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HEADER HYDROLASE 18-NOV-18 6ISP
TITLE STRUCTURE OF CANDIDA ANTARCTICA LIPASE B MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE B;
COMPND 3 CHAIN: D, A, C, B;
COMPND 4 SYNONYM: CALB;
COMPND 5 EC: 3.1.1.3;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOZYMA ANTARCTICA;
SOURCE 3 ORGANISM_COMMON: YEAST;
SOURCE 4 ORGANISM_TAXID: 84753;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS CALB, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.X.CEN,J.H.ZHOU,Q.WU
REVDAT 1 24-JUL-19 6ISP 0
JRNL AUTH M.T.REETZ,J.H.ZHOU,T.S.MOODY,M.L.HUANG,Q.WU,Y.X.CEN,W.SINGH,
JRNL AUTH 2 M.ARKIN
JRNL TITL ARTIFICIAL CYSTEINE-LIPASES WITH HIGH ACTIVITY AND ALTERED
JRNL TITL 2 CATALYTIC MECHANISM CREATED BY LABORATORY EVOLUTION.
JRNL REF NAT COMMUN 2019
JRNL REFN ESSN 2041-1723
JRNL DOI 10.1038/S41467-019-11155-3
REMARK 2
REMARK 2 RESOLUTION. 1.88 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10.1_2155: ???)
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) : 1.88
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.27
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 3 NUMBER OF REFLECTIONS : 106351
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.215
REMARK 3 R VALUE (WORKING SET) : 0.214
REMARK 3 FREE R VALUE : 0.238
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.160
REMARK 3 FREE R VALUE TEST SET COUNT : 5490
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 25.0213 - 5.0898 0.93 5054 252 0.1994 0.2273
REMARK 3 2 5.0898 - 4.0454 0.94 5146 261 0.1664 0.2125
REMARK 3 3 4.0454 - 3.5357 0.94 5060 283 0.1808 0.2010
REMARK 3 4 3.5357 - 3.2131 0.94 5125 273 0.1875 0.2117
REMARK 3 5 3.2131 - 2.9832 0.90 4831 275 0.2066 0.2371
REMARK 3 6 2.9832 - 2.8076 0.93 5001 297 0.2178 0.2393
REMARK 3 7 2.8076 - 2.6671 0.94 5076 287 0.2182 0.2295
REMARK 3 8 2.6671 - 2.5512 0.94 5070 260 0.2315 0.2539
REMARK 3 9 2.5512 - 2.4530 0.95 5078 252 0.2261 0.2230
REMARK 3 10 2.4530 - 2.3685 0.94 5039 284 0.2286 0.2902
REMARK 3 11 2.3685 - 2.2945 0.94 5106 290 0.2318 0.2334
REMARK 3 12 2.2945 - 2.2289 0.94 5025 280 0.2358 0.2834
REMARK 3 13 2.2289 - 2.1703 0.95 5115 275 0.2387 0.2539
REMARK 3 14 2.1703 - 2.1173 0.91 4898 266 0.2408 0.2836
REMARK 3 15 2.1173 - 2.0692 0.93 5012 255 0.2516 0.2698
REMARK 3 16 2.0692 - 2.0252 0.94 5061 264 0.2582 0.2824
REMARK 3 17 2.0252 - 1.9847 0.94 5050 274 0.2683 0.3156
REMARK 3 18 1.9847 - 1.9473 0.94 5033 274 0.2691 0.2442
REMARK 3 19 1.9473 - 1.9125 0.95 5083 261 0.2843 0.3187
REMARK 3 20 1.9125 - 1.8801 0.94 4984 280 0.3006 0.2743
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) : NULL
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.900
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 : 0.003 9979
REMARK 3 ANGLE : 0.924 13774
REMARK 3 CHIRALITY : 0.050 1654
REMARK 3 PLANARITY : 0.006 1741
REMARK 3 DIHEDRAL : 12.843 6067
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): -8.0068 1.7143 22.8803
REMARK 3 T TENSOR
REMARK 3 T11: 0.1193 T22: 0.1831
REMARK 3 T33: 0.2485 T12: -0.0080
REMARK 3 T13: 0.0099 T23: -0.0211
REMARK 3 L TENSOR
REMARK 3 L11: 0.1488 L22: 0.0837
REMARK 3 L33: 0.3296 L12: -0.0341
REMARK 3 L13: 0.1270 L23: -0.0936
REMARK 3 S TENSOR
REMARK 3 S11: 0.0055 S12: 0.0297 S13: -0.0255
REMARK 3 S21: -0.0043 S22: 0.0109 S23: -0.0073
REMARK 3 S31: 0.0095 S32: -0.0238 S33: -0.0158
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 6ISP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 03-DEC-18.
