18 UNP A0A654TLU EXPRESSION TAG
SEQADV 7SFM ALA A 19 UNP A0A654TLU EXPRESSION TAG
SEQRES 1 A 479 ALA ALA ALA ALA LEU ALA GLN PRO VAL GLU TRP THR PRO
SEQRES 2 A 479 CYS ARG SER SER ASN PRO GLN VAL LYS ILE PRO GLY GLY
SEQRES 3 A 479 ALA LEU CYS GLY LYS LEU ALA VAL PRO VAL ASP TYR ASP
SEQRES 4 A 479 ARG PRO ASP GLY ASP VAL ALA ALA LEU ALA LEU ILE ARG
SEQRES 5 A 479 PHE PRO ALA THR GLY ASP LYS ILE GLY SER LEU VAL ILE
SEQRES 6 A 479 ASN PRO GLY GLY PRO GLY GLU SER GLY ILE GLU ALA ALA
SEQRES 7 A 479 LEU GLY VAL PHE GLN THR LEU PRO LYS ARG VAL HIS GLU
SEQRES 8 A 479 ARG PHE ASP LEU VAL GLY PHE ASP PRO ARG GLY VAL ALA
SEQRES 9 A 479 SER SER ARG PRO ALA ILE TRP CYS ASN SER ASP ALA ASP
SEQRES 10 A 479 ASN ASP ARG LEU ARG ALA GLU PRO GLN VAL ASP TYR SER
SEQRES 11 A 479 ARG GLU GLY VAL ALA HIS ILE GLU ASN GLU THR LYS GLN
SEQRES 12 A 479 PHE VAL GLY ARG CYS VAL ASP LYS MSE GLY LYS ASN PHE
SEQRES 13 A 479 LEU ALA HIS VAL GLY THR VAL ASN VAL ALA LYS ASP LEU
SEQRES 14 A 479 ASP ALA ILE ARG ALA ALA LEU GLY ASP ASP LYS LEU THR
SEQRES 15 A 479 TYR LEU GLY TYR SER TYR GLY THR ARG ILE GLY SER ALA
SEQRES 16 A 479 TYR ALA GLU GLU PHE PRO GLN ARG VAL ARG ALA MSE ILE
SEQRES 17 A 479 LEU ASP GLY ALA VAL ASP PRO ASN ALA ASP PRO ILE GLU
SEQRES 18 A 479 ALA GLU LEU ARG GLN ALA LYS GLY PHE GLN ASP ALA PHE
SEQRES 19 A 479 ASN ASN TYR ALA ALA ASP CYS ALA LYS ASN ALA GLY CYS
SEQRES 20 A 479 PRO LEU GLY ALA ASP PRO ALA LYS ALA VAL GLU VAL TYR
SEQRES 21 A 479 HIS SER LEU VAL ASP PRO LEU VAL ASP PRO ASP ASN PRO
SEQRES 22 A 479 ARG ILE SER ARG PRO ALA ARG THR LYS ASP PRO ARG GLY
SEQRES 23 A 479 LEU SER TYR SER ASP ALA ILE VAL GLY THR ILE MSE ALA
SEQRES 24 A 479 LEU TYR SER PRO ASN LEU TRP GLN HIS LEU THR ASP GLY
SEQRES 25 A 479 LEU SER GLU LEU VAL ASP ASN ARG GLY ASP THR LEU LEU
SEQRES 26 A 479 ALA LEU ALA ASP MSE TYR MSE ARG ARG ASP SER HIS GLY
SEQRES 27 A 479 ARG TYR ASN ASN SER GLY ASP ALA ARG VAL ALA ILE ASN
SEQRES 28 A 479 CYS VAL ASP GLN PRO PRO VAL THR ASP ARG ASP LYS VAL
SEQRES 29 A 479 ILE ASP GLU ASP ARG ARG ALA ARG GLU ILE ALA PRO PHE
SEQRES 30 A 479 MSE SER TYR GLY LYS PHE THR GLY ASP ALA PRO LEU GLY
SEQRES 31 A 479 THR CYS ALA PHE TRP PRO VAL PRO PRO THR SER GLN PRO
SEQRES 32 A 479 HIS ALA VAL SER ALA PRO GLY LEU VAL PRO THR VAL VAL
SEQRES 33 A 479 VAL SER THR THR HIS ASP PRO ALA THR PRO TYR LYS ALA
SEQRES 34 A 479 GLY VAL ASP LEU ALA ASN GLN LEU ARG GLY SER LEU LEU
SEQRES 35 A 479 THR PHE ASP GLY THR GLN HIS THR VAL VAL PHE GLN GLY
SEQRES 36 A 479 ASP SER CYS ILE ASP GLU TYR VAL THR ALA TYR LEU ILE
SEQRES 37 A 479 GLY GLY THR THR PRO PRO SER GLY ALA LYS CYS
MODRES 7SFM MSE A 165 MET MODIFIED RESIDUE
MODRES 7SFM MSE A 220 MET MODIFIED RESIDUE
MODRES 7SFM MSE A 311 MET MODIFIED RESIDUE
MODRES 7SFM MSE A 343 MET MODIFIED RESIDUE
MODRES 7SFM MSE A 345 MET MODIFIED RESIDUE
MODRES 7SFM MSE A 391 MET MODIFIED RESIDUE
HET MSE A 165 8
HET MSE A 220 8
