HEADER PROTEIN BINDING 01-JUL-15 5CBN
TITLE FUSION PROTEIN OF MBP3-16 AND B4 DOMAIN OF PROTEIN A FROM
TITLE 2 STAPHYLOCOCCAL AUREUS WITH CHEMICAL CROSS-LINKER EY-CBS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MALTOSE-BINDING PERIPLASMIC PROTEIN;
COMPND 3 CHAIN: B;
COMPND 4 FRAGMENT: UNP RESIDUES 31-392;
COMPND 5 SYNONYM: MBP,MMBP,MALTODEXTRIN-BINDING PROTEIN;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: MBP3-16,IMMUNOGLOBULIN G-BINDING PROTEIN A;
COMPND 9 CHAIN: A;
COMPND 10 FRAGMENT: B4 DOMAIN (UNP RESIDUES 218-269);
COMPND 11 SYNONYM: IGG-BINDING PROTEIN A,STAPHYLOCOCCAL PROTEIN A;
COMPND 12 ENGINEERED: YES;
COMPND 13 MUTATION: YES;
COMPND 14 OTHER_DETAILS: FUSION PROTEIN OF MBP3-16 AND B4 DOMAIN (UNP RESIDUES
COMPND 15 102-153) OF PROTEIN A
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI (STRAIN K12);
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K12;
SOURCE 5 GENE: MALE, B4034, JW3994;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT, STAPHYLOCOCCUS AUREUS;
SOURCE 10 ORGANISM_TAXID: 32630, 1280;
SOURCE 11 GENE: SPA;
SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 13 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS FUSION, EY-CBS, ALPHA HELIX, CROSS-LINKER, PROTEIN BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR W.H.JEONG,H.LEE,D.H.SONG,J.O.LEE
REVDAT 2 08-NOV-23 5CBN 1 REMARK
REVDAT 1 30-MAR-16 5CBN 0
JRNL AUTH W.H.JEONG,H.LEE,D.H.SONG,J.H.EOM,S.C.KIM,H.S.LEE,H.LEE,
JRNL AUTH 2 J.O.LEE
JRNL TITL CONNECTING TWO PROTEINS USING A FUSION ALPHA HELIX
JRNL TITL 2 STABILIZED BY A CHEMICAL CROSS LINKER.
JRNL REF NAT COMMUN V. 7 11031 2016
JRNL REFN ESSN 2041-1723
JRNL PMID 26980593
JRNL DOI 10.1038/NCOMMS11031
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.09
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 24741
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.198
REMARK 3 R VALUE (WORKING SET) : 0.193
REMARK 3 FREE R VALUE : 0.260
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 8.080
REMARK 3 FREE R VALUE TEST SET COUNT : 2000
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 42.0921 - 5.5394 1.00 1751 154 0.1580 0.1905
REMARK 3 2 5.5394 - 4.3983 1.00 1671 148 0.1581 0.2238
REMARK 3 3 4.3983 - 3.8428 1.00 1646 144 0.1646 0.2445
REMARK 3 4 3.8428 - 3.4916 1.00 1645 145 0.1801 0.2403
REMARK 3 5 3.4916 - 3.2414 1.00 1640 144 0.2116 0.2726
REMARK 3 6 3.2414 - 3.0504 1.00 1590 140 0.2319 0.2828
REMARK 3 7 3.0504 - 2.8977 1.00 1640 144 0.2283 0.3409
REMARK 3 8 2.8977 - 2.7716 1.00 1602 141 0.2436 0.3195
REMARK 3 9 2.7716 - 2.6649 1.00 1603 141 0.2322 0.3151