REMARK 100 THE DEPOSITION ID IS D_1300009454.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-DEC-17
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 : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97918
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 106440
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.880
REMARK 200 RESOLUTION RANGE LOW (A) : 46.265
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 200 DATA REDUNDANCY : 6.600
REMARK 200 R MERGE (I) : 0.13200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.88
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.91
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.2
REMARK 200 DATA REDUNDANCY IN SHELL : 6.60
REMARK 200 R MERGE FOR SHELL (I) : 0.99300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.100
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: 1TCA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.91
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CALCIUM ACETATE 0.2 M HEPES 0.1 M PH
REMARK 280 7.5 PEG8000 12% DEOXY-BIGCHAP 1.4 MM, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 289K
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 77.98500
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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 TOTAL BURIED SURFACE AREA: 400 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12520 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -3.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 700 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12590 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -4.0 KCAL/MOL
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 90 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13350 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -3.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12390 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 GLY D -3
REMARK 465 ALA D -2
REMARK 465 MET D -1
REMARK 465 PRO D 317
REMARK 465 GLY A -3
REMARK 465 ALA A -2
REMARK 465 THR A 316
REMARK 465 PRO A 317
REMARK 465 GLY C -3
REMARK 465 ALA C -2
REMARK 465 GLY B -3
REMARK 465 ALA B -2
REMARK 465 MET B -1
REMARK 465 PRO B 317
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH D 716 O HOH D 733 2.15
REMARK 500 O HOH C 575 O HOH C 768 2.16
REMARK 500 O HOH B 699 O HOH B 707 2.17
REMARK 500 O HOH A 501 O HOH A 720 2.18
REMARK 500 O HOH D 782 O HOH D 784 2.18
REMARK 500 O HOH D 501 O HOH D 718 2.18
REMARK 500 O HOH B 776 O HOH B 783 2.19
REMARK 500 O HOH B 683 O HOH B 710 2.19
REMARK 500 O HOH C 501 O HOH C 617 2.19
REMARK 500 O HOH C 532 O HOH C 615 2.19
REMARK 500 O HOH D 580 O HOH D 728 2.19
REMARK 500 O HOH A 635 O HOH A 718 2.19
REMARK 500 O HOH C 667 O HOH C 748 2.19
REMARK 500 O HOH D 727 O HOH D 754 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LEU D 144 CB - CG - CD1 ANGL. DEV. = -18.8 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
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 D 29 83.11 -152.24
REMARK 500 ASN D 51 -87.86 -135.55
REMARK 500 SER D 105 -124.25 59.14
REMARK 500 ASP D 134 69.82 -117.34
REMARK 500 PRO D 143 86.60 -63.53
REMARK 500 ASP D 145 60.27 -110.79
REMARK 500 PRO D 198 -9.14 -57.45
REMARK 500 ASN D 206 -1.78 71.13
REMARK 500 ALA D 276 31.02 -96.37
REMARK 500 ALA D 305 45.45 -143.10
REMARK 500 THR D 310 -165.12 -118.95
REMARK 500 SER A 29 81.17 -150.71
REMARK 500 ASN A 51 -87.61 -135.31
REMARK 500 SER A 105 -123.56 58.03
REMARK 500 ASP A 134 70.73 -117.37
REMARK 500 LEU A 144 31.12 -142.50
