HEADER IMMUNE SYSTEM 16-JUL-13 3WEX
TITLE CRYSTAL STRUCTURE OF HLA-DP5 IN COMPLEX WITH CRY J 1-DERIVED PEPTIDE
TITLE 2 (RESIDUES 214-222)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MHC CLASS II ANTIGEN;
COMPND 3 CHAIN: A, C, E, G;
COMPND 4 FRAGMENT: EXTRACELLULAR DOMAIN, UNP RESIDUES 32-212;
COMPND 5 SYNONYM: HLA-DP5 ALPHA CHAIN;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: MHC CLASS II ANTIGEN;
COMPND 9 CHAIN: B, D, F, H;
COMPND 10 FRAGMENT: EXTRACELLULAR DOMAIN, UNP RESIDUES 1-184;
COMPND 11 SYNONYM: HLA-DP5 BETA CHAIN;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: BACULOVIRUS;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 13 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 14 EXPRESSION_SYSTEM_PLASMID: BACULOVIRUS
KEYWDS IMMUNOGLOBULIN FOLD, ANTIGEN PRESENTATION, T CELL RECEPTOR, CELL
KEYWDS 2 SURFACE, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR S.KUSANO,M.KUKIMOTO-NIINO,M.SHIROUZU,S.YOKOYAMA
REVDAT 3 29-JUL-20 3WEX 1 COMPND REMARK SEQADV HETNAM
REVDAT 3 2 1 LINK SITE
REVDAT 2 26-APR-17 3WEX 1 JRNL
REVDAT 1 23-JUL-14 3WEX 0
JRNL AUTH S.KUSANO,M.KUKIMOTO-NIINO,Y.SATTA,N.OHSAWA,T.UCHIKUBO-KAMO,
JRNL AUTH 2 M.WAKIYAMA,M.IKEDA,T.TERADA,K.YAMAMOTO,Y.NISHIMURA,
JRNL AUTH 3 M.SHIROUZU,T.SASAZUKI,S.YOKOYAMA
JRNL TITL STRUCTURAL BASIS FOR THE SPECIFIC RECOGNITION OF THE MAJOR
JRNL TITL 2 ANTIGENIC PEPTIDE FROM THE JAPANESE CEDAR POLLEN ALLERGEN
JRNL TITL 3 CRY J 1 BY HLA-DP5
JRNL REF J. MOL. BIOL. V. 426 3016 2014
JRNL REFN ESSN 1089-8638
JRNL PMID 25020231
JRNL DOI 10.1016/J.JMB.2014.06.020
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.1_1168)
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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 64.28
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 2.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.3
REMARK 3 NUMBER OF REFLECTIONS : 70389
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.203
REMARK 3 R VALUE (WORKING SET) : 0.202
REMARK 3 FREE R VALUE : 0.237
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3520
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 64.3019 - 7.0149 0.98 2693 142 0.1926 0.2477
REMARK 3 2 7.0149 - 5.5689 1.00 2708 143 0.2083 0.2238
REMARK 3 3 5.5689 - 4.8653 0.99 2739 144 0.1682 0.2183
REMARK 3 4 4.8653 - 4.4205 0.99 2735 144 0.1508 0.1733
REMARK 3 5 4.4205 - 4.1038 0.99 2701 142 0.1578 0.1697
REMARK 3 6 4.1038 - 3.8618 0.99 2730 144 0.1742 0.2030
REMARK 3 7 3.8618 - 3.6685 0.99 2740 144 0.1749 0.1924
REMARK 3 8 3.6685 - 3.5088 0.99 2706 143 0.1818 0.2123
REMARK 3 9 3.5088 - 3.3737 0.99 2697 141 0.1761 0.2146
REMARK 3 10 3.3737 - 3.2573 0.98 2713 143 0.1961 0.2231
REMARK 3 11 3.2573 - 3.1555 0.99 2721 144 0.2010 0.2383
REMARK 3 12 3.1555 - 3.0653 0.98 2675 140 0.2065 0.2553
REMARK 3 13 3.0653 - 2.9846 0.98 2736 144 0.2129 0.2684
REMARK 3 14 2.9846 - 2.9117 0.98 2645 140 0.2130 0.2611
REMARK 3 15 2.9117 - 2.8456 0.97 2695 141 0.2161 0.2342
REMARK 3 16 2.8456 - 2.7850 0.97 2629 139 0.2229 0.2740
REMARK 3 17 2.7850 - 2.7293 0.96 2724 143 0.2436 0.3014
REMARK 3 18 2.7293 - 2.6778 0.96 2573 136 0.2562 0.2973
REMARK 3 19 2.6778 - 2.6300 0.94 2639 138 0.2713 0.3353
REMARK 3 20 2.6300 - 2.5854 0.95 2598 136 0.2719 0.2898
REMARK 3 21 2.5854 - 2.5437 0.94 2576 136 0.2709 0.3553
REMARK 3 22 2.5437 - 2.5045 0.95 2621 138 0.2798 0.2815
REMARK 3 23 2.5045 - 2.4677 0.95 2618 138 0.2777 0.3185
REMARK 3 24 2.4677 - 2.4329 0.96 2607 137 0.2943 0.3266
REMARK 3 25 2.4329 - 2.4001 0.95 2650 140 0.2860 0.3279
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) : 0.280
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.930
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 28.06
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.005 12796
REMARK 3 ANGLE : 1.071 17396
REMARK 3 CHIRALITY : 0.064 1848
REMARK 3 PLANARITY : 0.005 2300
REMARK 3 DIHEDRAL : 14.516 4664
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 3WEX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-AUG-13.