REMARK 3 10 2.6649 - 2.5729 0.99 1603 141 0.2304 0.3427
REMARK 3 11 2.5729 - 2.4925 0.99 1601 140 0.2220 0.2857
REMARK 3 12 2.4925 - 2.4213 0.99 1585 139 0.2177 0.2968
REMARK 3 13 2.4213 - 2.3575 1.00 1589 141 0.2198 0.2999
REMARK 3 14 2.3575 - 2.3000 0.99 1575 138 0.2222 0.2945
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) : 0.310
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.780
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 : 0.008 4278
REMARK 3 ANGLE : 1.080 5812
REMARK 3 CHIRALITY : 0.039 630
REMARK 3 PLANARITY : 0.006 758
REMARK 3 DIHEDRAL : 15.696 1560
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A
REMARK 3 ORIGIN FOR THE GROUP (A): 5.6357 -2.0688 -31.9572
REMARK 3 T TENSOR
REMARK 3 T11: 0.2781 T22: 0.2877
REMARK 3 T33: 0.3156 T12: 0.0678
REMARK 3 T13: 0.0162 T23: 0.0483
REMARK 3 L TENSOR
REMARK 3 L11: 1.6502 L22: 3.9356
REMARK 3 L33: 2.1340 L12: -0.9873
REMARK 3 L13: -0.2484 L23: 1.4016
REMARK 3 S TENSOR
REMARK 3 S11: 0.1853 S12: 0.3131 S13: 0.0101
REMARK 3 S21: -0.5416 S22: -0.1722 S23: -0.1234
REMARK 3 S31: -0.0353 S32: 0.1351 S33: -0.0566
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN B
REMARK 3 ORIGIN FOR THE GROUP (A): -3.2606 -11.1389 15.2610
REMARK 3 T TENSOR
REMARK 3 T11: 0.4166 T22: 0.3148
REMARK 3 T33: 0.3571 T12: 0.0812
REMARK 3 T13: 0.0446 T23: -0.0059
REMARK 3 L TENSOR
REMARK 3 L11: 0.1237 L22: 0.4738
REMARK 3 L33: 4.2222 L12: 0.5872
REMARK 3 L13: -0.9116 L23: -1.8548
REMARK 3 S TENSOR
REMARK 3 S11: -0.0575 S12: -0.0283 S13: -0.0893
REMARK 3 S21: -0.3229 S22: -0.0798 S23: -0.1244
REMARK 3 S31: 0.6206 S32: 0.3829 S33: 0.0641
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 5CBN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 07-JUL-15.
REMARK 100 THE DEPOSITION ID IS D_1000211328.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-MAY-10
REMARK 200 TEMPERATURE (KELVIN) : 77
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PAL/PLS
REMARK 200 BEAMLINE : 4A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24863
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
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 (%) : 99.7
REMARK 200 DATA REDUNDANCY : 6.700
REMARK 200 R MERGE (I) : 0.06300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.2
REMARK 200 DATA REDUNDANCY IN SHELL : 6.60
REMARK 200 R MERGE FOR SHELL (I) : 0.50500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> 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: PHASER 1.3.2
REMARK 200 STARTING MODEL: 1SVX
REMARK 200
REMARK 200 REMARK: NEEDLE-ROD
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.17