REMARK 500 ASN A 206 -2.31 71.72
REMARK 500 ALA A 276 31.81 -96.91
REMARK 500 ALA A 305 45.52 -142.80
REMARK 500 THR A 310 -165.92 -118.59
REMARK 500 SER C 29 82.04 -151.69
REMARK 500 ASN C 51 -87.59 -135.24
REMARK 500 SER C 105 -123.58 58.49
REMARK 500 ASP C 134 70.45 -118.00
REMARK 500 ALA C 146 45.65 -93.32
REMARK 500 LEU C 147 -18.34 -140.76
REMARK 500 PRO C 198 -9.75 -56.86
REMARK 500 ASN C 206 -2.00 70.96
REMARK 500 ALA C 276 31.59 -96.15
REMARK 500 ALA C 305 45.09 -141.94
REMARK 500 THR C 310 -165.51 -119.01
REMARK 500 VAL C 315 97.51 -46.69
REMARK 500 SER B 29 81.96 -151.69
REMARK 500 ASN B 51 -87.43 -134.99
REMARK 500 SER B 105 -123.49 58.02
REMARK 500 ASP B 134 70.51 -117.96
REMARK 500 PRO B 198 -9.78 -57.66
REMARK 500 ASN B 206 -2.25 70.67
REMARK 500 ALA B 276 31.99 -97.41
REMARK 500 ALA B 305 44.64 -142.05
REMARK 500 THR B 310 -164.59 -119.65
REMARK 500 VAL B 315 108.13 -46.93
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 D 780 DISTANCE = 5.93 ANGSTROMS
REMARK 525 HOH D 781 DISTANCE = 6.01 ANGSTROMS
REMARK 525 HOH D 782 DISTANCE = 6.25 ANGSTROMS
REMARK 525 HOH D 783 DISTANCE = 6.41 ANGSTROMS
REMARK 525 HOH D 784 DISTANCE = 6.46 ANGSTROMS
REMARK 525 HOH D 785 DISTANCE = 6.60 ANGSTROMS
REMARK 525 HOH D 786 DISTANCE = 7.29 ANGSTROMS
REMARK 525 HOH A 806 DISTANCE = 5.83 ANGSTROMS
REMARK 525 HOH A 807 DISTANCE = 5.90 ANGSTROMS
REMARK 525 HOH A 808 DISTANCE = 5.99 ANGSTROMS
REMARK 525 HOH A 809 DISTANCE = 6.04 ANGSTROMS
REMARK 525 HOH A 810 DISTANCE = 6.28 ANGSTROMS
REMARK 525 HOH A 811 DISTANCE = 6.37 ANGSTROMS
REMARK 525 HOH A 812 DISTANCE = 6.45 ANGSTROMS
REMARK 525 HOH C 812 DISTANCE = 6.06 ANGSTROMS
REMARK 525 HOH C 813 DISTANCE = 6.07 ANGSTROMS
REMARK 525 HOH C 814 DISTANCE = 6.15 ANGSTROMS
REMARK 525 HOH C 815 DISTANCE = 6.29 ANGSTROMS
REMARK 525 HOH C 816 DISTANCE = 6.89 ANGSTROMS
REMARK 525 HOH C 817 DISTANCE = 7.02 ANGSTROMS
REMARK 525 HOH C 818 DISTANCE = 7.22 ANGSTROMS
REMARK 525 HOH C 819 DISTANCE = 9.29 ANGSTROMS
REMARK 525 HOH B 802 DISTANCE = 5.85 ANGSTROMS
REMARK 525 HOH B 803 DISTANCE = 6.01 ANGSTROMS
REMARK 525 HOH B 804 DISTANCE = 6.03 ANGSTROMS
REMARK 525 HOH B 805 DISTANCE = 6.17 ANGSTROMS
REMARK 525 HOH B 806 DISTANCE = 6.44 ANGSTROMS
REMARK 525 HOH B 807 DISTANCE = 6.55 ANGSTROMS
REMARK 525 HOH B 808 DISTANCE = 6.61 ANGSTROMS
REMARK 525 HOH B 809 DISTANCE = 6.82 ANGSTROMS
REMARK 525 HOH B 810 DISTANCE = 6.86 ANGSTROMS
REMARK 525 HOH B 811 DISTANCE = 6.99 ANGSTROMS
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 CPQ D 401
REMARK 610 CPQ D 402
REMARK 610 CPQ A 403
REMARK 610 CPQ A 404
REMARK 610 CPQ A 405
REMARK 610 CPQ C 401
REMARK 610 CPQ C 402
REMARK 610 CPQ C 403
REMARK 610 CPQ B 402
REMARK 610 CPQ B 403
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 CA A 401 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 223 OD2
REMARK 620 2 ASP A 223 OD2 162.0
REMARK 620 3 HOH D 698 O 91.8 103.4
REMARK 620 4 HOH A 668 O 96.2 74.9 88.6
REMARK 620 5 HOH D 691 O 84.4 93.6 127.8 143.6
REMARK 620 6 HOH D 651 O 75.6 86.4 144.7 61.0 84.3
REMARK 620 7 HOH A 699 O 116.0 81.1 55.3 130.0 80.0 159.2
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 401 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 223 OD2
REMARK 620 2 ASP B 223 OD2 166.5
REMARK 620 3 HOH C 673 O 75.8 94.4
REMARK 620 4 HOH B 704 O 98.1 85.3 148.0
REMARK 620 5 HOH C 646 O 74.5 118.9 132.3 73.0
REMARK 620 6 HOH B 674 O 87.7 79.8 67.4 81.2 145.9
REMARK 620 7 HOH B 706 O 98.2 88.5 77.4 134.4 70.9 141.7
