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HEADER LYASE 30-MAR-24 9EVI
TITLE CRYSTAL STRUCTURE OF CANDIDA ANTARCTICA LIPASE B WITH THE PUTATIVE
TITLE 2 PRO-PEPTIDE REGION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE B;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: CALB;
COMPND 5 EC: 3.1.1.3;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MOESZIOMYCES ANTARCTICUS;
SOURCE 3 ORGANISM_TAXID: 84753;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI B;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 37762
KEYWDS LIPASE B, PUTATIVE PRO-PEPTIDE REGION, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.A.SOHAIL,L.W.RUDDOCK
REVDAT 1 09-APR-25 9EVI 0
JRNL AUTH A.A.SOHAIL,R.RECACHA,L.W.RUDDOCK
JRNL TITL CRYSTAL STRUCTURE OF CANDIDA ANTARCTICA LIPASE B WITH THE
JRNL TITL 2 PUTATIVE PRO-PEPTIDE REGION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.45 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.17.1_3660)
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) : 1.45
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.85
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.380
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 97613
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.138
REMARK 3 R VALUE (WORKING SET) : 0.136
REMARK 3 FREE R VALUE : 0.168
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4876
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 46.8500 - 4.5100 1.00 3185 155 0.1432 0.1369
REMARK 3 2 4.5000 - 3.5800 1.00 3127 167 0.1228 0.1405
REMARK 3 3 3.5800 - 3.1200 1.00 3065 181 0.1377 0.1573
REMARK 3 4 3.1200 - 2.8400 1.00 3157 147 0.1463 0.1884
REMARK 3 5 2.8400 - 2.6300 1.00 3098 158 0.1337 0.1482
REMARK 3 6 2.6300 - 2.4800 1.00 3069 190 0.1293 0.1622
REMARK 3 7 2.4800 - 2.3600 1.00 3138 145 0.1233 0.1607
REMARK 3 8 2.3600 - 2.2500 1.00 3087 143 0.1240 0.1456
REMARK 3 9 2.2500 - 2.1700 1.00 3099 177 0.1272 0.1753
REMARK 3 10 2.1700 - 2.0900 1.00 3100 166 0.1269 0.1735
REMARK 3 11 2.0900 - 2.0300 1.00 3079 168 0.1288 0.1766
REMARK 3 12 2.0300 - 1.9700 1.00 3093 154 0.1314 0.1584
REMARK 3 13 1.9700 - 1.9200 1.00 3075 163 0.1318 0.1765
REMARK 3 14 1.9200 - 1.8700 1.00 3111 162 0.1335 0.1858
REMARK 3 15 1.8700 - 1.8300 1.00 3074 160 0.1388 0.1968
REMARK 3 16 1.8300 - 1.7900 1.00 3105 167 0.1370 0.2090
REMARK 3 17 1.7900 - 1.7500 1.00 3046 178 0.1384 0.1970
REMARK 3 18 1.7500 - 1.7200 1.00 3081 163 0.1424 0.2082
REMARK 3 19 1.7200 - 1.6900 1.00 3061 151 0.1314 0.2019
REMARK 3 20 1.6900 - 1.6600 1.00 3117 167 0.1308 0.1778
REMARK 3 21 1.6600 - 1.6300 1.00 3036 177 0.1310 0.1839
REMARK 3 22 1.6300 - 1.6100 1.00 3100 167 0.1292 0.1772
REMARK 3 23 1.6100 - 1.5800 1.00 3041 163 0.1360 0.1795
REMARK 3 24 1.5800 - 1.5600 1.00 3096 167 0.1478 0.2407
REMARK 3 25 1.5600 - 1.5400 1.00 3097 146 0.1539 0.1994
REMARK 3 26 1.5400 - 1.5200 1.00 3087 161 0.1638 0.2142
REMARK 3 27 1.5200 - 1.5000 1.00 3098 159 0.1683 0.2253
REMARK 3 28 1.5000 - 1.4800 1.00 3017 167 0.1832 0.2317
REMARK 3 29 1.4800 - 1.4700 1.00 3092 160 0.2151 0.2732
REMARK 3 30 1.4700 - 1.4500 0.99 3106 147 0.2304 0.2746
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) : 0.130
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.430
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 : 0.005 4920
REMARK 3 ANGLE : 0.812 6759
REMARK 3 CHIRALITY : 0.064 789
REMARK 3 PLANARITY : 0.005 889
REMARK 3 DIHEDRAL : 9.160 703
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 9EVI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 30-MAR-24.