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 36% W/V PEG 2000, 0.2M MAGNESIUM
REMARK 280 CHLORIDE HEXAHYDRATE, PH 6.5, EVAPORATION, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-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 32.14100
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 55.67600
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.91350
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 55.67600
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 32.14100
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 37.91350
REMARK 290 SMTRY3 4 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 APPLY THE FOLLOWING TO CHAINS: B, A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET B -2
REMARK 465 GLY B -1
REMARK 465 MET B 0
REMARK 465 LYS B 1
REMARK 465 ILE B 2
REMARK 465 GLU B 3
REMARK 465 GLU B 4
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 SER B 255 O HOH B 401 1.93
REMARK 500 O HOH A 1417 O HOH A 1436 1.97
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OE2 GLU B 278 OH TYR A 1225 4445 1.90
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 ASP B 55 -169.67 -117.31
REMARK 500 LEU B 122 85.13 -156.18
REMARK 500 ASN B 150 107.42 -54.67
REMARK 500 TYR B 167 146.10 -173.04
REMARK 500 TYR B 171 41.84 -87.04
REMARK 500 ASP B 209 -167.66 -112.76
REMARK 500 ASN B 332 30.15 -78.00
REMARK 500 GLN B 365 -17.73 -167.73
REMARK 500 ASP A 13 -105.54 -173.76
REMARK 500 ASP A1248 65.37 -173.30
REMARK 500 PRO A1268 52.81 -67.35
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 EYC A 1301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5CBO RELATED DB: PDB
DBREF 5CBN B 1 366 UNP P0AEX9 MALE_ECOLI 27 392
DBREF 5CBN A 12 135 PDB 5CBN 5CBN 12 135
DBREF 5CBN A 1218 1269 UNP P38507 SPA_STAAU 218 269
SEQADV 5CBN MET B -2 UNP P0AEX9 EXPRESSION TAG
SEQADV 5CBN GLY B -1 UNP P0AEX9 EXPRESSION TAG
SEQADV 5CBN MET B 0 UNP P0AEX9 EXPRESSION TAG
SEQADV 5CBN ALA A 1219 UNP P38507 GLU 219 ENGINEERED MUTATION
SEQADV 5CBN ALA A 1222 UNP P38507 ASN 222 ENGINEERED MUTATION
SEQADV 5CBN CYS A 1226 UNP P38507 GLU 226 ENGINEERED MUTATION
SEQADV 5CBN ALA A 1240 UNP P38507 GLY 240 ENGINEERED MUTATION
SEQRES 1 B 369 MET GLY MET LYS ILE GLU GLU GLY LYS LEU VAL ILE TRP
SEQRES 2 B 369 ILE ASN GLY ASP LYS GLY TYR ASN GLY LEU ALA GLU VAL
SEQRES 3 B 369 GLY LYS LYS PHE GLU LYS ASP THR GLY ILE LYS VAL THR
SEQRES 4 B 369 VAL GLU HIS PRO ASP LYS LEU GLU GLU LYS PHE PRO GLN
SEQRES 5 B 369 VAL ALA ALA THR GLY ASP GLY PRO ASP ILE ILE PHE TRP
SEQRES 6 B 369 ALA HIS ASP ARG PHE GLY GLY TYR ALA GLN SER GLY LEU
