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HEADER HYDROLASE 29-DEC-18 6J1S
TITLE CRYSTAL STRUCTURE OF CANDIDA ANTARCTICA LIPASE B MUTANT - SS
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;
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 01-JAN-20 6J1S 0
JRNL AUTH J.XU,Y.CEN,W.SINGH,J.FAN,L.WU,X.LIN,J.ZHOU,M.HUANG,
JRNL AUTH 2 M.T.REETZ,Q.WU
JRNL TITL STEREODIVERGENT PROTEIN ENGINEERING OF A LIPASE TO ACCESS
JRNL TITL 2 ALL POSSIBLE STEREOISOMERS OF CHIRAL ESTERS WITH TWO
JRNL TITL 3 STEREOCENTERS.
JRNL REF J.AM.CHEM.SOC. V. 141 7934 2019
JRNL REFN ESSN 1520-5126
JRNL PMID 31023008
JRNL DOI 10.1021/JACS.9B02709
REMARK 2
REMARK 2 RESOLUTION. 1.83 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) : 1.83
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.21
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.7
REMARK 3 NUMBER OF REFLECTIONS : 45510
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.190
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.219
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2321
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 40.2182 - 4.7031 0.99 2696 139 0.1382 0.1512
REMARK 3 2 4.7031 - 3.7339 1.00 2670 161 0.1334 0.1695
REMARK 3 3 3.7339 - 3.2621 1.00 2671 129 0.1774 0.2129
REMARK 3 4 3.2621 - 2.9640 1.00 2634 159 0.2155 0.2229
REMARK 3 5 2.9640 - 2.7516 1.00 2653 149 0.2100 0.2405
REMARK 3 6 2.7516 - 2.5894 1.00 2612 159 0.2123 0.2186
REMARK 3 7 2.5894 - 2.4597 1.00 2643 145 0.2121 0.2490
REMARK 3 8 2.4597 - 2.3527 1.00 2629 141 0.2126 0.2618
REMARK 3 9 2.3527 - 2.2621 1.00 2680 128 0.2074 0.2287
REMARK 3 10 2.2621 - 2.1841 1.00 2679 125 0.2053 0.2683
REMARK 3 11 2.1841 - 2.1158 1.00 2615 126 0.2121 0.2553
REMARK 3 12 2.1158 - 2.0553 0.99 2638 154 0.2129 0.2454
REMARK 3 13 2.0553 - 2.0012 0.95 2514 138 0.2074 0.2435
REMARK 3 14 2.0012 - 1.9524 0.92 2433 121 0.2104 0.2349
REMARK 3 15 1.9524 - 1.9080 0.86 2249 122 0.2151 0.2985
REMARK 3 16 1.9080 - 1.8674 0.81 2133 112 0.2150 0.2726
REMARK 3 17 1.8674 - 1.8300 0.77 2040 113 0.2148 0.2496
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) : 0.200
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.490
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 : 0.010 4822
REMARK 3 ANGLE : 1.140 6620
REMARK 3 CHIRALITY : 0.064 770
REMARK 3 PLANARITY : 0.009 868
REMARK 3 DIHEDRAL : 13.637 2916
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): 24.5184 1.7697 75.6159
REMARK 3 T TENSOR
REMARK 3 T11: 0.1324 T22: 0.1435
REMARK 3 T33: 0.1219 T12: -0.0139
REMARK 3 T13: 0.0394 T23: -0.0084
REMARK 3 L TENSOR
REMARK 3 L11: 0.5394 L22: 0.7944
REMARK 3 L33: 0.9982 L12: -0.5824
REMARK 3 L13: 0.6919 L23: -0.7915
REMARK 3 S TENSOR
REMARK 3 S11: 0.1418 S12: 0.0730 S13: -0.0586
REMARK 3 S21: -0.1427 S22: -0.0276 S23: 0.0735
REMARK 3 S31: 0.1689 S32: 0.0842 S33: -0.0858
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 6J1S COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-JAN-19.