REMARK 100 THE DEPOSITION ID IS D_1000096249.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-SEP-11
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 : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS, XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 70445
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 64.280
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.20100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.3100
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.57
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.4
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.700
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: PDB ENTRY 3LQZ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.05
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.51
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 24% (W/V) PEG 3350, 0.2M AMMONIUM
REMARK 280 NITRATE, PH 8.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6260 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18270 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
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: 6160 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18580 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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: 3
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: 6160 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18420 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6300 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18380 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H
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 SER A 182
REMARK 465 GLY A 183
REMARK 465 PRO A 184
REMARK 465 SER A 185
REMARK 465 SER A 186
REMARK 465 GLY A 187
REMARK 465 GLU A 188
REMARK 465 ASN A 189
REMARK 465 LEU A 190
REMARK 465 TYR A 191
REMARK 465 PHE A 192
REMARK 465 GLN A 193
REMARK 465 GLY B -10
REMARK 465 GLY B -9
REMARK 465 SER B -8
REMARK 465 LEU B -7
REMARK 465 VAL B -6
REMARK 465 PRO B -5
REMARK 465 ARG B -4
REMARK 465 GLY B -3
REMARK 465 SER B -2
REMARK 465 GLY B -1
REMARK 465 GLY B 0
REMARK 465 GLY B 1
REMARK 465 GLY B 2
REMARK 465 SER B 3
REMARK 465 SER B 190
REMARK 465 GLY B 191
REMARK 465 PRO B 192
REMARK 465 SER B 193
REMARK 465 SER B 194
REMARK 465 GLY B 195
REMARK 465 GLU B 196
REMARK 465 ASN B 197
REMARK 465 LEU B 198
REMARK 465 TYR B 199
REMARK 465 PHE B 200
REMARK 465 GLN B 201
REMARK 465 SER C 182
REMARK 465 GLY C 183
REMARK 465 PRO C 184
REMARK 465 SER C 185
REMARK 465 SER C 186
REMARK 465 GLY C 187
REMARK 465 GLU C 188
REMARK 465 ASN C 189
REMARK 465 LEU C 190
REMARK 465 TYR C 191
REMARK 465 PHE C 192
REMARK 465 GLN C 193
REMARK 465 GLY D -10
REMARK 465 GLY D -9
REMARK 465 SER D -8
REMARK 465 LEU D -7
REMARK 465 VAL D -6
REMARK 465 PRO D -5
REMARK 465 ARG D -4
REMARK 465 GLY D -3
REMARK 465 SER D -2
REMARK 465 GLY D -1
REMARK 465 GLY D 0
REMARK 465 GLY D 1
REMARK 465 GLY D 2
REMARK 465 SER D 3
REMARK 465 SER D 190
REMARK 465 GLY D 191
REMARK 465 PRO D 192
REMARK 465 SER D 193
REMARK 465 SER D 194
REMARK 465 GLY D 195
REMARK 465 GLU D 196
REMARK 465 ASN D 197
REMARK 465 LEU D 198
REMARK 465 TYR D 199
REMARK 465 PHE D 200
REMARK 465 GLN D 201
REMARK 465 SER E 182
REMARK 465 GLY E 183
REMARK 465 PRO E 184
REMARK 465 SER E 185
REMARK 465 SER E 186
REMARK 465 GLY E 187
REMARK 465 GLU E 188
REMARK 465 ASN E 189
REMARK 465 LEU E 190
REMARK 465 TYR E 191
REMARK 465 PHE E 192
REMARK 465 GLN E 193
REMARK 465 GLY F -10
REMARK 465 GLY F -9
REMARK 465 SER F -8
REMARK 465 LEU F -7
REMARK 465 VAL F -6
REMARK 465 PRO F -5
REMARK 465 ARG F -4
REMARK 465 GLY F -3
REMARK 465 SER F -2
REMARK 465 GLY F -1
REMARK 465 GLY F 0
REMARK 465 GLY F 1
REMARK 465 GLY F 2
REMARK 465 SER F 3
REMARK 465 SER F 190
REMARK 465 GLY F 191
REMARK 465 PRO F 192
REMARK 465 SER F 193
REMARK 465 SER F 194
REMARK 465 GLY F 195
REMARK 465 GLU F 196
REMARK 465 ASN F 197
REMARK 465 LEU F 198
REMARK 465 TYR F 199
REMARK 465 PHE F 200
REMARK 465 GLN F 201
REMARK 465 SER G 182
REMARK 465 GLY G 183
REMARK 465 PRO G 184
REMARK 465 SER G 185
REMARK 465 SER G 186
REMARK 465 GLY G 187
REMARK 465 GLU G 188
REMARK 465 ASN G 189
REMARK 465 LEU G 190
REMARK 465 TYR G 191
REMARK 465 PHE G 192
REMARK 465 GLN G 193
REMARK 465 GLY H -10
REMARK 465 GLY H -9
REMARK 465 SER H -8
REMARK 465 LEU H -7
REMARK 465 VAL H -6
REMARK 465 PRO H -5
REMARK 465 ARG H -4
REMARK 465 GLY H -3
REMARK 465 SER H -2
REMARK 465 GLY H -1
REMARK 465 GLY H 0
REMARK 465 GLY H 1
REMARK 465 GLY H 2
REMARK 465 SER H 3
REMARK 465 SER H 190
REMARK 465 GLY H 191
REMARK 465 PRO H 192
REMARK 465 SER H 193
REMARK 465 SER H 194
REMARK 465 GLY H 195
REMARK 465 GLU H 196
REMARK 465 ASN H 197
REMARK 465 LEU H 198
REMARK 465 TYR H 199
REMARK 465 PHE H 200
REMARK 465 GLN H 201
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 OE2 GLU H 44 NH1 ARG H 46 1.96
REMARK 500 OD1 ASP F 74 NH1 ARG F 78 2.02
REMARK 500 OE1 GLU B 50 NH2 ARG B 53 2.04
REMARK 500 ND2 ASN A 118 C2 NAG A 201 2.10
REMARK 500 ND2 ASN G 118 C2 NAG G 201 2.16
REMARK 500 OE1 GLU F 5 OH TYR F 7 2.16
REMARK 500 NH1 ARG C 164 OE2 GLU C 166 2.17
REMARK 500 NE ARG F 53 OE2 GLU F 57 2.17
REMARK 500 ND2 ASN C 118 C2 NAG C 201 2.18