SEQRES 7 B 369 LEU ALA GLU ILE THR PRO ASP LYS ALA PHE GLN ASP LYS
SEQRES 8 B 369 LEU TYR PRO PHE THR TRP ASP ALA VAL ARG TYR ASN GLY
SEQRES 9 B 369 LYS LEU ILE ALA TYR PRO ILE ALA VAL GLU ALA LEU SER
SEQRES 10 B 369 LEU ILE TYR ASN LYS ASP LEU LEU PRO ASN PRO PRO LYS
SEQRES 11 B 369 THR TRP GLU GLU ILE PRO ALA LEU ASP LYS GLU LEU LYS
SEQRES 12 B 369 ALA LYS GLY LYS SER ALA LEU MET PHE ASN LEU GLN GLU
SEQRES 13 B 369 PRO TYR PHE THR TRP PRO LEU ILE ALA ALA ASP GLY GLY
SEQRES 14 B 369 TYR ALA PHE LYS TYR GLU ASN GLY LYS TYR ASP ILE LYS
SEQRES 15 B 369 ASP VAL GLY VAL ASP ASN ALA GLY ALA LYS ALA GLY LEU
SEQRES 16 B 369 THR PHE LEU VAL ASP LEU ILE LYS ASN LYS HIS MET ASN
SEQRES 17 B 369 ALA ASP THR ASP TYR SER ILE ALA GLU ALA ALA PHE ASN
SEQRES 18 B 369 LYS GLY GLU THR ALA MET THR ILE ASN GLY PRO TRP ALA
SEQRES 19 B 369 TRP SER ASN ILE ASP THR SER LYS VAL ASN TYR GLY VAL
SEQRES 20 B 369 THR VAL LEU PRO THR PHE LYS GLY GLN PRO SER LYS PRO
SEQRES 21 B 369 PHE VAL GLY VAL LEU SER ALA GLY ILE ASN ALA ALA SER
SEQRES 22 B 369 PRO ASN LYS GLU LEU ALA LYS GLU PHE LEU GLU ASN TYR
SEQRES 23 B 369 LEU LEU THR ASP GLU GLY LEU GLU ALA VAL ASN LYS ASP
SEQRES 24 B 369 LYS PRO LEU GLY ALA VAL ALA LEU LYS SER TYR GLU GLU
SEQRES 25 B 369 GLU LEU ALA LYS ASP PRO ARG ILE ALA ALA THR MET GLU
SEQRES 26 B 369 ASN ALA GLN LYS GLY GLU ILE MET PRO ASN ILE PRO GLN
SEQRES 27 B 369 MET SER ALA PHE TRP TYR ALA VAL ARG THR ALA VAL ILE
SEQRES 28 B 369 ASN ALA ALA SER GLY ARG GLN THR VAL ASP GLU ALA LEU
SEQRES 29 B 369 LYS ASP ALA GLN THR
SEQRES 1 A 176 SER ASP LEU GLY LYS LYS LEU LEU GLU ALA ALA HIS ALA
SEQRES 2 A 176 GLY GLN ASP ASP GLU VAL ARG ILE LEU MET ALA ASN GLY
SEQRES 3 A 176 ALA ASP VAL ASN ALA MET ASP ASN PHE GLY VAL THR PRO
SEQRES 4 A 176 LEU HIS LEU ALA ALA TYR TRP GLY HIS PHE GLU ILE VAL
SEQRES 5 A 176 GLU VAL LEU LEU LYS TYR GLY ALA ASP VAL ASN ALA SER
SEQRES 6 A 176 ASP ALA THR GLY ASP THR PRO LEU HIS LEU ALA ALA LYS
SEQRES 7 A 176 TRP GLY TYR LEU GLY ILE VAL GLU VAL LEU LEU LYS TYR
SEQRES 8 A 176 GLY ALA ASP VAL ASN ALA GLN ASP LYS PHE GLY LYS THR
SEQRES 9 A 176 ALA PHE ASP ILE SER ILE ASP ASN GLY ASN GLU ASP LEU
SEQRES 10 A 176 ALA GLU ILE LEU CYS LYS ASN LYS ALA GLN GLN ALA ALA
SEQRES 11 A 176 PHE TYR CYS ILE LEU HIS LEU PRO ASN LEU ASN GLU GLU
SEQRES 12 A 176 GLN ARG ASN ALA PHE ILE GLN SER LEU LYS ASP ASP PRO
SEQRES 13 A 176 SER GLN SER ALA ASN LEU LEU ALA GLU ALA LYS LYS LEU
SEQRES 14 A 176 ASN ASP ALA GLN ALA PRO LYS
HET EYC A1301 30
HETNAM EYC 2,2'-ETHYNE-1,2-DIYLBIS{5-[(CHLOROACETYL)
HETNAM 2 EYC AMINO]BENZENESULFONIC ACID}