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CPQ D 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CPQ D 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CPQ A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CPQ A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CPQ A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CPQ A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CPQ C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CPQ C 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CPQ C 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CPQ B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CPQ B 403
DBREF 6ISP D 1 317 UNP P41365 LIPB_PSEA2 26 342
DBREF 6ISP A 1 317 UNP P41365 LIPB_PSEA2 26 342
DBREF 6ISP C 1 317 UNP P41365 LIPB_PSEA2 26 342
DBREF 6ISP B 1 317 UNP P41365 LIPB_PSEA2 26 342
SEQADV 6ISP GLY D -3 UNP P41365 EXPRESSION TAG
SEQADV 6ISP ALA D -2 UNP P41365 EXPRESSION TAG
SEQADV 6ISP MET D -1 UNP P41365 EXPRESSION TAG
SEQADV 6ISP ALA D 0 UNP P41365 EXPRESSION TAG
SEQADV 6ISP ALA D 57 UNP P41365 THR 82 ENGINEERED MUTATION
SEQADV 6ISP THR D 89 UNP P41365 ALA 114 ENGINEERED MUTATION
SEQADV 6ISP VAL D 104 UNP P41365 TRP 129 ENGINEERED MUTATION
SEQADV 6ISP GLY D 149 UNP P41365 VAL 174 ENGINEERED MUTATION
SEQADV 6ISP TYR D 281 UNP P41365 ALA 306 ENGINEERED MUTATION
SEQADV 6ISP TYR D 282 UNP P41365 ALA 307 ENGINEERED MUTATION
SEQADV 6ISP GLY A -3 UNP P41365 EXPRESSION TAG
SEQADV 6ISP ALA A -2 UNP P41365 EXPRESSION TAG
SEQADV 6ISP MET A -1 UNP P41365 EXPRESSION TAG
SEQADV 6ISP ALA A 0 UNP P41365 EXPRESSION TAG
SEQADV 6ISP ALA A 57 UNP P41365 THR 82 ENGINEERED MUTATION
SEQADV 6ISP THR A 89 UNP P41365 ALA 114 ENGINEERED MUTATION
SEQADV 6ISP VAL A 104 UNP P41365 TRP 129 ENGINEERED MUTATION
SEQADV 6ISP GLY A 149 UNP P41365 VAL 174 ENGINEERED MUTATION
SEQADV 6ISP TYR A 281 UNP P41365 ALA 306 ENGINEERED MUTATION
SEQADV 6ISP TYR A 282 UNP P41365 ALA 307 ENGINEERED MUTATION
SEQADV 6ISP GLY C -3 UNP P41365 EXPRESSION TAG
SEQADV 6ISP ALA C -2 UNP P41365 EXPRESSION TAG
SEQADV 6ISP MET C -1 UNP P41365 EXPRESSION TAG
SEQADV 6ISP ALA C 0 UNP P41365 EXPRESSION TAG
SEQADV 6ISP ALA C 57 UNP P41365 THR 82 ENGINEERED MUTATION
SEQADV 6ISP THR C 89 UNP P41365 ALA 114 ENGINEERED MUTATION
SEQADV 6ISP VAL C 104 UNP P41365 TRP 129 ENGINEERED MUTATION
SEQADV 6ISP GLY C 149 UNP P41365 VAL 174 ENGINEERED MUTATION
SEQADV 6ISP TYR C 281 UNP P41365 ALA 306 ENGINEERED MUTATION
SEQADV 6ISP TYR C 282 UNP P41365 ALA 307 ENGINEERED MUTATION
SEQADV 6ISP GLY B -3 UNP P41365 EXPRESSION TAG
SEQADV 6ISP ALA B -2 UNP P41365 EXPRESSION TAG
SEQADV 6ISP MET B -1 UNP P41365 EXPRESSION TAG
SEQADV 6ISP ALA B 0 UNP P41365 EXPRESSION TAG
SEQADV 6ISP ALA B 57 UNP P41365 THR 82 ENGINEERED MUTATION
SEQADV 6ISP THR B 89 UNP P41365 ALA 114 ENGINEERED MUTATION
SEQADV 6ISP VAL B 104 UNP P41365 TRP 129 ENGINEERED MUTATION
SEQADV 6ISP GLY B 149 UNP P41365 VAL 174 ENGINEERED MUTATION
SEQADV 6ISP TYR B 281 UNP P41365 ALA 306 ENGINEERED MUTATION
SEQADV 6ISP TYR B 282 UNP P41365 ALA 307 ENGINEERED MUTATION
SEQRES 1 D 321 GLY ALA MET ALA LEU PRO SER GLY SER ASP PRO ALA PHE
SEQRES 2 D 321 SER GLN PRO LYS SER VAL LEU ASP ALA GLY LEU THR CYS
SEQRES 3 D 321 GLN GLY ALA SER PRO SER SER VAL SER LYS PRO ILE LEU
SEQRES 4 D 321 LEU VAL PRO GLY THR GLY THR THR GLY PRO GLN SER PHE
SEQRES 5 D 321 ASP SER ASN TRP ILE PRO LEU SER ALA GLN LEU GLY TYR
SEQRES 6 D 321 THR PRO CYS TRP ILE SER PRO PRO PRO PHE MET LEU ASN
SEQRES 7 D 321 ASP THR GLN VAL ASN THR GLU TYR MET VAL ASN ALA ILE
SEQRES 8 D 321 THR THR LEU TYR ALA GLY SER GLY ASN ASN LYS LEU PRO