REMARK 100 THE DEPOSITION ID IS D_1292136991.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-JAN-20
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 XE 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 129759
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.190
REMARK 200 RESOLUTION RANGE LOW (A) : 54.370
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 73.5
REMARK 200 DATA REDUNDANCY : 4.400
REMARK 200 R MERGE (I) : 0.04700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.19
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.21
REMARK 200 COMPLETENESS FOR SHELL (%) : 3.0
REMARK 200 DATA REDUNDANCY IN SHELL : 1.00
REMARK 200 R MERGE FOR SHELL (I) : 0.64200
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: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.75
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M POTASSIUM SODIUM TARTRATE
REMARK 280 TETRAHYDRATE; 0.1 M BIS-TRIS PROPANE, PH 7.5; 25 % W/V PEG 3350,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 295.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 40.49250
REMARK 290 SMTRY3 2 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2480 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23540 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 KCAL/MOL
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 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 ALA B 19
REMARK 465 THR B 20
REMARK 465 PRO B 21
REMARK 465 LEU B 22
REMARK 465 VAL B 23
REMARK 465 LYS B 24
REMARK 465 ARG B 25
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 54 88.76 -159.29
REMARK 500 ASN A 76 -93.94 -149.24
REMARK 500 ASP A 100 118.30 -34.91
REMARK 500 ASP A 100 118.30 -31.03
REMARK 500 SER A 130 -129.43 58.34
REMARK 500 ASP A 159 67.44 -113.96
REMARK 500 ALA A 166 70.55 51.00
REMARK 500 ALA A 171 -129.78 64.09
REMARK 500 ASN A 231 -3.74 71.99
REMARK 500 ALA A 330 31.21 -146.49
REMARK 500 ASN B 76 -92.10 -147.04
REMARK 500 ASP B 100 116.99 -26.61
REMARK 500 SER B 130 -127.60 56.62
REMARK 500 ASP B 159 67.07 -114.93
REMARK 500 ASN B 231 -3.16 70.34
REMARK 500 ALA B 330 35.33 -143.25
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 920 DISTANCE = 6.08 ANGSTROMS
REMARK 525 HOH A 921 DISTANCE = 6.26 ANGSTROMS
REMARK 525 HOH A 922 DISTANCE = 6.50 ANGSTROMS
REMARK 525 HOH A 923 DISTANCE = 7.22 ANGSTROMS
REMARK 525 HOH A 924 DISTANCE = 8.72 ANGSTROMS
REMARK 525 HOH B 919 DISTANCE = 5.81 ANGSTROMS
REMARK 525 HOH B 920 DISTANCE = 6.48 ANGSTROMS