REMARK 500 OD2 ASP C 162 O HOH C 335 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 NH2 ARG D 128 O ASN F 132 1455 2.01
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 PRO F 106 C - N - CA ANGL. DEV. = 9.7 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 ASN B 19 -121.45 54.40
REMARK 500 ASN B 31 -107.37 55.13
REMARK 500 ARG B 75 -79.90 -100.10
REMARK 500 VAL B 87 -69.66 -126.62
REMARK 500 PRO B 106 -179.46 -63.73
REMARK 500 ASN D 19 -124.40 57.41
REMARK 500 ASN D 31 -106.78 55.14
REMARK 500 ARG D 75 -80.41 -100.90
REMARK 500 VAL D 87 -70.97 -125.92
REMARK 500 PRO D 106 -152.50 -70.95
REMARK 500 ASN D 144 -178.78 72.93
REMARK 500 ASN F 19 -121.80 51.90
REMARK 500 ASN F 31 -108.57 54.20
REMARK 500 ARG F 75 -81.87 -97.80
REMARK 500 VAL F 87 -69.10 -127.13
REMARK 500 LYS F 104 -137.33 -94.52
REMARK 500 GLN F 108 78.74 -100.53
REMARK 500 HIS F 109 -179.71 -171.72
REMARK 500 ASN H 19 -125.97 57.33
REMARK 500 ASN H 31 -107.93 54.52
REMARK 500 ARG H 75 -78.95 -101.37
REMARK 500 VAL H 87 -70.44 -125.83
REMARK 500 GLN H 108 -1.19 75.58
REMARK 500 ASN H 144 -175.65 71.08
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3WEY RELATED DB: PDB
DBREF 3WEX A 1 181 UNP I2G9G1 I2G9G1_HUMAN 32 212
DBREF 3WEX B 6 189 UNP I2FL84 I2FL84_HUMAN 1 184
DBREF 3WEX C 1 181 UNP I2G9G1 I2G9G1_HUMAN 32 212
DBREF 3WEX D 6 189 UNP I2FL84 I2FL84_HUMAN 1 184
DBREF 3WEX E 1 181 UNP I2G9G1 I2G9G1_HUMAN 32 212
DBREF 3WEX F 6 189 UNP I2FL84 I2FL84_HUMAN 1 184
DBREF 3WEX G 1 181 UNP I2G9G1 I2G9G1_HUMAN 32 212
DBREF 3WEX H 6 189 UNP I2FL84 I2FL84_HUMAN 1 184
SEQADV 3WEX SER A 182 UNP I2G9G1 EXPRESSION TAG
SEQADV 3WEX GLY A 183 UNP I2G9G1 EXPRESSION TAG
SEQADV 3WEX PRO A 184 UNP I2G9G1 EXPRESSION TAG
SEQADV 3WEX SER A 185 UNP I2G9G1 EXPRESSION TAG
SEQADV 3WEX SER A 186 UNP I2G9G1 EXPRESSION TAG
SEQADV 3WEX GLY A 187 UNP I2G9G1 EXPRESSION TAG
SEQADV 3WEX GLU A 188 UNP I2G9G1 EXPRESSION TAG
SEQADV 3WEX ASN A 189 UNP I2G9G1 EXPRESSION TAG
SEQADV 3WEX LEU A 190 UNP I2G9G1 EXPRESSION TAG
SEQADV 3WEX TYR A 191 UNP I2G9G1 EXPRESSION TAG
SEQADV 3WEX PHE A 192 UNP I2G9G1 EXPRESSION TAG
SEQADV 3WEX GLN A 193 UNP I2G9G1 EXPRESSION TAG
SEQADV 3WEX LYS B -19 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX VAL B -18 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX THR B -17 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX VAL B -16 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX ALA B -15 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX PHE B -14 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX ASN B -13 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX GLN B -12 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX PHE B -11 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX GLY B -10 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX GLY B -9 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX SER B -8 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX LEU B -7 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX VAL B -6 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX PRO B -5 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX ARG B -4 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX GLY B -3 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX SER B -2 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX GLY B -1 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX GLY B 0 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX GLY B 1 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX GLY B 2 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX SER B 3 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX PRO B 4 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX GLU B 5 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX SER B 190 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX GLY B 191 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX PRO B 192 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX SER B 193 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX SER B 194 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX GLY B 195 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX GLU B 196 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX ASN B 197 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX LEU B 198 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX TYR B 199 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX PHE B 200 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX GLN B 201 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX SER C 182 UNP I2G9G1 EXPRESSION TAG
SEQADV 3WEX GLY C 183 UNP I2G9G1 EXPRESSION TAG
SEQADV 3WEX PRO C 184 UNP I2G9G1 EXPRESSION TAG
SEQADV 3WEX SER C 185 UNP I2G9G1 EXPRESSION TAG
SEQADV 3WEX SER C 186 UNP I2G9G1 EXPRESSION TAG
SEQADV 3WEX GLY C 187 UNP I2G9G1 EXPRESSION TAG
SEQADV 3WEX GLU C 188 UNP I2G9G1 EXPRESSION TAG
SEQADV 3WEX ASN C 189 UNP I2G9G1 EXPRESSION TAG
SEQADV 3WEX LEU C 190 UNP I2G9G1 EXPRESSION TAG
SEQADV 3WEX TYR C 191 UNP I2G9G1 EXPRESSION TAG
SEQADV 3WEX PHE C 192 UNP I2G9G1 EXPRESSION TAG
SEQADV 3WEX GLN C 193 UNP I2G9G1 EXPRESSION TAG