SEQRES 9 D 321 VAL LEU THR VAL SER GLN GLY GLY LEU VAL ALA GLN TRP
SEQRES 10 D 321 GLY LEU THR PHE PHE PRO SER ILE ARG SER LYS VAL ASP
SEQRES 11 D 321 ARG LEU MET ALA PHE ALA PRO ASP TYR LYS GLY THR VAL
SEQRES 12 D 321 LEU ALA GLY PRO LEU ASP ALA LEU ALA GLY SER ALA PRO
SEQRES 13 D 321 SER VAL TRP GLN GLN THR THR GLY SER ALA LEU THR THR
SEQRES 14 D 321 ALA LEU ARG ASN ALA GLY GLY LEU THR GLN ILE VAL PRO
SEQRES 15 D 321 THR THR ASN LEU TYR SER ALA THR ASP GLU ILE VAL GLN
SEQRES 16 D 321 PRO GLN VAL SER ASN SER PRO LEU ASP SER SER TYR LEU
SEQRES 17 D 321 PHE ASN GLY LYS ASN VAL GLN ALA GLN ALA VAL CYS GLY
SEQRES 18 D 321 PRO LEU PHE VAL ILE ASP HIS ALA GLY SER LEU THR SER
SEQRES 19 D 321 GLN PHE SER TYR VAL VAL GLY ARG SER ALA LEU ARG SER
SEQRES 20 D 321 THR THR GLY GLN ALA ARG SER ALA ASP TYR GLY ILE THR
SEQRES 21 D 321 ASP CYS ASN PRO LEU PRO ALA ASN ASP LEU THR PRO GLU
SEQRES 22 D 321 GLN LYS VAL ALA ALA ALA ALA LEU LEU ALA PRO TYR TYR
SEQRES 23 D 321 ALA ALA ILE VAL ALA GLY PRO LYS GLN ASN CYS GLU PRO
SEQRES 24 D 321 ASP LEU MET PRO TYR ALA ARG PRO PHE ALA VAL GLY LYS
SEQRES 25 D 321 ARG THR CYS SER GLY ILE VAL THR PRO
SEQRES 1 A 321 GLY ALA MET ALA LEU PRO SER GLY SER ASP PRO ALA PHE
SEQRES 2 A 321 SER GLN PRO LYS SER VAL LEU ASP ALA GLY LEU THR CYS
SEQRES 3 A 321 GLN GLY ALA SER PRO SER SER VAL SER LYS PRO ILE LEU
SEQRES 4 A 321 LEU VAL PRO GLY THR GLY THR THR GLY PRO GLN SER PHE
SEQRES 5 A 321 ASP SER ASN TRP ILE PRO LEU SER ALA GLN LEU GLY TYR
SEQRES 6 A 321 THR PRO CYS TRP ILE SER PRO PRO PRO PHE MET LEU ASN
SEQRES 7 A 321 ASP THR GLN VAL ASN THR GLU TYR MET VAL ASN ALA ILE
SEQRES 8 A 321 THR THR LEU TYR ALA GLY SER GLY ASN ASN LYS LEU PRO
SEQRES 9 A 321 VAL LEU THR VAL SER GLN GLY GLY LEU VAL ALA GLN TRP
SEQRES 10 A 321 GLY LEU THR PHE PHE PRO SER ILE ARG SER LYS VAL ASP
SEQRES 11 A 321 ARG LEU MET ALA PHE ALA PRO ASP TYR LYS GLY THR VAL
SEQRES 12 A 321 LEU ALA GLY PRO LEU ASP ALA LEU ALA GLY SER ALA PRO
SEQRES 13 A 321 SER VAL TRP GLN GLN THR THR GLY SER ALA LEU THR THR
SEQRES 14 A 321 ALA LEU ARG ASN ALA GLY GLY LEU THR GLN ILE VAL PRO
SEQRES 15 A 321 THR THR ASN LEU TYR SER ALA THR ASP GLU ILE VAL GLN
SEQRES 16 A 321 PRO GLN VAL SER ASN SER PRO LEU ASP SER SER TYR LEU
SEQRES 17 A 321 PHE ASN GLY LYS ASN VAL GLN ALA GLN ALA VAL CYS GLY
SEQRES 18 A 321 PRO LEU PHE VAL ILE ASP HIS ALA GLY SER LEU THR SER
SEQRES 19 A 321 GLN PHE SER TYR VAL VAL GLY ARG SER ALA LEU ARG SER
SEQRES 20 A 321 THR THR GLY GLN ALA ARG SER ALA ASP TYR GLY ILE THR
SEQRES 21 A 321 ASP CYS ASN PRO LEU PRO ALA ASN ASP LEU THR PRO GLU
SEQRES 22 A 321 GLN LYS VAL ALA ALA ALA ALA LEU LEU ALA PRO TYR TYR
SEQRES 23 A 321 ALA ALA ILE VAL ALA GLY PRO LYS GLN ASN CYS GLU PRO
SEQRES 24 A 321 ASP LEU MET PRO TYR ALA ARG PRO PHE ALA VAL GLY LYS
SEQRES 25 A 321 ARG THR CYS SER GLY ILE VAL THR PRO
SEQRES 1 C 321 GLY ALA MET ALA LEU PRO SER GLY SER ASP PRO ALA PHE
SEQRES 2 C 321 SER GLN PRO LYS SER VAL LEU ASP ALA GLY LEU THR CYS
SEQRES 3 C 321 GLN GLY ALA SER PRO SER SER VAL SER LYS PRO ILE LEU
SEQRES 4 C 321 LEU VAL PRO GLY THR GLY THR THR GLY PRO GLN SER PHE
SEQRES 5 C 321 ASP SER ASN TRP ILE PRO LEU SER ALA GLN LEU GLY TYR
SEQRES 6 C 321 THR PRO CYS TRP ILE SER PRO PRO PRO PHE MET LEU ASN
SEQRES 7 C 321 ASP THR GLN VAL ASN THR GLU TYR MET VAL ASN ALA ILE
SEQRES 8 C 321 THR THR LEU TYR ALA GLY SER GLY ASN ASN LYS LEU PRO
SEQRES 9 C 321 VAL LEU THR VAL SER GLN GLY GLY LEU VAL ALA GLN TRP
SEQRES 10 C 321 GLY LEU THR PHE PHE PRO SER ILE ARG SER LYS VAL ASP
SEQRES 11 C 321 ARG LEU MET ALA PHE ALA PRO ASP TYR LYS GLY THR VAL
