HEADER IMMUNE SYSTEM 11-NOV-17 6BLQ
TITLE CRYSTAL STRUCTURE OF IAG7 IN COMPLEX WITH INSULIN MIMOTOPE P8E9E
CAVEAT 6BLQ THE GAP DISTANCE ( 31.33 ANGSTROM ) BETWEEN RESIDUES ( B GLY
CAVEAT 2 6BLQ -11 ) AND ( B GLY 3 ) IS TOO LARGE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: H-2 CLASS II HISTOCOMPATIBILITY ANTIGEN, A-D ALPHA CHAIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: H2-AB1 PROTEIN;
COMPND 7 CHAIN: B;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: H2-AA;
SOURCE 6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 8 EXPRESSION_SYSTEM_CELL: HI5;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 11 ORGANISM_COMMON: MOUSE;
SOURCE 12 ORGANISM_TAXID: 10090;
SOURCE 13 GENE: H2-AB1;
SOURCE 14 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 16 EXPRESSION_SYSTEM_CELL_LINE: HI5
KEYWDS INSULIN, TYPE I DIABETES, T CELL, AUTOIMMUNE DISEASE, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.WANG,S.DAI
REVDAT 7 04-OCT-23 6BLQ 1 HETSYN
REVDAT 6 29-JUL-20 6BLQ 1 COMPND REMARK HETNAM LINK
REVDAT 6 2 1 SITE ATOM
REVDAT 5 11-DEC-19 6BLQ 1 SEQADV
REVDAT 4 17-JAN-18 6BLQ 1 REMARK
REVDAT 3 10-JAN-18 6BLQ 1 JRNL
REVDAT 2 03-JAN-18 6BLQ 1 JRNL
REVDAT 1 20-DEC-17 6BLQ 0
JRNL AUTH Y.WANG,T.SOSINOWSKI,A.NOVIKOV,F.CRAWFORD,D.B.NEAU,J.YANG,
JRNL AUTH 2 W.W.KWOK,P.MARRACK,J.W.KAPPLER,S.DAI
JRNL TITL C-TERMINAL MODIFICATION OF THE INSULIN B:11-23 PEPTIDE
JRNL TITL 2 CREATES SUPERAGONISTS IN MOUSE AND HUMAN TYPE 1 DIABETES.
JRNL REF PROC. NATL. ACAD. SCI. V. 115 162 2018
JRNL REF 2 U.S.A.
JRNL REFN ESSN 1091-6490
JRNL PMID 29255035
JRNL DOI 10.1073/PNAS.1716527115
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.12_2829: ???)
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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.87
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.380
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.8
REMARK 3 NUMBER OF REFLECTIONS : 44763
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.170
REMARK 3 R VALUE (WORKING SET) : 0.168
REMARK 3 FREE R VALUE : 0.203
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990
REMARK 3 FREE R VALUE TEST SET COUNT : 2235
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 40.8827 - 4.5338 0.99 2869 151 0.1574 0.1885
REMARK 3 2 4.5338 - 3.5993 1.00 2847 142 0.1502 0.1747
REMARK 3 3 3.5993 - 3.1445 1.00 2836 149 0.1539 0.1968
REMARK 3 4 3.1445 - 2.8571 1.00 2833 145 0.1718 0.1857
REMARK 3 5 2.8571 - 2.6523 1.00 2829 166 0.1748 0.1988
REMARK 3 6 2.6523 - 2.4960 1.00 2845 149 0.1756 0.2231
REMARK 3 7 2.4960 - 2.3710 1.00 2797 170 0.1802 0.2076
REMARK 3 8 2.3710 - 2.2678 0.99 2837 121 0.1663 0.2381
REMARK 3 9 2.2678 - 2.1805 1.00 2761 163 0.1681 0.2113
REMARK 3 10 2.1805 - 2.1053 0.99 2830 159 0.1740 0.2166
REMARK 3 11 2.1053 - 2.0394 0.99 2802 163 0.1865 0.2305
REMARK 3 12 2.0394 - 1.9811 0.98 2779 139 0.1944 0.2189
REMARK 3 13 1.9811 - 1.9290 0.94 2669 138 0.1902 0.2422
REMARK 3 14 1.9290 - 1.8819 0.86 2413 111 0.1995 0.2402
REMARK 3 15 1.8819 - 1.8391 0.69 1983 93 0.2053 0.2368
REMARK 3 16 1.8391 - 1.8000 0.56 1598 76 0.2116 0.2681
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) : 0.160
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.210
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 : 0.007 3329
REMARK 3 ANGLE : 0.875 4517
REMARK 3 CHIRALITY : 0.059 490
REMARK 3 PLANARITY : 0.006 583
REMARK 3 DIHEDRAL : 8.515 2663
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 6BLQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-NOV-17.