SEQADV 3WEX LYS D -19 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX VAL D -18 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX THR D -17 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX VAL D -16 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX ALA D -15 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX PHE D -14 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX ASN D -13 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX GLN D -12 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX PHE D -11 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX GLY D -10 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX GLY D -9 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX SER D -8 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX LEU D -7 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX VAL D -6 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX PRO D -5 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX ARG D -4 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX GLY D -3 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX SER D -2 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX GLY D -1 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX GLY D 0 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX GLY D 1 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX GLY D 2 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX SER D 3 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX PRO D 4 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX GLU D 5 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX SER D 190 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX GLY D 191 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX PRO D 192 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX SER D 193 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX SER D 194 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX GLY D 195 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX GLU D 196 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX ASN D 197 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX LEU D 198 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX TYR D 199 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX PHE D 200 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX GLN D 201 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX SER E 182 UNP I2G9G1 EXPRESSION TAG
SEQADV 3WEX GLY E 183 UNP I2G9G1 EXPRESSION TAG
SEQADV 3WEX PRO E 184 UNP I2G9G1 EXPRESSION TAG
SEQADV 3WEX SER E 185 UNP I2G9G1 EXPRESSION TAG
SEQADV 3WEX SER E 186 UNP I2G9G1 EXPRESSION TAG
SEQADV 3WEX GLY E 187 UNP I2G9G1 EXPRESSION TAG
SEQADV 3WEX GLU E 188 UNP I2G9G1 EXPRESSION TAG
SEQADV 3WEX ASN E 189 UNP I2G9G1 EXPRESSION TAG
SEQADV 3WEX LEU E 190 UNP I2G9G1 EXPRESSION TAG
SEQADV 3WEX TYR E 191 UNP I2G9G1 EXPRESSION TAG
SEQADV 3WEX PHE E 192 UNP I2G9G1 EXPRESSION TAG
SEQADV 3WEX GLN E 193 UNP I2G9G1 EXPRESSION TAG
SEQADV 3WEX LYS F -19 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX VAL F -18 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX THR F -17 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX VAL F -16 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX ALA F -15 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX PHE F -14 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX ASN F -13 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX GLN F -12 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX PHE F -11 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX GLY F -10 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX GLY F -9 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX SER F -8 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX LEU F -7 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX VAL F -6 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX PRO F -5 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX ARG F -4 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX GLY F -3 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX SER F -2 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX GLY F -1 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX GLY F 0 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX GLY F 1 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX GLY F 2 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX SER F 3 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX PRO F 4 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX GLU F 5 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX SER F 190 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX GLY F 191 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX PRO F 192 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX SER F 193 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX SER F 194 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX GLY F 195 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX GLU F 196 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX ASN F 197 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX LEU F 198 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX TYR F 199 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX PHE F 200 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX GLN F 201 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX SER G 182 UNP I2G9G1 EXPRESSION TAG