HET MSE A 311 8
HET MSE A 343 8
HET MSE A 345 8
HET MSE A 391 8
HET GOL A 501 6
HET GOL A 502 6
HET GOL A 503 6
HET GOL A 504 6
HET ACT A 505 4
HETNAM MSE SELENOMETHIONINE
HETNAM GOL GLYCEROL
HETNAM ACT ACETATE ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 1 MSE 6(C5 H11 N O2 SE)
FORMUL 2 GOL 4(C3 H8 O3)
FORMUL 6 ACT C2 H3 O2 1-
FORMUL 7 HOH *466(H2 O)
HELIX 1 AA1 SER A 86 LEU A 98 1 13
HELIX 2 AA2 PRO A 99 ARG A 105 1 7
HELIX 3 AA3 SER A 127 ALA A 136 1 10
HELIX 4 AA4 SER A 143 GLY A 166 1 24
HELIX 5 AA5 GLY A 166 HIS A 172 1 7
HELIX 6 AA6 GLY A 174 LEU A 189 1 16
HELIX 7 AA7 TYR A 201 PHE A 213 1 13
HELIX 8 AA8 ASP A 231 LYS A 256 1 26
HELIX 9 AA9 ASP A 265 ALA A 267 5 3
HELIX 10 AB1 LYS A 268 ASP A 278 1 11
HELIX 11 AB2 PRO A 279 VAL A 281 5 3
HELIX 12 AB3 SER A 301 LEU A 313 1 13
HELIX 13 AB4 TYR A 314 ASN A 317 5 4
HELIX 14 AB5 LEU A 318 ASP A 331 1 14
HELIX 15 AB6 GLY A 334 ARG A 346 1 13
HELIX 16 AB7 ASN A 355 ASP A 367 1 13
HELIX 17 AB8 ASP A 373 ALA A 388 1 16
HELIX 18 AB9 PRO A 389 SER A 392 5 4
HELIX 19 AC1 GLY A 403 TRP A 408 5 6
HELIX 20 AC2 PRO A 439 ARG A 451 1 13
HELIX 21 AC3 ASP A 469 GLY A 483 1 15
SHEET 1 AA110 THR A 25 PRO A 26 0
SHEET 2 AA110 LEU A 41 PRO A 48 -1 O CYS A 42 N THR A 25
SHEET 3 AA110 VAL A 58 PHE A 66 -1 O LEU A 61 N LEU A 45
SHEET 4 AA110 PHE A 106 PHE A 111 -1 O LEU A 108 N PHE A 66
SHEET 5 AA110 GLY A 74 ASN A 79 1 N LEU A 76 O ASP A 107
SHEET 6 AA110 LEU A 194 TYR A 199 1 O THR A 195 N VAL A 77
SHEET 7 AA110 VAL A 217 ASP A 223 1 O ILE A 221 N GLY A 198
SHEET 8 AA110 VAL A 428 THR A 432 1 O VAL A 428 N LEU A 222
SHEET 9 AA110 SER A 453 PHE A 457 1 O SER A 453 N VAL A 429
SHEET 10 AA110 LYS A 491 CYS A 492 1 O CYS A 492 N THR A 456
SSBOND 1 CYS A 27 CYS A 42 1555 1555 2.05
SSBOND 2 CYS A 125 CYS A 161 1555 1555 2.04
SSBOND 3 CYS A 254 CYS A 260 1555 1555 2.06
SSBOND 4 CYS A 365 CYS A 405 1555 1555 2.03
SSBOND 5 CYS A 471 CYS A 492 1555 1555 2.08
LINK C LYS A 164 N MSE A 165 1555 1555 1.33
LINK C MSE A 165 N GLY A 166 1555 1555 1.33
LINK C ALA A 219 N MSE A 220 1555 1555 1.33
LINK C MSE A 220 N ILE A 221 1555 1555 1.33
LINK C ILE A 310 N MSE A 311 1555 1555 1.33
LINK C MSE A 311 N ALA A 312 1555 1555 1.33
LINK C ASP A 342 N MSE A 343 1555 1555 1.33
LINK C MSE A 343 N TYR A 344 1555 1555 1.34
LINK C TYR A 344 N MSE A 345 1555 1555 1.34
LINK C MSE A 345 N ARG A 346 1555 1555 1.34
LINK C PHE A 390 N MSE A 391 1555 1555 1.33
LINK C MSE A 391 N SER A 392 1555 1555 1.32
CISPEP 1 GLY A 82 PRO A 83 0 -1.84
CISPEP 2 ARG A 120 PRO A 121 0 -4.79
CRYST1 104.891 104.891 127.802 90.00 90.00 120.00 P 31 2 1 6
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 0.009534 0.005504 0.000000 0.00000
SCALE2 0.000000 0.011009 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007825 0.00000
TER 3559 CYS A 492
MASTER 249 0 11 21 10 0 0 6 4052 1 98 37
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