REMARK 100 THE DEPOSITION ID IS D_1000231076.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-JAN-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979500
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 : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 44763
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 (%) : 99.8
REMARK 200 DATA REDUNDANCY : 5.800
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.5000
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) : 1.84
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.48000
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
REMARK 200 STARTING MODEL: 5DMK
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.46
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.82
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG3350, 100MM SODIUM CITRATE AT
REMARK 280 PH5.0, 5% ISOPROPANOL, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298K
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 56.36650
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: 9250 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19220 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 20.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 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 GLU A 181
REMARK 465 SER B -4
REMARK 465 LEU B -3
REMARK 465 VAL B -2
REMARK 465 GLY B -1
REMARK 465 GLY B 0
REMARK 465 SER B 1
REMARK 465 GLY B 2
REMARK 465 ARG B 106
REMARK 465 THR B 107
REMARK 465 GLU B 108
REMARK 465 ALA B 109
REMARK 465 LEU B 110
REMARK 465 ASN B 111
REMARK 465 HIS B 112
REMARK 465 GLN B 192
REMARK 465 GLY B 193
REMARK 465 GLY B 194
REMARK 465 LEU B 195
REMARK 465 VAL B 196
REMARK 465 PRO B 197
REMARK 465 ARG B 198
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 HIS B 113 CG ND1 CD2 CE1 NE2
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 B 465 O HOH B 484 2.10
REMARK 500 O HOH B 384 O HOH B 421 2.14
REMARK 500 O HOH B 455 O HOH B 460 2.17
REMARK 500 OE1 GLU B 85 O HOH B 301 2.18
REMARK 500 O HOH B 340 O HOH B 383 2.19
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 O HOH A 421 O HOH A 461 1655 2.17
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 ASN B 35 -106.27 51.98
REMARK 500 THR B 90 -85.82 -123.19
REMARK 500 ASN B 114 -135.10 -123.34
REMARK 500 PRO B 125 -168.71 -79.87
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 496 DISTANCE = 5.95 ANGSTROMS