REMARK 525 HOH B 921 DISTANCE = 7.07 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 402 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PRO A 168 O
REMARK 620 2 ASP A 170 O 98.7
REMARK 620 3 LEU A 172 O 85.1 79.6
REMARK 620 4 VAL A 174 O 85.8 150.7 71.9
REMARK 620 5 SER A 175 OG 51.6 140.2 117.3 63.1
REMARK 620 6 HOH A 772 O 91.2 78.1 156.5 131.0 77.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 404 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ILE B 310 O
REMARK 620 2 PRO B 314 O 129.5
REMARK 620 3 HOH B 671 O 119.0 103.0
REMARK 620 N 1 2
DBREF 9EVI A 19 342 UNP P41365 LIPB_PSEA2 19 342
DBREF 9EVI B 19 342 UNP P41365 LIPB_PSEA2 19 342
SEQRES 1 A 324 ALA THR PRO LEU VAL LYS ARG LEU PRO SER GLY SER ASP
SEQRES 2 A 324 PRO ALA PHE SER GLN PRO LYS SER VAL LEU ASP ALA GLY
SEQRES 3 A 324 LEU THR CYS GLN GLY ALA SER PRO SER SER VAL SER LYS
SEQRES 4 A 324 PRO ILE LEU LEU VAL PRO GLY THR GLY THR THR GLY PRO
SEQRES 5 A 324 GLN SER PHE ASP SER ASN TRP ILE PRO LEU SER THR GLN
SEQRES 6 A 324 LEU GLY TYR THR PRO CYS TRP ILE SER PRO PRO PRO PHE
SEQRES 7 A 324 MET LEU ASN ASP THR GLN VAL ASN THR GLU TYR MET VAL
SEQRES 8 A 324 ASN ALA ILE THR ALA LEU TYR ALA GLY SER GLY ASN ASN
SEQRES 9 A 324 LYS LEU PRO VAL LEU THR TRP SER GLN GLY GLY LEU VAL
SEQRES 10 A 324 ALA GLN TRP GLY LEU THR PHE PHE PRO SER ILE ARG SER
SEQRES 11 A 324 LYS VAL ASP ARG LEU MET ALA PHE ALA PRO ASP TYR LYS
SEQRES 12 A 324 GLY THR VAL LEU ALA GLY PRO LEU ASP ALA LEU ALA VAL
SEQRES 13 A 324 SER ALA PRO SER VAL TRP GLN GLN THR THR GLY SER ALA
SEQRES 14 A 324 LEU THR THR ALA LEU ARG ASN ALA GLY GLY LEU THR GLN
SEQRES 15 A 324 ILE VAL PRO THR THR ASN LEU TYR SER ALA THR ASP GLU
SEQRES 16 A 324 ILE VAL GLN PRO GLN VAL SER ASN SER PRO LEU ASP SER
SEQRES 17 A 324 SER TYR LEU PHE ASN GLY LYS ASN VAL GLN ALA GLN ALA
SEQRES 18 A 324 VAL CYS GLY PRO LEU PHE VAL ILE ASP HIS ALA GLY SER
SEQRES 19 A 324 LEU THR SER GLN PHE SER TYR VAL VAL GLY ARG SER ALA
SEQRES 20 A 324 LEU ARG SER THR THR GLY GLN ALA ARG SER ALA ASP TYR
SEQRES 21 A 324 GLY ILE THR ASP CYS ASN PRO LEU PRO ALA ASN ASP LEU
SEQRES 22 A 324 THR PRO GLU GLN LYS VAL ALA ALA ALA ALA LEU LEU ALA
SEQRES 23 A 324 PRO ALA ALA ALA ALA ILE VAL ALA GLY PRO LYS GLN ASN
SEQRES 24 A 324 CYS GLU PRO ASP LEU MET PRO TYR ALA ARG PRO PHE ALA
SEQRES 25 A 324 VAL GLY LYS ARG THR CYS SER GLY ILE VAL THR PRO
SEQRES 1 B 324 ALA THR PRO LEU VAL LYS ARG LEU PRO SER GLY SER ASP
SEQRES 2 B 324 PRO ALA PHE SER GLN PRO LYS SER VAL LEU ASP ALA GLY
SEQRES 3 B 324 LEU THR CYS GLN GLY ALA SER PRO SER SER VAL SER LYS
SEQRES 4 B 324 PRO ILE LEU LEU VAL PRO GLY THR GLY THR THR GLY PRO