SEQRES 12 C 321 LEU ALA GLY PRO LEU ASP ALA LEU ALA GLY SER ALA PRO
SEQRES 13 C 321 SER VAL TRP GLN GLN THR THR GLY SER ALA LEU THR THR
SEQRES 14 C 321 ALA LEU ARG ASN ALA GLY GLY LEU THR GLN ILE VAL PRO
SEQRES 15 C 321 THR THR ASN LEU TYR SER ALA THR ASP GLU ILE VAL GLN
SEQRES 16 C 321 PRO GLN VAL SER ASN SER PRO LEU ASP SER SER TYR LEU
SEQRES 17 C 321 PHE ASN GLY LYS ASN VAL GLN ALA GLN ALA VAL CYS GLY
SEQRES 18 C 321 PRO LEU PHE VAL ILE ASP HIS ALA GLY SER LEU THR SER
SEQRES 19 C 321 GLN PHE SER TYR VAL VAL GLY ARG SER ALA LEU ARG SER
SEQRES 20 C 321 THR THR GLY GLN ALA ARG SER ALA ASP TYR GLY ILE THR
SEQRES 21 C 321 ASP CYS ASN PRO LEU PRO ALA ASN ASP LEU THR PRO GLU
SEQRES 22 C 321 GLN LYS VAL ALA ALA ALA ALA LEU LEU ALA PRO TYR TYR
SEQRES 23 C 321 ALA ALA ILE VAL ALA GLY PRO LYS GLN ASN CYS GLU PRO
SEQRES 24 C 321 ASP LEU MET PRO TYR ALA ARG PRO PHE ALA VAL GLY LYS
SEQRES 25 C 321 ARG THR CYS SER GLY ILE VAL THR PRO
SEQRES 1 B 321 GLY ALA MET ALA LEU PRO SER GLY SER ASP PRO ALA PHE
SEQRES 2 B 321 SER GLN PRO LYS SER VAL LEU ASP ALA GLY LEU THR CYS
SEQRES 3 B 321 GLN GLY ALA SER PRO SER SER VAL SER LYS PRO ILE LEU
SEQRES 4 B 321 LEU VAL PRO GLY THR GLY THR THR GLY PRO GLN SER PHE
SEQRES 5 B 321 ASP SER ASN TRP ILE PRO LEU SER ALA GLN LEU GLY TYR
SEQRES 6 B 321 THR PRO CYS TRP ILE SER PRO PRO PRO PHE MET LEU ASN
SEQRES 7 B 321 ASP THR GLN VAL ASN THR GLU TYR MET VAL ASN ALA ILE
SEQRES 8 B 321 THR THR LEU TYR ALA GLY SER GLY ASN ASN LYS LEU PRO
SEQRES 9 B 321 VAL LEU THR VAL SER GLN GLY GLY LEU VAL ALA GLN TRP
SEQRES 10 B 321 GLY LEU THR PHE PHE PRO SER ILE ARG SER LYS VAL ASP
SEQRES 11 B 321 ARG LEU MET ALA PHE ALA PRO ASP TYR LYS GLY THR VAL
SEQRES 12 B 321 LEU ALA GLY PRO LEU ASP ALA LEU ALA GLY SER ALA PRO
SEQRES 13 B 321 SER VAL TRP GLN GLN THR THR GLY SER ALA LEU THR THR
SEQRES 14 B 321 ALA LEU ARG ASN ALA GLY GLY LEU THR GLN ILE VAL PRO
SEQRES 15 B 321 THR THR ASN LEU TYR SER ALA THR ASP GLU ILE VAL GLN
SEQRES 16 B 321 PRO GLN VAL SER ASN SER PRO LEU ASP SER SER TYR LEU
SEQRES 17 B 321 PHE ASN GLY LYS ASN VAL GLN ALA GLN ALA VAL CYS GLY
SEQRES 18 B 321 PRO LEU PHE VAL ILE ASP HIS ALA GLY SER LEU THR SER
SEQRES 19 B 321 GLN PHE SER TYR VAL VAL GLY ARG SER ALA LEU ARG SER
SEQRES 20 B 321 THR THR GLY GLN ALA ARG SER ALA ASP TYR GLY ILE THR
SEQRES 21 B 321 ASP CYS ASN PRO LEU PRO ALA ASN ASP LEU THR PRO GLU
SEQRES 22 B 321 GLN LYS VAL ALA ALA ALA ALA LEU LEU ALA PRO TYR TYR
SEQRES 23 B 321 ALA ALA ILE VAL ALA GLY PRO LYS GLN ASN CYS GLU PRO
SEQRES 24 B 321 ASP LEU MET PRO TYR ALA ARG PRO PHE ALA VAL GLY LYS
SEQRES 25 B 321 ARG THR CYS SER GLY ILE VAL THR PRO
HET CPQ D 401 45
HET CPQ D 402 22
HET CA A 401 1
HET CPQ A 402 60
HET CPQ A 403 28
HET CPQ A 404 35
HET CPQ A 405 27
HET CPQ C 401 22
HET CPQ C 402 30
HET CPQ C 403 28
HET CA B 401 1
HET CPQ B 402 45
HET CPQ B 403 22
HETNAM CPQ N,N-BIS(3-D-GLUCONAMIDOPROPYL)DEOXYCHOLAMIDE
HETNAM CA CALCIUM ION
HETSYN CPQ DEOXY-BIGCHAP
FORMUL 5 CPQ 11(C42 H75 N3 O15)
FORMUL 7 CA 2(CA 2+)
FORMUL 18 HOH *1228(H2 O)
HELIX 1 AA1 PRO D 12 GLY D 19 1 8
HELIX 2 AA2 THR D 43 ASP D 49 1 7
HELIX 3 AA3 ASN D 51 LEU D 59 1 9
HELIX 4 AA4 ASP D 75 SER D 94 1 20
HELIX 5 AA5 SER D 105 PHE D 118 1 14
HELIX 6 AA6 PRO D 119 SER D 123 5 5
HELIX 7 AA7 ALA D 151 GLN D 157 1 7
HELIX 8 AA8 SER D 161 ALA D 170 1 10
HELIX 9 AA9 ALA D 212 GLY D 217 1 6
HELIX 10 AB1 ALA D 225 SER D 230 1 6
HELIX 11 AB2 SER D 230 SER D 243 1 14
HELIX 12 AB3 ARG D 249 TYR D 253 5 5
HELIX 13 AB4 GLY D 254 CYS D 258 5 5
HELIX 14 AB5 THR D 267 ALA D 276 1 10