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 INSULIN MIMOTOPE
DBREF 6BLQ A -3 181 UNP P04228 HA2D_MOUSE 24 208
DBREF 6BLQ B 5 192 UNP Q31135 Q31135_MOUSE 30 217
SEQADV 6BLQ HIS B -28 UNP Q31135 SEE REMARK 999
SEQADV 6BLQ LEU B -27 UNP Q31135 SEE REMARK 999
SEQADV 6BLQ VAL B -26 UNP Q31135 SEE REMARK 999
SEQADV 6BLQ GLU B -25 UNP Q31135 SEE REMARK 999
SEQADV 6BLQ ARG B -24 UNP Q31135 SEE REMARK 999
SEQADV 6BLQ LEU B -23 UNP Q31135 SEE REMARK 999
SEQADV 6BLQ TYR B -22 UNP Q31135 SEE REMARK 999
SEQADV 6BLQ LEU B -21 UNP Q31135 SEE REMARK 999
SEQADV 6BLQ VAL B -20 UNP Q31135 SEE REMARK 999
SEQADV 6BLQ CYS B -19 UNP Q31135 SEE REMARK 999
SEQADV 6BLQ GLY B -18 UNP Q31135 SEE REMARK 999
SEQADV 6BLQ GLU B -17 UNP Q31135 SEE REMARK 999
SEQADV 6BLQ GLU B -16 UNP Q31135 SEE REMARK 999
SEQADV 6BLQ GLY B -15 UNP Q31135 LINKER
SEQADV 6BLQ ALA B -14 UNP Q31135 LINKER
SEQADV 6BLQ GLY B -13 UNP Q31135 LINKER
SEQADV 6BLQ GLY B -12 UNP Q31135 LINKER
SEQADV 6BLQ GLY B -11 UNP Q31135 LINKER
SEQADV 6BLQ SER B -4 UNP Q31135 LINKER
SEQADV 6BLQ LEU B -3 UNP Q31135 LINKER
SEQADV 6BLQ VAL B -2 UNP Q31135 LINKER
SEQADV 6BLQ GLY B -1 UNP Q31135 LINKER
SEQADV 6BLQ GLY B 0 UNP Q31135 LINKER
SEQADV 6BLQ SER B 1 UNP Q31135 LINKER
SEQADV 6BLQ GLY B 2 UNP Q31135 LINKER
SEQADV 6BLQ GLY B 3 UNP Q31135 LINKER
SEQADV 6BLQ GLY B 4 UNP Q31135 LINKER
SEQADV 6BLQ GLY B 193 UNP Q31135 EXPRESSION TAG
SEQADV 6BLQ GLY B 194 UNP Q31135 EXPRESSION TAG
SEQADV 6BLQ LEU B 195 UNP Q31135 EXPRESSION TAG
SEQADV 6BLQ VAL B 196 UNP Q31135 EXPRESSION TAG
SEQADV 6BLQ PRO B 197 UNP Q31135 EXPRESSION TAG
SEQADV 6BLQ ARG B 198 UNP Q31135 EXPRESSION TAG
SEQRES 1 A 185 GLU ASP ASP ILE GLU ALA ASP HIS VAL GLY PHE TYR GLY
SEQRES 2 A 185 THR THR VAL TYR GLN SER PRO GLY ASP ILE GLY GLN TYR
SEQRES 3 A 185 THR HIS GLU PHE ASP GLY ASP GLU LEU PHE TYR VAL ASP
SEQRES 4 A 185 LEU ASP LYS LYS LYS THR VAL TRP ARG LEU PRO GLU PHE
SEQRES 5 A 185 GLY GLN LEU ILE LEU PHE GLU PRO GLN GLY GLY LEU GLN
SEQRES 6 A 185 ASN ILE ALA ALA GLU LYS HIS ASN LEU GLY ILE LEU THR
SEQRES 7 A 185 LYS ARG SER ASN PHE THR PRO ALA THR ASN GLU ALA PRO
SEQRES 8 A 185 GLN ALA THR VAL PHE PRO LYS SER PRO VAL LEU LEU GLY
SEQRES 9 A 185 GLN PRO ASN THR LEU ILE CYS PHE VAL ASP ASN ILE PHE
SEQRES 10 A 185 PRO PRO VAL ILE ASN ILE THR TRP LEU ARG ASN SER LYS
SEQRES 11 A 185 SER VAL THR ASP GLY VAL TYR GLU THR SER PHE LEU VAL
SEQRES 12 A 185 ASN ARG ASP HIS SER PHE HIS LYS LEU SER TYR LEU THR