SEQRES 5 B 324 GLN SER PHE ASP SER ASN TRP ILE PRO LEU SER THR GLN
SEQRES 6 B 324 LEU GLY TYR THR PRO CYS TRP ILE SER PRO PRO PRO PHE
SEQRES 7 B 324 MET LEU ASN ASP THR GLN VAL ASN THR GLU TYR MET VAL
SEQRES 8 B 324 ASN ALA ILE THR ALA LEU TYR ALA GLY SER GLY ASN ASN
SEQRES 9 B 324 LYS LEU PRO VAL LEU THR TRP SER GLN GLY GLY LEU VAL
SEQRES 10 B 324 ALA GLN TRP GLY LEU THR PHE PHE PRO SER ILE ARG SER
SEQRES 11 B 324 LYS VAL ASP ARG LEU MET ALA PHE ALA PRO ASP TYR LYS
SEQRES 12 B 324 GLY THR VAL LEU ALA GLY PRO LEU ASP ALA LEU ALA VAL
SEQRES 13 B 324 SER ALA PRO SER VAL TRP GLN GLN THR THR GLY SER ALA
SEQRES 14 B 324 LEU THR THR ALA LEU ARG ASN ALA GLY GLY LEU THR GLN
SEQRES 15 B 324 ILE VAL PRO THR THR ASN LEU TYR SER ALA THR ASP GLU
SEQRES 16 B 324 ILE VAL GLN PRO GLN VAL SER ASN SER PRO LEU ASP SER
SEQRES 17 B 324 SER TYR LEU PHE ASN GLY LYS ASN VAL GLN ALA GLN ALA
SEQRES 18 B 324 VAL CYS GLY PRO LEU PHE VAL ILE ASP HIS ALA GLY SER
SEQRES 19 B 324 LEU THR SER GLN PHE SER TYR VAL VAL GLY ARG SER ALA
SEQRES 20 B 324 LEU ARG SER THR THR GLY GLN ALA ARG SER ALA ASP TYR
SEQRES 21 B 324 GLY ILE THR ASP CYS ASN PRO LEU PRO ALA ASN ASP LEU
SEQRES 22 B 324 THR PRO GLU GLN LYS VAL ALA ALA ALA ALA LEU LEU ALA
SEQRES 23 B 324 PRO ALA ALA ALA ALA ILE VAL ALA GLY PRO LYS GLN ASN
SEQRES 24 B 324 CYS GLU PRO ASP LEU MET PRO TYR ALA ARG PRO PHE ALA
SEQRES 25 B 324 VAL GLY LYS ARG THR CYS SER GLY ILE VAL THR PRO
HET TLA A 401 14
HET NA A 402 1
HET PEG B 401 17
HET PG4 B 402 31
HET TLA B 403 14
HET NA B 404 1
HETNAM TLA L(+)-TARTARIC ACID
HETNAM NA SODIUM ION
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM PG4 TETRAETHYLENE GLYCOL
FORMUL 3 TLA 2(C4 H6 O6)
FORMUL 4 NA 2(NA 1+)
FORMUL 5 PEG C4 H10 O3
FORMUL 6 PG4 C8 H18 O5
FORMUL 9 HOH *845(H2 O)
HELIX 1 AA1 PRO A 37 GLY A 44 1 8
HELIX 2 AA2 THR A 68 ASP A 74 1 7
HELIX 3 AA3 ASN A 76 GLN A 83 1 8
HELIX 4 AA4 ASP A 100 SER A 119 1 20
HELIX 5 AA5 SER A 130 PHE A 143 1 14
HELIX 6 AA6 PRO A 144 SER A 148 5 5
HELIX 7 AA7 ALA A 176 GLN A 182 1 7
HELIX 8 AA8 SER A 186 ALA A 195 1 10
HELIX 9 AA9 ALA A 237 GLY A 242 1 6
HELIX 10 AB1 ALA A 250 SER A 255 1 6
HELIX 11 AB2 SER A 255 SER A 268 1 14
HELIX 12 AB3 ARG A 274 TYR A 278 5 5
HELIX 13 AB4 GLY A 279 CYS A 283 5 5
HELIX 14 AB5 THR A 292 ALA A 301 1 10
HELIX 15 AB6 LEU A 303 GLY A 313 1 11
HELIX 16 AB7 ALA A 326 ALA A 330 5 5
HELIX 17 AB8 PRO B 37 GLY B 44 1 8
HELIX 18 AB9 THR B 68 ASP B 74 1 7
HELIX 19 AC1 ASN B 76 LEU B 84 1 9
HELIX 20 AC2 ASP B 100 SER B 119 1 20
HELIX 21 AC3 SER B 130 PHE B 143 1 14
HELIX 22 AC4 PRO B 144 ARG B 147 5 4