SEQADV 3WEX GLY G 183 UNP I2G9G1 EXPRESSION TAG
SEQADV 3WEX PRO G 184 UNP I2G9G1 EXPRESSION TAG
SEQADV 3WEX SER G 185 UNP I2G9G1 EXPRESSION TAG
SEQADV 3WEX SER G 186 UNP I2G9G1 EXPRESSION TAG
SEQADV 3WEX GLY G 187 UNP I2G9G1 EXPRESSION TAG
SEQADV 3WEX GLU G 188 UNP I2G9G1 EXPRESSION TAG
SEQADV 3WEX ASN G 189 UNP I2G9G1 EXPRESSION TAG
SEQADV 3WEX LEU G 190 UNP I2G9G1 EXPRESSION TAG
SEQADV 3WEX TYR G 191 UNP I2G9G1 EXPRESSION TAG
SEQADV 3WEX PHE G 192 UNP I2G9G1 EXPRESSION TAG
SEQADV 3WEX GLN G 193 UNP I2G9G1 EXPRESSION TAG
SEQADV 3WEX LYS H -19 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX VAL H -18 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX THR H -17 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX VAL H -16 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX ALA H -15 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX PHE H -14 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX ASN H -13 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX GLN H -12 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX PHE H -11 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX GLY H -10 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX GLY H -9 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX SER H -8 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX LEU H -7 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX VAL H -6 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX PRO H -5 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX ARG H -4 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX GLY H -3 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX SER H -2 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX GLY H -1 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX GLY H 0 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX GLY H 1 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX GLY H 2 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX SER H 3 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX PRO H 4 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX GLU H 5 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX SER H 190 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX GLY H 191 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX PRO H 192 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX SER H 193 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX SER H 194 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX GLY H 195 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX GLU H 196 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX ASN H 197 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX LEU H 198 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX TYR H 199 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX PHE H 200 UNP I2FL84 EXPRESSION TAG
SEQADV 3WEX GLN H 201 UNP I2FL84 EXPRESSION TAG
SEQRES 1 A 193 ILE LYS ALA ASP HIS VAL SER THR TYR ALA MET PHE VAL
SEQRES 2 A 193 GLN THR HIS ARG PRO THR GLY GLU PHE MET PHE GLU PHE
SEQRES 3 A 193 ASP GLU ASP GLU GLN PHE TYR VAL ASP LEU ASP LYS LYS
SEQRES 4 A 193 GLU THR VAL TRP HIS LEU GLU GLU PHE GLY ARG ALA PHE
SEQRES 5 A 193 SER PHE GLU ALA GLN GLY GLY LEU ALA ASN ILE ALA ILE
SEQRES 6 A 193 LEU ASN ASN ASN LEU ASN THR LEU ILE GLN ARG SER ASN
SEQRES 7 A 193 HIS THR GLN ALA ALA ASN ASP PRO PRO GLU VAL THR VAL
SEQRES 8 A 193 PHE PRO LYS GLU PRO VAL GLU LEU GLY GLN PRO ASN THR
SEQRES 9 A 193 LEU ILE CYS HIS ILE ASP ARG PHE PHE PRO PRO VAL LEU
SEQRES 10 A 193 ASN VAL THR TRP LEU CYS ASN GLY GLU PRO VAL THR GLU
SEQRES 11 A 193 GLY VAL ALA GLU SER LEU PHE LEU PRO ARG THR ASP TYR
SEQRES 12 A 193 SER PHE HIS LYS PHE HIS TYR LEU THR PHE VAL PRO SER
SEQRES 13 A 193 ALA GLU ASP VAL TYR ASP CYS ARG VAL GLU HIS TRP GLY
SEQRES 14 A 193 LEU ASP GLN PRO LEU LEU LYS HIS TRP GLU ALA GLN SER
SEQRES 15 A 193 GLY PRO SER SER GLY GLU ASN LEU TYR PHE GLN
SEQRES 1 B 221 LYS VAL THR VAL ALA PHE ASN GLN PHE GLY GLY SER LEU
SEQRES 2 B 221 VAL PRO ARG GLY SER GLY GLY GLY GLY SER PRO GLU ASN
SEQRES 3 B 221 TYR LEU PHE GLN GLY ARG GLN GLU CYS TYR ALA PHE ASN
SEQRES 4 B 221 GLY THR GLN ARG PHE LEU GLU ARG TYR ILE TYR ASN ARG
SEQRES 5 B 221 GLU GLU LEU VAL ARG PHE ASP SER ASP VAL GLY GLU PHE
SEQRES 6 B 221 ARG ALA VAL THR GLU LEU GLY ARG PRO GLU ALA GLU TYR
SEQRES 7 B 221 TRP ASN SER GLN LYS ASP ILE LEU GLU GLU LYS ARG ALA
SEQRES 8 B 221 VAL PRO ASP ARG MET CYS ARG HIS ASN TYR GLU LEU ASP
SEQRES 9 B 221 GLU ALA VAL THR LEU GLN ARG ARG VAL GLN PRO LYS VAL
SEQRES 10 B 221 ASN VAL SER PRO SER LYS LYS GLY PRO LEU GLN HIS HIS
SEQRES 11 B 221 ASN LEU LEU VAL CYS HIS VAL THR ASP PHE TYR PRO GLY
SEQRES 12 B 221 SER ILE GLN VAL ARG TRP PHE LEU ASN GLY GLN GLU GLU
SEQRES 13 B 221 THR ALA GLY VAL VAL SER THR ASN LEU ILE ARG ASN GLY
SEQRES 14 B 221 ASP TRP THR PHE GLN ILE LEU VAL MET LEU GLU MET THR
SEQRES 15 B 221 PRO GLN GLN GLY ASP VAL TYR ILE CYS GLN VAL GLU HIS
SEQRES 16 B 221 THR SER LEU ASP SER PRO VAL THR VAL GLU TRP LYS ALA
SEQRES 17 B 221 GLN SER GLY PRO SER SER GLY GLU ASN LEU TYR PHE GLN
SEQRES 1 C 193 ILE LYS ALA ASP HIS VAL SER THR TYR ALA MET PHE VAL
SEQRES 2 C 193 GLN THR HIS ARG PRO THR GLY GLU PHE MET PHE GLU PHE
SEQRES 3 C 193 ASP GLU ASP GLU GLN PHE TYR VAL ASP LEU ASP LYS LYS