SEQRES 13 A 185 PHE ILE PRO SER ASP ASP ASP ILE TYR ASP CYS LYS VAL
SEQRES 14 A 185 GLU HIS TRP GLY LEU GLU GLU PRO VAL LEU LYS HIS TRP
SEQRES 15 A 185 GLU PRO GLU
SEQRES 1 B 221 HIS LEU VAL GLU ARG LEU TYR LEU VAL CYS GLY GLU GLU
SEQRES 2 B 221 GLY ALA GLY GLY GLY SER LEU VAL GLY GLY SER GLY GLY
SEQRES 3 B 221 GLY SER GLU ARG HIS PHE VAL HIS GLN PHE LYS GLY GLU
SEQRES 4 B 221 CYS TYR PHE THR ASN GLY THR GLN ARG ILE ARG LEU VAL
SEQRES 5 B 221 THR ARG TYR ILE TYR ASN ARG GLU GLU TYR LEU ARG PHE
SEQRES 6 B 221 ASP SER ASP VAL GLY GLU TYR ARG ALA VAL THR GLU LEU
SEQRES 7 B 221 GLY ARG HIS SER ALA GLU TYR TYR ASN LYS GLN TYR LEU
SEQRES 8 B 221 GLU ARG THR ARG ALA GLU LEU ASP THR ALA CYS ARG HIS
SEQRES 9 B 221 ASN TYR GLU GLU THR GLU VAL PRO THR SER LEU ARG ARG
SEQRES 10 B 221 LEU GLU GLN PRO ASN VAL ALA ILE SER LEU SER ARG THR
SEQRES 11 B 221 GLU ALA LEU ASN HIS HIS ASN THR LEU VAL CYS SER VAL
SEQRES 12 B 221 THR ASP PHE TYR PRO ALA LYS ILE LYS VAL ARG TRP PHE
SEQRES 13 B 221 ARG ASN GLY GLN GLU GLU THR VAL GLY VAL SER SER THR
SEQRES 14 B 221 GLN LEU ILE ARG ASN GLY ASP TRP THR PHE GLN VAL LEU
SEQRES 15 B 221 VAL MET LEU GLU MET THR PRO HIS GLN GLY GLU VAL TYR
SEQRES 16 B 221 THR CYS HIS VAL GLU HIS PRO SER LEU LYS SER PRO ILE
SEQRES 17 B 221 THR VAL GLU TRP ARG ALA GLN GLY GLY LEU VAL PRO ARG
HET NAG C 1 14
HET NAG C 2 14
HET NAG A 201 14
HET IPA A 204 4
HET IPA A 205 4
HET IPA A 206 4
HET EDO A 207 4
HET EDO A 208 4
HET EDO A 209 4
HET NAG B 201 14
HET IPA B 202 4
HET EDO B 203 4
HET EDO B 204 4
HET EDO B 205 4
HET EDO B 206 4
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM IPA ISOPROPYL ALCOHOL
HETNAM EDO 1,2-ETHANEDIOL
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN IPA 2-PROPANOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 NAG 4(C8 H15 N O6)
FORMUL 5 IPA 4(C3 H8 O)
FORMUL 8 EDO 7(C2 H6 O2)
FORMUL 17 HOH *394(H2 O)
HELIX 1 AA1 LEU A 45 GLN A 50 5 6
HELIX 2 AA2 PRO A 56 SER A 77 1 22
HELIX 3 AA3 THR B 53 LEU B 55 5 3
HELIX 4 AA4 GLY B 56 TYR B 67 1 12
HELIX 5 AA5 TYR B 67 ALA B 78 1 12
HELIX 6 AA6 ALA B 78 THR B 86 1 9
HELIX 7 AA7 THR B 90 ARG B 94 5 5
SHEET 1 AA1 8 LYS A 40 TRP A 43 0
SHEET 2 AA1 8 ASP A 29 ASP A 35 -1 N ASP A 35 O LYS A 40
SHEET 3 AA1 8 ILE A 19 PHE A 26 -1 N HIS A 24 O LEU A 31
SHEET 4 AA1 8 HIS A 4 SER A 15 -1 N PHE A 7 O GLU A 25
SHEET 5 AA1 8 PHE B 9 THR B 20 -1 O CYS B 17 N GLY A 6