HELIX 15 AB6 LEU D 278 GLY D 288 1 11
HELIX 16 AB7 ALA D 301 ALA D 305 5 5
HELIX 17 AB8 PRO A 12 GLY A 19 1 8
HELIX 18 AB9 THR A 43 ASP A 49 1 7
HELIX 19 AC1 ASN A 51 LEU A 59 1 9
HELIX 20 AC2 ASP A 75 SER A 94 1 20
HELIX 21 AC3 SER A 105 PHE A 118 1 14
HELIX 22 AC4 PRO A 119 SER A 123 5 5
HELIX 23 AC5 ALA A 151 GLN A 157 1 7
HELIX 24 AC6 SER A 161 ALA A 170 1 10
HELIX 25 AC7 ALA A 212 GLY A 217 1 6
HELIX 26 AC8 ALA A 225 SER A 230 1 6
HELIX 27 AC9 SER A 230 SER A 243 1 14
HELIX 28 AD1 ARG A 249 TYR A 253 5 5
HELIX 29 AD2 GLY A 254 CYS A 258 5 5
HELIX 30 AD3 THR A 267 ALA A 276 1 10
HELIX 31 AD4 LEU A 278 GLY A 288 1 11
HELIX 32 AD5 ALA A 301 ALA A 305 5 5
HELIX 33 AD6 PRO C 12 GLY C 19 1 8
HELIX 34 AD7 THR C 43 ASP C 49 1 7
HELIX 35 AD8 ASN C 51 LEU C 59 1 9
HELIX 36 AD9 ASP C 75 SER C 94 1 20
HELIX 37 AE1 SER C 105 PHE C 118 1 14
HELIX 38 AE2 PRO C 119 SER C 123 5 5
HELIX 39 AE3 ALA C 151 GLN C 157 1 7
HELIX 40 AE4 SER C 161 ALA C 170 1 10
HELIX 41 AE5 ALA C 212 GLY C 217 1 6
HELIX 42 AE6 ALA C 225 SER C 230 1 6
HELIX 43 AE7 SER C 230 SER C 243 1 14
HELIX 44 AE8 ARG C 249 TYR C 253 5 5
HELIX 45 AE9 GLY C 254 CYS C 258 5 5
HELIX 46 AF1 THR C 267 ALA C 276 1 10
HELIX 47 AF2 LEU C 278 GLY C 288 1 11
HELIX 48 AF3 ALA C 301 ALA C 305 5 5
HELIX 49 AF4 PRO B 12 GLY B 19 1 8
HELIX 50 AF5 THR B 43 ASP B 49 1 7
HELIX 51 AF6 ASN B 51 LEU B 59 1 9
HELIX 52 AF7 ASP B 75 SER B 94 1 20
HELIX 53 AF8 SER B 105 PHE B 118 1 14
HELIX 54 AF9 PRO B 119 SER B 123 5 5
HELIX 55 AG1 ASP B 145 GLY B 149 5 5
HELIX 56 AG2 ALA B 151 GLN B 157 1 7
HELIX 57 AG3 SER B 161 ALA B 170 1 10
HELIX 58 AG4 ALA B 212 GLY B 217 1 6
HELIX 59 AG5 ALA B 225 SER B 230 1 6
HELIX 60 AG6 SER B 230 ARG B 242 1 13
HELIX 61 AG7 ARG B 249 TYR B 253 5 5
HELIX 62 AG8 GLY B 254 CYS B 258 5 5
HELIX 63 AG9 THR B 267 ALA B 276 1 10
HELIX 64 AH1 LEU B 278 GLY B 288 1 11
HELIX 65 AH2 ALA B 301 ALA B 305 5 5
SHEET 1 AA1 7 LEU D 20 CYS D 22 0
SHEET 2 AA1 7 THR D 62 ILE D 66 -1 O TRP D 65 N THR D 21
SHEET 3 AA1 7 PRO D 33 VAL D 37 1 N LEU D 36 O CYS D 64
SHEET 4 AA1 7 LEU D 99 VAL D 104 1 O LEU D 102 N LEU D 35
SHEET 5 AA1 7 VAL D 125 PHE D 131 1 O MET D 129 N VAL D 101
SHEET 6 AA1 7 THR D 179 TYR D 183 1 O THR D 180 N ALA D 130
SHEET 7 AA1 7 LYS D 208 GLN D 211 1 O VAL D 210 N ASN D 181
SHEET 1 AA2 2 ARG D 309 THR D 310 0
SHEET 2 AA2 2 GLY D 313 ILE D 314 -1 O GLY D 313 N THR D 310
SHEET 1 AA3 7 LEU A 20 CYS A 22 0
SHEET 2 AA3 7 THR A 62 ILE A 66 -1 O TRP A 65 N THR A 21
SHEET 3 AA3 7 PRO A 33 VAL A 37 1 N LEU A 36 O CYS A 64
SHEET 4 AA3 7 LEU A 99 VAL A 104 1 O LEU A 102 N LEU A 35
SHEET 5 AA3 7 VAL A 125 PHE A 131 1 O MET A 129 N VAL A 101
SHEET 6 AA3 7 THR A 179 TYR A 183 1 O THR A 180 N ALA A 130
SHEET 7 AA3 7 LYS A 208 GLN A 211 1 O VAL A 210 N ASN A 181
SHEET 1 AA4 2 ARG A 309 THR A 310 0
SHEET 2 AA4 2 GLY A 313 ILE A 314 -1 O GLY A 313 N THR A 310
SHEET 1 AA5 7 LEU C 20 CYS C 22 0
SHEET 2 AA5 7 THR C 62 ILE C 66 -1 O TRP C 65 N THR C 21
SHEET 3 AA5 7 PRO C 33 VAL C 37 1 N ILE C 34 O CYS C 64
SHEET 4 AA5 7 LEU C 99 VAL C 104 1 O LEU C 102 N LEU C 35
SHEET 5 AA5 7 VAL C 125 PHE C 131 1 O MET C 129 N VAL C 101
SHEET 6 AA5 7 THR C 179 TYR C 183 1 O THR C 180 N LEU C 128
SHEET 7 AA5 7 LYS C 208 GLN C 211 1 O VAL C 210 N ASN C 181
SHEET 1 AA6 2 ARG C 309 THR C 310 0
SHEET 2 AA6 2 GLY C 313 ILE C 314 -1 O GLY C 313 N THR C 310
SHEET 1 AA7 7 LEU B 20 CYS B 22 0
SHEET 2 AA7 7 THR B 62 ILE B 66 -1 O TRP B 65 N THR B 21
SHEET 3 AA7 7 PRO B 33 VAL B 37 1 N ILE B 34 O CYS B 64
SHEET 4 AA7 7 LEU B 99 VAL B 104 1 O LEU B 102 N LEU B 35