SEQRES 4 C 193 GLU THR VAL TRP HIS LEU GLU GLU PHE GLY ARG ALA PHE
SEQRES 5 C 193 SER PHE GLU ALA GLN GLY GLY LEU ALA ASN ILE ALA ILE
SEQRES 6 C 193 LEU ASN ASN ASN LEU ASN THR LEU ILE GLN ARG SER ASN
SEQRES 7 C 193 HIS THR GLN ALA ALA ASN ASP PRO PRO GLU VAL THR VAL
SEQRES 8 C 193 PHE PRO LYS GLU PRO VAL GLU LEU GLY GLN PRO ASN THR
SEQRES 9 C 193 LEU ILE CYS HIS ILE ASP ARG PHE PHE PRO PRO VAL LEU
SEQRES 10 C 193 ASN VAL THR TRP LEU CYS ASN GLY GLU PRO VAL THR GLU
SEQRES 11 C 193 GLY VAL ALA GLU SER LEU PHE LEU PRO ARG THR ASP TYR
SEQRES 12 C 193 SER PHE HIS LYS PHE HIS TYR LEU THR PHE VAL PRO SER
SEQRES 13 C 193 ALA GLU ASP VAL TYR ASP CYS ARG VAL GLU HIS TRP GLY
SEQRES 14 C 193 LEU ASP GLN PRO LEU LEU LYS HIS TRP GLU ALA GLN SER
SEQRES 15 C 193 GLY PRO SER SER GLY GLU ASN LEU TYR PHE GLN
SEQRES 1 D 221 LYS VAL THR VAL ALA PHE ASN GLN PHE GLY GLY SER LEU
SEQRES 2 D 221 VAL PRO ARG GLY SER GLY GLY GLY GLY SER PRO GLU ASN
SEQRES 3 D 221 TYR LEU PHE GLN GLY ARG GLN GLU CYS TYR ALA PHE ASN
SEQRES 4 D 221 GLY THR GLN ARG PHE LEU GLU ARG TYR ILE TYR ASN ARG
SEQRES 5 D 221 GLU GLU LEU VAL ARG PHE ASP SER ASP VAL GLY GLU PHE
SEQRES 6 D 221 ARG ALA VAL THR GLU LEU GLY ARG PRO GLU ALA GLU TYR
SEQRES 7 D 221 TRP ASN SER GLN LYS ASP ILE LEU GLU GLU LYS ARG ALA
SEQRES 8 D 221 VAL PRO ASP ARG MET CYS ARG HIS ASN TYR GLU LEU ASP
SEQRES 9 D 221 GLU ALA VAL THR LEU GLN ARG ARG VAL GLN PRO LYS VAL
SEQRES 10 D 221 ASN VAL SER PRO SER LYS LYS GLY PRO LEU GLN HIS HIS
SEQRES 11 D 221 ASN LEU LEU VAL CYS HIS VAL THR ASP PHE TYR PRO GLY
SEQRES 12 D 221 SER ILE GLN VAL ARG TRP PHE LEU ASN GLY GLN GLU GLU
SEQRES 13 D 221 THR ALA GLY VAL VAL SER THR ASN LEU ILE ARG ASN GLY
SEQRES 14 D 221 ASP TRP THR PHE GLN ILE LEU VAL MET LEU GLU MET THR
SEQRES 15 D 221 PRO GLN GLN GLY ASP VAL TYR ILE CYS GLN VAL GLU HIS
SEQRES 16 D 221 THR SER LEU ASP SER PRO VAL THR VAL GLU TRP LYS ALA
SEQRES 17 D 221 GLN SER GLY PRO SER SER GLY GLU ASN LEU TYR PHE GLN
SEQRES 1 E 193 ILE LYS ALA ASP HIS VAL SER THR TYR ALA MET PHE VAL
SEQRES 2 E 193 GLN THR HIS ARG PRO THR GLY GLU PHE MET PHE GLU PHE
SEQRES 3 E 193 ASP GLU ASP GLU GLN PHE TYR VAL ASP LEU ASP LYS LYS
SEQRES 4 E 193 GLU THR VAL TRP HIS LEU GLU GLU PHE GLY ARG ALA PHE
SEQRES 5 E 193 SER PHE GLU ALA GLN GLY GLY LEU ALA ASN ILE ALA ILE
SEQRES 6 E 193 LEU ASN ASN ASN LEU ASN THR LEU ILE GLN ARG SER ASN
SEQRES 7 E 193 HIS THR GLN ALA ALA ASN ASP PRO PRO GLU VAL THR VAL
SEQRES 8 E 193 PHE PRO LYS GLU PRO VAL GLU LEU GLY GLN PRO ASN THR
SEQRES 9 E 193 LEU ILE CYS HIS ILE ASP ARG PHE PHE PRO PRO VAL LEU
SEQRES 10 E 193 ASN VAL THR TRP LEU CYS ASN GLY GLU PRO VAL THR GLU
SEQRES 11 E 193 GLY VAL ALA GLU SER LEU PHE LEU PRO ARG THR ASP TYR
SEQRES 12 E 193 SER PHE HIS LYS PHE HIS TYR LEU THR PHE VAL PRO SER
SEQRES 13 E 193 ALA GLU ASP VAL TYR ASP CYS ARG VAL GLU HIS TRP GLY
SEQRES 14 E 193 LEU ASP GLN PRO LEU LEU LYS HIS TRP GLU ALA GLN SER
SEQRES 15 E 193 GLY PRO SER SER GLY GLU ASN LEU TYR PHE GLN
SEQRES 1 F 221 LYS VAL THR VAL ALA PHE ASN GLN PHE GLY GLY SER LEU
SEQRES 2 F 221 VAL PRO ARG GLY SER GLY GLY GLY GLY SER PRO GLU ASN
SEQRES 3 F 221 TYR LEU PHE GLN GLY ARG GLN GLU CYS TYR ALA PHE ASN
SEQRES 4 F 221 GLY THR GLN ARG PHE LEU GLU ARG TYR ILE TYR ASN ARG
SEQRES 5 F 221 GLU GLU LEU VAL ARG PHE ASP SER ASP VAL GLY GLU PHE
SEQRES 6 F 221 ARG ALA VAL THR GLU LEU GLY ARG PRO GLU ALA GLU TYR
SEQRES 7 F 221 TRP ASN SER GLN LYS ASP ILE LEU GLU GLU LYS ARG ALA
SEQRES 8 F 221 VAL PRO ASP ARG MET CYS ARG HIS ASN TYR GLU LEU ASP
SEQRES 9 F 221 GLU ALA VAL THR LEU GLN ARG ARG VAL GLN PRO LYS VAL
SEQRES 10 F 221 ASN VAL SER PRO SER LYS LYS GLY PRO LEU GLN HIS HIS
SEQRES 11 F 221 ASN LEU LEU VAL CYS HIS VAL THR ASP PHE TYR PRO GLY
SEQRES 12 F 221 SER ILE GLN VAL ARG TRP PHE LEU ASN GLY GLN GLU GLU
SEQRES 13 F 221 THR ALA GLY VAL VAL SER THR ASN LEU ILE ARG ASN GLY
SEQRES 14 F 221 ASP TRP THR PHE GLN ILE LEU VAL MET LEU GLU MET THR
SEQRES 15 F 221 PRO GLN GLN GLY ASP VAL TYR ILE CYS GLN VAL GLU HIS
SEQRES 16 F 221 THR SER LEU ASP SER PRO VAL THR VAL GLU TRP LYS ALA
SEQRES 17 F 221 GLN SER GLY PRO SER SER GLY GLU ASN LEU TYR PHE GLN
SEQRES 1 G 193 ILE LYS ALA ASP HIS VAL SER THR TYR ALA MET PHE VAL
SEQRES 2 G 193 GLN THR HIS ARG PRO THR GLY GLU PHE MET PHE GLU PHE
SEQRES 3 G 193 ASP GLU ASP GLU GLN PHE TYR VAL ASP LEU ASP LYS LYS
SEQRES 4 G 193 GLU THR VAL TRP HIS LEU GLU GLU PHE GLY ARG ALA PHE
SEQRES 5 G 193 SER PHE GLU ALA GLN GLY GLY LEU ALA ASN ILE ALA ILE
SEQRES 6 G 193 LEU ASN ASN ASN LEU ASN THR LEU ILE GLN ARG SER ASN
SEQRES 7 G 193 HIS THR GLN ALA ALA ASN ASP PRO PRO GLU VAL THR VAL
SEQRES 8 G 193 PHE PRO LYS GLU PRO VAL GLU LEU GLY GLN PRO ASN THR
SEQRES 9 G 193 LEU ILE CYS HIS ILE ASP ARG PHE PHE PRO PRO VAL LEU
SEQRES 10 G 193 ASN VAL THR TRP LEU CYS ASN GLY GLU PRO VAL THR GLU
SEQRES 11 G 193 GLY VAL ALA GLU SER LEU PHE LEU PRO ARG THR ASP TYR
SEQRES 12 G 193 SER PHE HIS LYS PHE HIS TYR LEU THR PHE VAL PRO SER
SEQRES 13 G 193 ALA GLU ASP VAL TYR ASP CYS ARG VAL GLU HIS TRP GLY
SEQRES 14 G 193 LEU ASP GLN PRO LEU LEU LYS HIS TRP GLU ALA GLN SER
SEQRES 15 G 193 GLY PRO SER SER GLY GLU ASN LEU TYR PHE GLN
SEQRES 1 H 221 LYS VAL THR VAL ALA PHE ASN GLN PHE GLY GLY SER LEU
SEQRES 2 H 221 VAL PRO ARG GLY SER GLY GLY GLY GLY SER PRO GLU ASN