HELIX 23 AC5 THR B 163 GLY B 167 5 5
HELIX 24 AC6 PRO B 168 LEU B 172 5 5
HELIX 25 AC7 ALA B 176 GLN B 182 1 7
HELIX 26 AC8 SER B 186 ALA B 195 1 10
HELIX 27 AC9 ALA B 237 GLY B 242 1 6
HELIX 28 AD1 ALA B 250 SER B 255 1 6
HELIX 29 AD2 SER B 255 SER B 268 1 14
HELIX 30 AD3 ARG B 274 TYR B 278 5 5
HELIX 31 AD4 GLY B 279 CYS B 283 5 5
HELIX 32 AD5 THR B 292 ALA B 301 1 10
HELIX 33 AD6 LEU B 303 GLY B 313 1 11
HELIX 34 AD7 ALA B 326 ALA B 330 5 5
SHEET 1 AA1 7 LEU A 45 CYS A 47 0
SHEET 2 AA1 7 THR A 87 ILE A 91 -1 O TRP A 90 N THR A 46
SHEET 3 AA1 7 PRO A 58 VAL A 62 1 N LEU A 61 O CYS A 89
SHEET 4 AA1 7 LEU A 124 TRP A 129 1 O LEU A 127 N LEU A 60
SHEET 5 AA1 7 VAL A 150 PHE A 156 1 O MET A 154 N VAL A 126
SHEET 6 AA1 7 THR A 204 TYR A 208 1 O THR A 205 N ALA A 155
SHEET 7 AA1 7 LYS A 233 GLN A 236 1 O VAL A 235 N ASN A 206
SHEET 1 AA2 2 ARG A 334 THR A 335 0
SHEET 2 AA2 2 GLY A 338 ILE A 339 -1 O GLY A 338 N THR A 335
SHEET 1 AA3 7 LEU B 45 CYS B 47 0
SHEET 2 AA3 7 THR B 87 ILE B 91 -1 O TRP B 90 N THR B 46
SHEET 3 AA3 7 PRO B 58 VAL B 62 1 N LEU B 61 O CYS B 89
SHEET 4 AA3 7 LEU B 124 TRP B 129 1 O LEU B 127 N LEU B 60
SHEET 5 AA3 7 VAL B 150 PHE B 156 1 O MET B 154 N VAL B 126
SHEET 6 AA3 7 THR B 204 TYR B 208 1 O THR B 205 N ALA B 155
SHEET 7 AA3 7 LYS B 233 GLN B 236 1 O VAL B 235 N ASN B 206
SHEET 1 AA4 2 ARG B 334 THR B 335 0
SHEET 2 AA4 2 GLY B 338 ILE B 339 -1 O GLY B 338 N THR B 335
SSBOND 1 CYS A 47 CYS A 89 1555 1555 2.06
SSBOND 2 CYS A 241 CYS A 283 1555 1555 2.04
SSBOND 3 CYS A 318 CYS A 336 1555 1555 2.03
SSBOND 4 CYS B 47 CYS B 89 1555 1555 2.05
SSBOND 5 CYS B 241 CYS B 283 1555 1555 2.05
SSBOND 6 CYS B 318 CYS B 336 1555 1555 2.04
LINK O PRO A 168 NA NA A 402 1555 1555 2.88
LINK O ASP A 170 NA NA A 402 1555 1555 2.71
LINK O LEU A 172 NA NA A 402 1555 1555 2.41
LINK O VAL A 174 NA NA A 402 1555 1555 3.01
LINK OG SER A 175 NA NA A 402 1555 1555 2.94
LINK NA NA A 402 O HOH A 772 1555 1555 2.55
LINK O ILE B 310 NA NA B 404 1555 1555 2.79
LINK O PRO B 314 NA NA B 404 1555 1555 2.83
LINK NA NA B 404 O HOH B 671 1555 1555 2.92
CISPEP 1 PRO A 94 PRO A 95 0 -10.86
CISPEP 2 GLN A 216 PRO A 217 0 4.70
CISPEP 3 PRO B 94 PRO B 95 0 -11.22
CISPEP 4 GLN B 216 PRO B 217 0 1.84
CRYST1 47.344 80.985 73.993 90.00 98.30 90.00 P 1 21 1 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 0.021122 0.000000 0.003081 0.00000
SCALE2 0.000000 0.012348 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013658 0.00000
TER 4802 PRO A 342
TER 9480 PRO B 342
MASTER 304 0 6 34 18 0 0 6 5587 2 100 50
END |