SHEET 5 AA7 7 VAL B 125 PHE B 131 1 O MET B 129 N VAL B 101
SHEET 6 AA7 7 THR B 179 TYR B 183 1 O THR B 180 N LEU B 128
SHEET 7 AA7 7 LYS B 208 GLN B 211 1 O VAL B 210 N ASN B 181
SHEET 1 AA8 2 ARG B 309 THR B 310 0
SHEET 2 AA8 2 GLY B 313 ILE B 314 -1 O GLY B 313 N THR B 310
SSBOND 1 CYS D 22 CYS D 64 1555 1555 2.03
SSBOND 2 CYS D 216 CYS D 258 1555 1555 2.03
SSBOND 3 CYS D 293 CYS D 311 1555 1555 2.03
SSBOND 4 CYS A 22 CYS A 64 1555 1555 2.03
SSBOND 5 CYS A 216 CYS A 258 1555 1555 2.03
SSBOND 6 CYS A 293 CYS A 311 1555 1555 2.03
SSBOND 7 CYS C 22 CYS C 64 1555 1555 2.03
SSBOND 8 CYS C 216 CYS C 258 1555 1555 2.03
SSBOND 9 CYS C 293 CYS C 311 1555 1555 2.04
SSBOND 10 CYS B 22 CYS B 64 1555 1555 2.03
SSBOND 11 CYS B 216 CYS B 258 1555 1555 2.03
SSBOND 12 CYS B 293 CYS B 311 1555 1555 2.03
LINK OD2 ASP D 223 CA CA A 401 1555 1555 2.37
LINK OD2 ASP A 223 CA CA A 401 1555 1555 2.44
LINK OD2 ASP C 223 CA CA B 401 1555 1555 2.39
LINK OD2 ASP B 223 CA CA B 401 1555 1555 2.38
LINK CA CA A 401 O HOH D 698 1555 1555 2.46
LINK CA CA A 401 O HOH A 668 1555 1555 2.47
LINK CA CA A 401 O HOH D 691 1555 1555 2.59
LINK CA CA A 401 O HOH D 651 1555 1555 2.44
LINK CA CA A 401 O HOH A 699 1555 1555 2.44
LINK CA CA B 401 O HOH C 673 1555 1555 2.54
LINK CA CA B 401 O HOH B 704 1555 1555 2.53
LINK CA CA B 401 O HOH C 646 1555 1555 2.43
LINK CA CA B 401 O HOH B 674 1555 1555 2.38
LINK CA CA B 401 O HOH B 706 1555 1555 2.41
CISPEP 1 PRO D 69 PRO D 70 0 -9.71
CISPEP 2 GLN D 191 PRO D 192 0 3.28
CISPEP 3 PRO A 69 PRO A 70 0 -8.18
CISPEP 4 GLN A 191 PRO A 192 0 3.52
CISPEP 5 PRO C 69 PRO C 70 0 -8.31
CISPEP 6 GLN C 191 PRO C 192 0 3.22
CISPEP 7 PRO B 69 PRO B 70 0 -8.62
CISPEP 8 GLN B 191 PRO B 192 0 3.09
SITE 1 AC1 9 CPQ A 403 THR D 186 ASN D 196 PRO D 218
SITE 2 AC1 9 PHE D 220 CPQ D 402 HOH D 501 HOH D 535
SITE 3 AC1 9 HOH D 597
SITE 1 AC2 3 PRO A 218 ALA D 287 CPQ D 401
SITE 1 AC3 7 ASP A 223 HOH A 668 HOH A 699 ASP D 223
SITE 2 AC3 7 HOH D 651 HOH D 691 HOH D 698
SITE 1 AC4 18 THR A 186 VAL A 194 SER A 195 ASN A 196
SITE 2 AC4 18 SER A 197 LEU A 199 GLN A 213 PRO A 218
SITE 3 AC4 18 PHE A 220 CPQ A 404 CPQ A 405 HOH A 519
SITE 4 AC4 18 HOH A 579 HOH A 665 HOH A 671 ARG C 302
SITE 5 AC4 18 THR C 316 PRO C 317
SITE 1 AC5 9 PRO A 143 TYR A 282 HOH A 531 HOH A 602
SITE 2 AC5 9 HOH A 638 LEU D 140 ALA D 185 GLN D 191
SITE 3 AC5 9 CPQ D 401
SITE 1 AC6 8 VAL A 139 LEU A 140 ALA A 185 THR A 186
SITE 2 AC6 8 GLN A 191 CPQ A 402 HOH A 561 LEU D 144
SITE 1 AC7 7 GLN A 46 PHE A 71 ALA A 283 ALA A 284
SITE 2 AC7 7 ALA A 287 CPQ A 402 PRO C 317
SITE 1 AC8 4 CPQ B 402 CPQ C 402 CPQ C 403 HOH C 633
SITE 1 AC9 11 CPQ B 402 THR C 186 VAL C 194 GLN C 213
SITE 2 AC9 11 PRO C 218 PHE C 220 CPQ C 401 HOH C 517
SITE 3 AC9 11 HOH C 622 HOH C 633 HOH C 816
SITE 1 AD1 9 GLN C 46 PHE C 71 ALA C 283 ALA C 287
SITE 2 AD1 9 CPQ C 401 HOH C 506 HOH C 514 HOH C 633
SITE 3 AD1 9 HOH C 801
SITE 1 AD2 7 ASP B 223 HOH B 674 HOH B 704 HOH B 706
SITE 2 AD2 7 ASP C 223 HOH C 646 HOH C 673
SITE 1 AD3 9 THR B 186 VAL B 194 GLN B 213 PRO B 218
SITE 2 AD3 9 PHE B 220 HOH B 562 HOH B 651 CPQ C 401
SITE 3 AD3 9 CPQ C 402
SITE 1 AD4 4 ALA B 185 THR B 186 HOH B 559 PRO C 143
CRYST1 46.980 155.970 92.530 90.00 90.00 90.00 P 1 21 1 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 0.021286 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006411 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010807 0.00000
TER 2337 THR D 316
TER 4664 VAL A 315
TER 7006 PRO C 317
TER 9340 THR B 316
MASTER 518 0 13 65 36 0 31 610911 4 405 100
END |