SEQRES 3 H 221 TYR LEU PHE GLN GLY ARG GLN GLU CYS TYR ALA PHE ASN
SEQRES 4 H 221 GLY THR GLN ARG PHE LEU GLU ARG TYR ILE TYR ASN ARG
SEQRES 5 H 221 GLU GLU LEU VAL ARG PHE ASP SER ASP VAL GLY GLU PHE
SEQRES 6 H 221 ARG ALA VAL THR GLU LEU GLY ARG PRO GLU ALA GLU TYR
SEQRES 7 H 221 TRP ASN SER GLN LYS ASP ILE LEU GLU GLU LYS ARG ALA
SEQRES 8 H 221 VAL PRO ASP ARG MET CYS ARG HIS ASN TYR GLU LEU ASP
SEQRES 9 H 221 GLU ALA VAL THR LEU GLN ARG ARG VAL GLN PRO LYS VAL
SEQRES 10 H 221 ASN VAL SER PRO SER LYS LYS GLY PRO LEU GLN HIS HIS
SEQRES 11 H 221 ASN LEU LEU VAL CYS HIS VAL THR ASP PHE TYR PRO GLY
SEQRES 12 H 221 SER ILE GLN VAL ARG TRP PHE LEU ASN GLY GLN GLU GLU
SEQRES 13 H 221 THR ALA GLY VAL VAL SER THR ASN LEU ILE ARG ASN GLY
SEQRES 14 H 221 ASP TRP THR PHE GLN ILE LEU VAL MET LEU GLU MET THR
SEQRES 15 H 221 PRO GLN GLN GLY ASP VAL TYR ILE CYS GLN VAL GLU HIS
SEQRES 16 H 221 THR SER LEU ASP SER PRO VAL THR VAL GLU TRP LYS ALA
SEQRES 17 H 221 GLN SER GLY PRO SER SER GLY GLU ASN LEU TYR PHE GLN
MODRES 3WEX ASN G 118 ASN GLYCOSYLATION SITE
MODRES 3WEX ASN A 118 ASN GLYCOSYLATION SITE
MODRES 3WEX ASN E 118 ASN GLYCOSYLATION SITE
MODRES 3WEX ASN C 118 ASN GLYCOSYLATION SITE
HET NAG A 201 14
HET NAG C 201 14
HET NAG E 201 14
HET NAG G 201 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
FORMUL 9 NAG 4(C8 H15 N O6)
FORMUL 13 HOH *267(H2 O)
HELIX 1 1 LEU A 45 PHE A 52 1 8
HELIX 2 2 ALA A 56 SER A 77 1 22
HELIX 3 3 THR B 49 LEU B 51 5 3
HELIX 4 4 GLY B 52 ASN B 60 1 9
HELIX 5 5 GLN B 62 ALA B 71 1 10
HELIX 6 6 ARG B 75 VAL B 87 1 13
HELIX 7 7 THR B 88 ARG B 91 5 4
HELIX 8 8 LEU C 45 PHE C 52 1 8
HELIX 9 9 ALA C 56 SER C 77 1 22
HELIX 10 10 THR D 49 LEU D 51 5 3
HELIX 11 11 GLY D 52 ASN D 60 1 9
HELIX 12 12 GLN D 62 ALA D 71 1 10
HELIX 13 13 ARG D 75 VAL D 87 1 13
HELIX 14 14 THR D 88 ARG D 91 5 4
HELIX 15 15 LEU E 45 PHE E 52 1 8
HELIX 16 16 GLU E 55 SER E 77 1 23
HELIX 17 17 THR F 49 LEU F 51 5 3
HELIX 18 18 GLY F 52 ASN F 60 1 9
HELIX 19 19 GLN F 62 ALA F 71 1 10
HELIX 20 20 ARG F 75 VAL F 87 1 13
HELIX 21 21 THR F 88 ARG F 91 5 4
HELIX 22 22 LEU G 45 PHE G 52 1 8
HELIX 23 23 ALA G 56 SER G 77 1 22
HELIX 24 24 THR H 49 LEU H 51 5 3
HELIX 25 25 GLY H 52 ASN H 60 1 9
HELIX 26 26 GLN H 62 ALA H 71 1 10
HELIX 27 27 ARG H 75 VAL H 87 1 13
HELIX 28 28 THR H 88 ARG H 91 5 4
SHEET 1 A 8 GLU A 40 TRP A 43 0
SHEET 2 A 8 ASP A 29 ASP A 35 -1 N TYR A 33 O VAL A 42
SHEET 3 A 8 GLY A 20 PHE A 26 -1 N PHE A 24 O PHE A 32
SHEET 4 A 8 HIS A 5 GLN A 14 -1 N THR A 8 O GLU A 25
SHEET 5 A 8 LEU B 8 PHE B 18 -1 O CYS B 15 N SER A 7
SHEET 6 A 8 THR B 21 TYR B 30 -1 O ILE B 29 N GLN B 10
SHEET 7 A 8 GLU B 33 ASP B 39 -1 O LEU B 35 N TYR B 28
SHEET 8 A 8 PHE B 45 ALA B 47 -1 O ARG B 46 N ARG B 37
SHEET 1 B 4 GLU A 88 PRO A 93 0
SHEET 2 B 4 ASN A 103 PHE A 112 -1 O ASP A 110 N GLU A 88
SHEET 3 B 4 PHE A 145 PHE A 153 -1 O LEU A 151 N LEU A 105
SHEET 4 B 4 VAL A 132 GLU A 134 -1 N ALA A 133 O TYR A 150
SHEET 1 C 4 GLU A 88 PRO A 93 0
SHEET 2 C 4 ASN A 103 PHE A 112 -1 O ASP A 110 N GLU A 88
SHEET 3 C 4 PHE A 145 PHE A 153 -1 O LEU A 151 N LEU A 105
SHEET 4 C 4 LEU A 138 PRO A 139 -1 N LEU A 138 O HIS A 146
SHEET 1 D 4 GLU A 126 PRO A 127 0
SHEET 2 D 4 ASN A 118 CYS A 123 -1 N CYS A 123 O GLU A 126
SHEET 3 D 4 VAL A 160 GLU A 166 -1 O ARG A 164 N THR A 120
SHEET 4 D 4 LEU A 174 GLU A 179 -1 O LEU A 174 N VAL A 165
SHEET 1 E 4 LYS B 96 PRO B 101 0
SHEET 2 E 4 ASN B 111 PHE B 120 -1 O HIS B 116 N ASN B 98
SHEET 3 E 4 PHE B 153 MET B 161 -1 O ILE B 155 N VAL B 117
SHEET 4 E 4 VAL B 140 SER B 142 -1 N VAL B 141 O MET B 158
SHEET 1 F 4 LYS B 96 PRO B 101 0
SHEET 2 F 4 ASN B 111 PHE B 120 -1 O HIS B 116 N ASN B 98
SHEET 3 F 4 PHE B 153 MET B 161 -1 O ILE B 155 N VAL B 117
SHEET 4 F 4 ILE B 146 ARG B 147 -1 N ILE B 146 O GLN B 154
SHEET 1 G 4 GLN B 134 GLU B 135 0
SHEET 2 G 4 GLN B 126 LEU B 131 -1 N LEU B 131 O GLN B 134
SHEET 3 G 4 VAL B 168 GLU B 174 -1 O GLN B 172 N ARG B 128
SHEET 4 G 4 VAL B 182 LYS B 187 -1 O VAL B 182 N VAL B 173
SHEET 1 H 8 GLU C 40 TRP C 43 0
SHEET 2 H 8 ASP C 29 ASP C 35 -1 N ASP C 35 O GLU C 40
SHEET 3 H 8 GLY C 20 PHE C 26 -1 N PHE C 24 O GLN C 31
SHEET 4 H 8 HIS C 5 GLN C 14 -1 N THR C 8 O GLU C 25
SHEET 5 H 8 LEU D 8 PHE D 18 -1 O CYS D 15 N SER C 7
SHEET 6 H 8 THR D 21 TYR D 30 -1 O LEU D 25 N GLU D 14
SHEET 7 H 8 GLU D 33 ASP D 39 -1 O LEU D 35 N TYR D 28
SHEET 8 H 8 PHE D 45 ALA D 47 -1 O ARG D 46 N ARG D 37
SHEET 1 I 4 GLU C 88 PRO C 93 0
SHEET 2 I 4 ASN C 103 PHE C 112 -1 O HIS C 108 N THR C 90
SHEET 3 I 4 PHE C 145 PHE C 153 -1 O LEU C 151 N LEU C 105
SHEET 4 I 4 VAL C 132 GLU C 134 -1 N ALA C 133 O TYR C 150
SHEET 1 J 4 GLU C 88 PRO C 93 0
SHEET 2 J 4 ASN C 103 PHE C 112 -1 O HIS C 108 N THR C 90
SHEET 3 J 4 PHE C 145 PHE C 153 -1 O LEU C 151 N LEU C 105
SHEET 4 J 4 LEU C 138 PRO C 139 -1 N LEU C 138 O HIS C 146
SHEET 1 K 4 GLU C 126 VAL C 128 0
SHEET 2 K 4 ASN C 118 CYS C 123 -1 N CYS C 123 O GLU C 126
SHEET 3 K 4 TYR C 161 GLU C 166 -1 O ARG C 164 N THR C 120
SHEET 4 K 4 LEU C 174 TRP C 178 -1 O LEU C 174 N VAL C 165
SHEET 1 L 4 LYS D 96 PRO D 101 0
SHEET 2 L 4 ASN D 111 PHE D 120 -1 O HIS D 116 N ASN D 98
SHEET 3 L 4 PHE D 153 MET D 161 -1 O ILE D 155 N VAL D 117
SHEET 4 L 4 VAL D 140 SER D 142 -1 N VAL D 141 O MET D 158
SHEET 1 M 4 LYS D 96 PRO D 101 0