FORMUL 3 EYC C18 H14 CL2 N2 O8 S2
FORMUL 4 HOH *113(H2 O)
HELIX 1 AA1 GLY B 16 GLY B 32 1 17
HELIX 2 AA2 LYS B 42 ALA B 52 1 11
HELIX 3 AA3 ARG B 66 SER B 73 1 8
HELIX 4 AA4 ASP B 82 ASP B 87 1 6
HELIX 5 AA5 TYR B 90 ALA B 96 1 7
HELIX 6 AA6 THR B 128 GLU B 130 5 3
HELIX 7 AA7 GLU B 131 LYS B 142 1 12
HELIX 8 AA8 GLU B 153 ALA B 162 1 10
HELIX 9 AA9 TYR B 171 LYS B 175 5 5
HELIX 10 AB1 ASN B 185 ASN B 201 1 17
HELIX 11 AB2 ASP B 209 LYS B 219 1 11
HELIX 12 AB3 GLY B 228 TRP B 230 5 3
HELIX 13 AB4 ALA B 231 LYS B 239 1 9
HELIX 14 AB5 ASN B 272 TYR B 283 1 12
HELIX 15 AB6 THR B 286 LYS B 297 1 12
HELIX 16 AB7 LEU B 304 ALA B 312 1 9
HELIX 17 AB8 ASP B 314 GLY B 327 1 14
HELIX 18 AB9 GLN B 335 SER B 352 1 18
HELIX 19 AC1 THR B 356 ALA B 364 1 9
HELIX 20 AC2 ASP A 13 GLY A 25 1 13
HELIX 21 AC3 GLN A 26 ASN A 36 1 11
HELIX 22 AC4 THR A 49 GLY A 58 1 10
HELIX 23 AC5 HIS A 59 TYR A 69 1 11
HELIX 24 AC6 THR A 82 TRP A 90 1 9
HELIX 25 AC7 TYR A 92 TYR A 102 1 11
HELIX 26 AC8 THR A 115 ASN A 123 1 9
HELIX 27 AC9 ASN A 125 LEU A 1230 1 24
HELIX 28 AD1 ASN A 1234 ASP A 1247 1 14
HELIX 29 AD2 GLN A 1251 GLN A 1266 1 16
SHEET 1 AA1 6 VAL B 35 GLU B 38 0
SHEET 2 AA1 6 LEU B 7 TRP B 10 1 N LEU B 7 O THR B 36
SHEET 3 AA1 6 ILE B 59 ALA B 63 1 O PHE B 61 N TRP B 10
SHEET 4 AA1 6 PHE B 258 ILE B 266 -1 O SER B 263 N TRP B 62
SHEET 5 AA1 6 TYR B 106 GLU B 111 -1 N ILE B 108 O LEU B 262
SHEET 6 AA1 6 ALA B 301 VAL B 302 -1 O ALA B 301 N VAL B 110
SHEET 1 AA2 5 VAL B 35 GLU B 38 0
SHEET 2 AA2 5 LEU B 7 TRP B 10 1 N LEU B 7 O THR B 36
SHEET 3 AA2 5 ILE B 59 ALA B 63 1 O PHE B 61 N TRP B 10
SHEET 4 AA2 5 PHE B 258 ILE B 266 -1 O SER B 263 N TRP B 62
SHEET 5 AA2 5 GLU B 328 ILE B 329 1 O GLU B 328 N VAL B 259
SHEET 1 AA3 2 ARG B 98 TYR B 99 0
SHEET 2 AA3 2 LYS B 102 LEU B 103 -1 O LYS B 102 N TYR B 99
SHEET 1 AA4 4 SER B 145 LEU B 147 0
SHEET 2 AA4 4 THR B 222 ASN B 227 1 O ALA B 223 N SER B 145
SHEET 3 AA4 4 SER B 114 ASN B 118 -1 N ASN B 118 O ALA B 223
SHEET 4 AA4 4 TYR B 242 THR B 245 -1 O THR B 245 N LEU B 115
LINK SG CYS A 133 C03 EYC A1301 1555 1555 1.79
LINK SG CYS A1226 C19 EYC A1301 1555 1555 1.76
SITE 1 AC1 12 GLN A 26 ASP A 28 GLU A 29 CYS A 133
SITE 2 AC1 12 ALA A1222 CYS A1226 LEU A1256 LYS A1260
SITE 3 AC1 12 HOH A1402 HOH A1408 LYS B 26 ASP B 30
CRYST1 64.282 75.827 111.352 90.00 90.00 90.00 P 21 21 21 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 0.015556 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013188 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008981 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