REMARK 100 THE DEPOSITION ID IS D_1300010235.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-JUN-17
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 : SSRF
REMARK 200 BEAMLINE : BL19U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97775
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 50449
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 6.100
REMARK 200 R MERGE (I) : 0.08100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 17.6820
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.83
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.28900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 5.240
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 (%): 40.61
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM SULFATE 0.1 M SODIUM
REMARK 280 CITRATE PH 5.5 25% PEG 4000, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 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 40.20850
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
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: 180 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12080 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 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: 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: 300 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12170 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 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 A -3
REMARK 465 ALA A -2
REMARK 465 MET A -1
REMARK 465 GLY B -3
REMARK 465 ALA B -2
REMARK 465 MET B -1
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 ASP B 75 CB - CG - OD2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 PRO B 260 C - N - CD ANGL. DEV. = -14.2 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 A 29 82.26 -153.75
REMARK 500 ASN A 51 -90.66 -149.80
REMARK 500 SER A 105 -119.02 47.28
REMARK 500 LEU A 134 65.17 -107.62
REMARK 500 ALA A 141 -112.39 42.98
REMARK 500 ALA A 146 -3.70 61.81
REMARK 500 ASN A 206 -1.02 73.92
REMARK 500 ALA A 305 35.11 -141.42
REMARK 500 SER B 29 88.53 -151.60
REMARK 500 ASN B 51 -91.08 -147.89
REMARK 500 ASP B 75 125.05 -36.84
REMARK 500 SER B 105 -121.15 52.01
REMARK 500 LEU B 134 64.65 -104.80
REMARK 500 GLN B 193 16.45 -141.94
REMARK 500 ASN B 206 -0.08 72.81
REMARK 500 ALA B 276 41.38 -109.87
REMARK 500 ALA B 305 36.34 -141.55
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 SO4 A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 403
DBREF 6J1S A 1 317 UNP P41365 LIPB_PSEA2 26 342
DBREF 6J1S B 1 317 UNP P41365 LIPB_PSEA2 26 342
SEQADV 6J1S GLY A -3 UNP P41365 EXPRESSION TAG
SEQADV 6J1S ALA A -2 UNP P41365 EXPRESSION TAG
SEQADV 6J1S MET A -1 UNP P41365 EXPRESSION TAG
SEQADV 6J1S ALA A 0 UNP P41365 EXPRESSION TAG
SEQADV 6J1S ALA A 57 UNP P41365 THR 82 ENGINEERED MUTATION
SEQADV 6J1S THR A 89 UNP P41365 ALA 114 ENGINEERED MUTATION
SEQADV 6J1S ALA A 104 UNP P41365 TRP 129 ENGINEERED MUTATION
SEQADV 6J1S LEU A 134 UNP P41365 ASP 159 ENGINEERED MUTATION
SEQADV 6J1S MET A 189 UNP P41365 ILE 214 ENGINEERED MUTATION
SEQADV 6J1S CYS A 190 UNP P41365 VAL 215 ENGINEERED MUTATION
SEQADV 6J1S GLY B -3 UNP P41365 EXPRESSION TAG
SEQADV 6J1S ALA B -2 UNP P41365 EXPRESSION TAG
SEQADV 6J1S MET B -1 UNP P41365 EXPRESSION TAG
SEQADV 6J1S ALA B 0 UNP P41365 EXPRESSION TAG
SEQADV 6J1S ALA B 57 UNP P41365 THR 82 ENGINEERED MUTATION
SEQADV 6J1S THR B 89 UNP P41365 ALA 114 ENGINEERED MUTATION
SEQADV 6J1S ALA B 104 UNP P41365 TRP 129 ENGINEERED MUTATION
SEQADV 6J1S LEU B 134 UNP P41365 ASP 159 ENGINEERED MUTATION
SEQADV 6J1S MET B 189 UNP P41365 ILE 214 ENGINEERED MUTATION
SEQADV 6J1S CYS B 190 UNP P41365 VAL 215 ENGINEERED MUTATION
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 ALA 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 LEU TYR LYS GLY THR VAL
SEQRES 12 A 321 LEU ALA GLY PRO LEU ASP ALA LEU ALA VAL 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 MET CYS 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 ALA ALA