SHEET 2 M 4 ASN D 111 PHE D 120 -1 O HIS D 116 N ASN D 98
SHEET 3 M 4 PHE D 153 MET D 161 -1 O ILE D 155 N VAL D 117
SHEET 4 M 4 ILE D 146 ARG D 147 -1 N ILE D 146 O GLN D 154
SHEET 1 N 4 GLN D 134 GLU D 135 0
SHEET 2 N 4 GLN D 126 LEU D 131 -1 N LEU D 131 O GLN D 134
SHEET 3 N 4 VAL D 168 GLU D 174 -1 O GLN D 172 N ARG D 128
SHEET 4 N 4 VAL D 182 LYS D 187 -1 O VAL D 182 N VAL D 173
SHEET 1 O 8 GLU E 40 TRP E 43 0
SHEET 2 O 8 ASP E 29 ASP E 35 -1 N TYR E 33 O VAL E 42
SHEET 3 O 8 GLY E 20 PHE E 26 -1 N PHE E 24 O GLN E 31
SHEET 4 O 8 HIS E 5 GLN E 14 -1 N THR E 8 O GLU E 25
SHEET 5 O 8 LEU F 8 PHE F 18 -1 O CYS F 15 N SER E 7
SHEET 6 O 8 THR F 21 TYR F 30 -1 O ILE F 29 N GLN F 10
SHEET 7 O 8 GLU F 33 ASP F 39 -1 O LEU F 35 N TYR F 28
SHEET 8 O 8 PHE F 45 ALA F 47 -1 O ARG F 46 N ARG F 37
SHEET 1 P 4 GLU E 88 PRO E 93 0
SHEET 2 P 4 ASN E 103 PHE E 112 -1 O HIS E 108 N THR E 90
SHEET 3 P 4 PHE E 145 PHE E 153 -1 O LEU E 151 N LEU E 105
SHEET 4 P 4 VAL E 132 GLU E 134 -1 N ALA E 133 O TYR E 150
SHEET 1 Q 4 GLU E 88 PRO E 93 0
SHEET 2 Q 4 ASN E 103 PHE E 112 -1 O HIS E 108 N THR E 90
SHEET 3 Q 4 PHE E 145 PHE E 153 -1 O LEU E 151 N LEU E 105
SHEET 4 Q 4 LEU E 138 PRO E 139 -1 N LEU E 138 O HIS E 146
SHEET 1 R 4 GLU E 126 PRO E 127 0
SHEET 2 R 4 ASN E 118 CYS E 123 -1 N CYS E 123 O GLU E 126
SHEET 3 R 4 TYR E 161 GLU E 166 -1 O ARG E 164 N THR E 120
SHEET 4 R 4 LEU E 174 TRP E 178 -1 O LEU E 174 N VAL E 165
SHEET 1 S 4 LYS F 96 PRO F 101 0
SHEET 2 S 4 ASN F 111 PHE F 120 -1 O VAL F 114 N SER F 100
SHEET 3 S 4 PHE F 153 MET F 161 -1 O MET F 161 N ASN F 111
SHEET 4 S 4 VAL F 140 SER F 142 -1 N VAL F 141 O MET F 158
SHEET 1 T 4 LYS F 96 PRO F 101 0
SHEET 2 T 4 ASN F 111 PHE F 120 -1 O VAL F 114 N SER F 100
SHEET 3 T 4 PHE F 153 MET F 161 -1 O MET F 161 N ASN F 111
SHEET 4 T 4 ILE F 146 ARG F 147 -1 N ILE F 146 O GLN F 154
SHEET 1 U 4 GLN F 134 GLU F 135 0
SHEET 2 U 4 GLN F 126 LEU F 131 -1 N LEU F 131 O GLN F 134
SHEET 3 U 4 VAL F 168 GLU F 174 -1 O GLN F 172 N ARG F 128
SHEET 4 U 4 VAL F 182 LYS F 187 -1 O TRP F 186 N TYR F 169
SHEET 1 V 8 GLU G 40 TRP G 43 0
SHEET 2 V 8 ASP G 29 ASP G 35 -1 N TYR G 33 O VAL G 42
SHEET 3 V 8 GLY G 20 PHE G 26 -1 N PHE G 24 O GLN G 31
SHEET 4 V 8 HIS G 5 GLN G 14 -1 N THR G 8 O GLU G 25
SHEET 5 V 8 LEU H 8 PHE H 18 -1 O CYS H 15 N SER G 7
SHEET 6 V 8 THR H 21 TYR H 30 -1 O ILE H 29 N GLN H 10
SHEET 7 V 8 GLU H 33 ASP H 39 -1 O LEU H 35 N TYR H 28
SHEET 8 V 8 PHE H 45 ALA H 47 -1 O ARG H 46 N ARG H 37
SHEET 1 W 4 GLU G 88 PRO G 93 0
SHEET 2 W 4 ASN G 103 PHE G 112 -1 O ASP G 110 N GLU G 88
SHEET 3 W 4 PHE G 145 PHE G 153 -1 O LEU G 151 N LEU G 105
SHEET 4 W 4 VAL G 132 GLU G 134 -1 N ALA G 133 O TYR G 150
SHEET 1 X 4 GLU G 88 PRO G 93 0
SHEET 2 X 4 ASN G 103 PHE G 112 -1 O ASP G 110 N GLU G 88
SHEET 3 X 4 PHE G 145 PHE G 153 -1 O LEU G 151 N LEU G 105
SHEET 4 X 4 LEU G 138 PRO G 139 -1 N LEU G 138 O HIS G 146
SHEET 1 Y 4 GLU G 126 VAL G 128 0
SHEET 2 Y 4 ASN G 118 CYS G 123 -1 N CYS G 123 O GLU G 126
SHEET 3 Y 4 TYR G 161 GLU G 166 -1 O ARG G 164 N THR G 120
SHEET 4 Y 4 LEU G 174 TRP G 178 -1 O LEU G 174 N VAL G 165
SHEET 1 Z 4 LYS H 96 PRO H 101 0
SHEET 2 Z 4 ASN H 111 PHE H 120 -1 O HIS H 116 N ASN H 98
SHEET 3 Z 4 PHE H 153 MET H 161 -1 O ILE H 155 N VAL H 117
SHEET 4 Z 4 VAL H 140 SER H 142 -1 N VAL H 141 O MET H 158
SHEET 1 AA 4 LYS H 96 PRO H 101 0
SHEET 2 AA 4 ASN H 111 PHE H 120 -1 O HIS H 116 N ASN H 98
SHEET 3 AA 4 PHE H 153 MET H 161 -1 O ILE H 155 N VAL H 117
SHEET 4 AA 4 ILE H 146 ARG H 147 -1 N ILE H 146 O GLN H 154
SHEET 1 AB 4 GLN H 134 GLU H 136 0
SHEET 2 AB 4 GLN H 126 LEU H 131 -1 N TRP H 129 O GLU H 136
SHEET 3 AB 4 VAL H 168 GLU H 174 -1 O ILE H 170 N PHE H 130
SHEET 4 AB 4 VAL H 182 LYS H 187 -1 O TRP H 186 N TYR H 169
SSBOND 1 CYS A 107 CYS A 163 1555 1555 2.04
SSBOND 2 CYS B 15 CYS B 77 1555 1555 2.03
SSBOND 3 CYS B 115 CYS B 171 1555 1555 2.02
SSBOND 4 CYS C 107 CYS C 163 1555 1555 2.04
SSBOND 5 CYS D 15 CYS D 77 1555 1555 2.04
SSBOND 6 CYS D 115 CYS D 171 1555 1555 2.03
SSBOND 7 CYS E 107 CYS E 163 1555 1555 2.04
SSBOND 8 CYS F 15 CYS F 77 1555 1555 2.03
SSBOND 9 CYS F 115 CYS F 171 1555 1555 2.03
SSBOND 10 CYS G 107 CYS G 163 1555 1555 2.04
SSBOND 11 CYS H 15 CYS H 77 1555 1555 2.03
SSBOND 12 CYS H 115 CYS H 171 1555 1555 2.03
LINK ND2 ASN A 118 C1 NAG A 201 1555 1555 1.44
LINK ND2 ASN C 118 C1 NAG C 201 1555 1555 1.44
LINK ND2 ASN E 118 C1 NAG E 201 1555 1555 1.44
LINK ND2 ASN G 118 C1 NAG G 201 1555 1555 1.44
CISPEP 1 ARG A 17 PRO A 18 0 -0.35
CISPEP 2 PHE A 113 PRO A 114 0 1.69
CISPEP 3 TYR B 121 PRO B 122 0 -0.29
CISPEP 4 ARG C 17 PRO C 18 0 0.82
CISPEP 5 PHE C 113 PRO C 114 0 0.70
CISPEP 6 TYR D 121 PRO D 122 0 1.21
CISPEP 7 ARG E 17 PRO E 18 0 1.50
CISPEP 8 PHE E 113 PRO E 114 0 1.32
CISPEP 9 PRO F 106 LEU F 107 0 11.83
CISPEP 10 TYR F 121 PRO F 122 0 1.35
CISPEP 11 GLN F 165 GLY F 166 0 11.85
CISPEP 12 ARG G 17 PRO G 18 0 -0.66
CISPEP 13 PHE G 113 PRO G 114 0 1.55
CISPEP 14 TYR H 121 PRO H 122 0 0.72
CRYST1 61.150 64.370 130.360 92.99 97.53 109.41 P 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 0.016353 0.005762 0.002766 0.00000
SCALE2 0.000000 0.016471 0.001694 0.00000
SCALE3 0.000000 0.000000 0.007779 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