SHEET 6 AA1 8 ARG B 25 TYR B 34 -1 O ARG B 27 N TYR B 18
SHEET 7 AA1 8 GLU B 37 ASP B 43 -1 O GLU B 37 N TYR B 34
SHEET 8 AA1 8 TYR B 49 ALA B 51 -1 O ARG B 50 N ARG B 41
SHEET 1 AA2 2 ILE A 52 LEU A 53 0
SHEET 2 AA2 2 VAL B -26 GLU B -25 1 O VAL B -26 N LEU A 53
SHEET 1 AA3 4 GLN A 88 PRO A 93 0
SHEET 2 AA3 4 ASN A 103 ILE A 112 -1 O PHE A 108 N THR A 90
SHEET 3 AA3 4 PHE A 145 PHE A 153 -1 O PHE A 153 N ASN A 103
SHEET 4 AA3 4 VAL A 132 GLU A 134 -1 N TYR A 133 O TYR A 150
SHEET 1 AA4 4 GLN A 88 PRO A 93 0
SHEET 2 AA4 4 ASN A 103 ILE A 112 -1 O PHE A 108 N THR A 90
SHEET 3 AA4 4 PHE A 145 PHE A 153 -1 O PHE A 153 N ASN A 103
SHEET 4 AA4 4 LEU A 138 VAL A 139 -1 N LEU A 138 O HIS A 146
SHEET 1 AA5 4 LYS A 126 VAL A 128 0
SHEET 2 AA5 4 ASN A 118 ARG A 123 -1 N ARG A 123 O LYS A 126
SHEET 3 AA5 4 TYR A 161 GLU A 166 -1 O LYS A 164 N THR A 120
SHEET 4 AA5 4 VAL A 174 TRP A 178 -1 O LYS A 176 N CYS A 163
SHEET 1 AA6 4 ASN B 99 SER B 103 0
SHEET 2 AA6 4 THR B 115 PHE B 123 -1 O VAL B 117 N SER B 103
SHEET 3 AA6 4 PHE B 156 GLU B 163 -1 O VAL B 160 N CYS B 118
SHEET 4 AA6 4 VAL B 143 SER B 145 -1 N SER B 144 O MET B 161
SHEET 1 AA7 4 ASN B 99 SER B 103 0
SHEET 2 AA7 4 THR B 115 PHE B 123 -1 O VAL B 117 N SER B 103
SHEET 3 AA7 4 PHE B 156 GLU B 163 -1 O VAL B 160 N CYS B 118
SHEET 4 AA7 4 ILE B 149 ARG B 150 -1 N ILE B 149 O GLN B 157
SHEET 1 AA8 4 GLN B 137 GLU B 139 0
SHEET 2 AA8 4 LYS B 129 ARG B 134 -1 N ARG B 134 O GLN B 137
SHEET 3 AA8 4 VAL B 171 GLU B 177 -1 O HIS B 175 N ARG B 131
SHEET 4 AA8 4 ILE B 185 ARG B 190 -1 O ILE B 185 N VAL B 176
SSBOND 1 CYS A 107 CYS A 163 1555 1555 2.03
SSBOND 2 CYS B 17 CYS B 79 1555 1555 2.06
SSBOND 3 CYS B 118 CYS B 174 1555 1555 2.03
LINK ND2 ASN A 78 C1 NAG A 201 1555 1555 1.43
LINK ND2 ASN A 118 C1 NAG C 1 1555 1555 1.43
LINK ND2 ASN B 21 C1 NAG B 201 1555 1555 1.45
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.44
CISPEP 1 TYR A 8 GLY A 9 0 9.51
CISPEP 2 SER A 15 PRO A 16 0 -3.81
CISPEP 3 PHE A 113 PRO A 114 0 -4.33
CISPEP 4 HIS B 113 ASN B 114 0 5.73
CISPEP 5 TYR B 124 PRO B 125 0 3.39
CISPEP 6 VAL B 141 GLY B 142 0 -9.18
CISPEP 7 GLN B 168 GLY B 169 0 -9.03
CRYST1 39.274 112.733 62.172 90.00 107.32 90.00 P 1 21 1 2
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 0.025462 0.000000 0.007940 0.00000
SCALE2 0.000000 0.008871 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016848 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