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 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 ALA 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 LEU TYR LYS GLY THR VAL
SEQRES 12 B 321 LEU ALA GLY PRO LEU ASP ALA LEU ALA VAL 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 MET CYS 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 ALA ALA
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 SO4 A 401 5
HET SO4 A 402 5
HET PEG A 403 7
HET SO4 B 401 5
HET EDO B 402 4
HET EDO B 403 4
HETNAM SO4 SULFATE ION
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 SO4 3(O4 S 2-)
FORMUL 5 PEG C4 H10 O3
FORMUL 7 EDO 2(C2 H6 O2)
FORMUL 9 HOH *269(H2 O)
HELIX 1 AA1 PRO A 12 GLY A 19 1 8
HELIX 2 AA2 THR A 43 ASP A 49 1 7
HELIX 3 AA3 ASN A 51 LEU A 59 1 9
HELIX 4 AA4 ASP A 75 SER A 94 1 20
HELIX 5 AA5 GLN A 106 PHE A 118 1 13
HELIX 6 AA6 PRO A 119 ARG A 122 5 4
HELIX 7 AA7 ALA A 151 GLN A 157 1 7
HELIX 8 AA8 SER A 161 ALA A 170 1 10
HELIX 9 AA9 ALA A 212 GLY A 217 1 6
HELIX 10 AB1 ALA A 225 SER A 230 1 6
HELIX 11 AB2 SER A 230 SER A 243 1 14
HELIX 12 AB3 ARG A 249 TYR A 253 5 5
HELIX 13 AB4 GLY A 254 CYS A 258 5 5
HELIX 14 AB5 THR A 267 ALA A 275 1 9
HELIX 15 AB6 LEU A 277 GLY A 288 1 12
HELIX 16 AB7 ALA A 301 VAL A 306 5 6
HELIX 17 AB8 PRO B 12 GLY B 19 1 8
HELIX 18 AB9 THR B 43 ASP B 49 1 7
HELIX 19 AC1 ASN B 51 LEU B 59 1 9
HELIX 20 AC2 ASP B 75 SER B 94 1 20
HELIX 21 AC3 SER B 105 PHE B 118 1 14
HELIX 22 AC4 PRO B 119 SER B 123 5 5
HELIX 23 AC5 PRO B 143 LEU B 147 5 5
HELIX 24 AC6 ALA B 151 GLN B 157 1 7
HELIX 25 AC7 SER B 161 ALA B 170 1 10
HELIX 26 AC8 ALA B 212 GLY B 217 1 6
HELIX 27 AC9 ALA B 225 SER B 230 1 6
HELIX 28 AD1 SER B 230 SER B 243 1 14
HELIX 29 AD2 ARG B 249 TYR B 253 5 5
HELIX 30 AD3 GLY B 254 CYS B 258 5 5
HELIX 31 AD4 THR B 267 ALA B 276 1 10
HELIX 32 AD5 LEU B 277 GLY B 288 1 12
HELIX 33 AD6 ALA B 301 VAL B 306 5 6
SHEET 1 AA1 7 LEU A 20 CYS A 22 0
SHEET 2 AA1 7 THR A 62 ILE A 66 -1 O TRP A 65 N THR A 21
SHEET 3 AA1 7 PRO A 33 VAL A 37 1 N LEU A 36 O CYS A 64
SHEET 4 AA1 7 LEU A 99 ALA A 104 1 O LEU A 102 N LEU A 35
SHEET 5 AA1 7 VAL A 125 PHE A 131 1 O MET A 129 N VAL A 101
SHEET 6 AA1 7 THR A 179 TYR A 183 1 O THR A 180 N ALA A 130
SHEET 7 AA1 7 LYS A 208 GLN A 211 1 O VAL A 210 N ASN A 181
SHEET 1 AA2 2 ARG A 309 THR A 310 0
SHEET 2 AA2 2 GLY A 313 ILE A 314 -1 O GLY A 313 N THR A 310
SHEET 1 AA3 7 LEU B 20 CYS B 22 0
SHEET 2 AA3 7 THR B 62 ILE B 66 -1 O TRP B 65 N THR B 21
SHEET 3 AA3 7 PRO B 33 VAL B 37 1 N LEU B 36 O CYS B 64
SHEET 4 AA3 7 LEU B 99 ALA B 104 1 O LEU B 102 N LEU B 35
SHEET 5 AA3 7 VAL B 125 PHE B 131 1 O ASP B 126 N LEU B 99
SHEET 6 AA3 7 THR B 179 TYR B 183 1 O THR B 180 N ALA B 130
SHEET 7 AA3 7 LYS B 208 GLN B 211 1 O VAL B 210 N ASN B 181
SHEET 1 AA4 2 ARG B 309 THR B 310 0
SHEET 2 AA4 2 GLY B 313 ILE B 314 -1 O GLY B 313 N THR B 310
SSBOND 1 CYS A 22 CYS A 64 1555 1555 2.08
SSBOND 2 CYS A 216 CYS A 258 1555 1555 2.03
SSBOND 3 CYS A 293 CYS A 311 1555 1555 2.05
SSBOND 4 CYS B 22 CYS B 64 1555 1555 2.05
SSBOND 5 CYS B 216 CYS B 258 1555 1555 2.05
SSBOND 6 CYS B 293 CYS B 311 1555 1555 2.06
CISPEP 1 PRO A 69 PRO A 70 0 -14.50
CISPEP 2 GLN A 191 PRO A 192 0 4.20
CISPEP 3 PRO B 69 PRO B 70 0 -12.95
CISPEP 4 GLN B 191 PRO B 192 0 6.02
SITE 1 AC1 5 LYS A 208 ARG A 249 SER A 250 HOH A 502
SITE 2 AC1 5 HOH A 600
SITE 1 AC2 1 ARG A 168
SITE 1 AC3 4 ALA A 214 VAL A 215 GLY A 217 GLY B 142
SITE 1 AC4 4 LYS B 208 SER B 250 HOH B 519 HOH B 559
SITE 1 AC5 8 LYS B 32 PRO B 33 SER B 94 ASN B 97
SITE 2 AC5 8 LYS B 98 LEU B 99 PRO B 100 HOH B 563
SITE 1 AC6 4 TYR B 203 PHE B 205 ASN B 206 GLY B 207
CRYST1 46.998 80.417 73.167 90.00 98.47 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 0.021278 0.000000 0.003169 0.00000
SCALE2 0.000000 0.012435 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013818 0.00000
TER 2328 PRO A 317
TER 4675 PRO B 317
MASTER 320 0 6 33 18 0 8 6 4937 2 42 50
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