HEADER TRANSFERASE 30-MAY-08 3DAR
TITLE CRYSTAL STRUCTURE OF D2 DOMAIN FROM HUMAN FGFR2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FIBROBLAST GROWTH FACTOR RECEPTOR 2;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: D2 DOMAIN, IG-LIKE C2-TYPE 2, UNP RESIDUES 146-249;
COMPND 5 SYNONYM: FGFR-2, KERATINOCYTE GROWTH FACTOR RECEPTOR 2, CD332
COMPND 6 ANTIGEN;
COMPND 7 EC: 2.7.10.1;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: FGFR2, BEK, KGFR, KSAM;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA2;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PBAT4
KEYWDS IMMUNOGLOBULIN FOLD, ATP-BINDING, CRANIOSYNOSTOSIS, DISEASE MUTATION,
KEYWDS 2 ECTODERMAL DYSPLASIA, GLYCOPROTEIN, HEPARIN-BINDING, IMMUNOGLOBULIN
KEYWDS 3 DOMAIN, KINASE, LACRIMO-AURICULO-DENTO-DIGITAL SYNDROME, MEMBRANE,
KEYWDS 4 NUCLEOTIDE-BINDING, PHOSPHOPROTEIN, RECEPTOR, SECRETED, TRANSFERASE,
KEYWDS 5 TRANSMEMBRANE, TYROSINE-PROTEIN KINASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.BROWN,T.L.BLUNDELL
REVDAT 5 30-AUG-23 3DAR 1 SEQADV
REVDAT 4 10-SEP-14 3DAR 1 VERSN MTRIX1 MTRIX2 MTRIX3
REVDAT 3 12-MAY-09 3DAR 1 MTRIX1 MTRIX2 MTRIX3
REVDAT 2 24-FEB-09 3DAR 1 VERSN
REVDAT 1 10-JUN-08 3DAR 0
JRNL AUTH A.BROWN,T.L.BLUNDELL
JRNL TITL CRYSTAL STRUCTURE OF THE FGFR2 D2 DOMAIN
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
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 : MLHL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.92
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.3
REMARK 3 NUMBER OF REFLECTIONS : 13756
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.219
REMARK 3 R VALUE (WORKING SET) : 0.212
REMARK 3 FREE R VALUE : 0.255
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.060
REMARK 3 FREE R VALUE TEST SET COUNT : 696
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 33.9210 - 6.5030 0.92 598 0 0.2150 0.0000
REMARK 3 2 6.5030 - 5.1670 0.93 562 0 0.1900 0.0000
REMARK 3 3 5.1670 - 4.5160 0.92 551 0 0.1610 0.0000
REMARK 3 4 4.5160 - 4.1040 0.94 540 0 0.1610 0.0000
REMARK 3 5 4.1040 - 3.8100 0.91 534 0 0.1720 0.0000
REMARK 3 6 3.8100 - 3.5860 0.94 549 0 0.1680 0.0000
REMARK 3 7 3.5860 - 3.4060 0.94 542 0 0.1830 0.0000
REMARK 3 8 3.4060 - 3.2580 0.93 533 0 0.1970 0.0000
REMARK 3 9 3.2580 - 3.1330 0.92 530 0 0.2270 0.0000
REMARK 3 10 3.1330 - 3.0250 0.92 523 0 0.2380 0.0000
REMARK 3 11 3.0250 - 2.9300 0.91 521 0 0.1960 0.0000
REMARK 3 12 2.9300 - 2.8460 0.86 489 0 0.2090 0.0000
REMARK 3 13 2.8460 - 2.7720 0.90 500 0 0.2180 0.0000
REMARK 3 14 2.7720 - 2.7040 0.90 515 0 0.2280 0.0000
REMARK 3 15 2.7040 - 2.6430 0.88 494 0 0.2510 0.0000
REMARK 3 16 2.6430 - 2.5860 0.86 483 0 0.2200 0.0000
REMARK 3 17 2.5860 - 2.5350 0.86 489 0 0.2250 0.0000
REMARK 3 18 2.5350 - 2.4870 0.83 469 0 0.2320 0.0000
REMARK 3 19 2.4870 - 2.4420 0.82 455 0 0.2470 0.0000
REMARK 3 20 2.4420 - 2.4010 0.85 481 0 0.2380 0.0000
REMARK 3 21 2.4010 - 2.3620 0.84 479 0 0.2570 0.0000
REMARK 3 22 2.3620 - 2.3260 0.81 431 0 0.2530 0.0000
REMARK 3 23 2.3260 - 2.2920 0.80 461 0 0.2640 0.0000
REMARK 3 24 2.2920 - 2.2600 0.78 452 0 0.2550 0.0000
REMARK 3 25 2.2600 - 2.2290 0.82 448 0 0.2620 0.0000
REMARK 3 26 2.2290 - 2.2000 0.80 431 0 0.2820 0.0000
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : NULL
REMARK 3 SHRINKAGE RADIUS : NULL
REMARK 3 K_SOL : 0.35
REMARK 3 B_SOL : 58.25
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 44.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.91
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -10.24700
REMARK 3 B22 (A**2) : 8.64300
REMARK 3 B33 (A**2) : 1.60400
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
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 NULL
REMARK 3 ANGLE : 1.149 NULL
REMARK 3 CHIRALITY : 0.082 NULL
REMARK 3 PLANARITY : 0.005 NULL
REMARK 3 DIHEDRAL : 14.438 NULL
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 : 1
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: B
REMARK 3 SELECTION : A
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3DAR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-JUN-08.
REMARK 100 THE DEPOSITION ID IS D_1000047804.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-MAY-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9763
REMARK 200 MONOCHROMATOR : SI(311) MONOCHROMATOR
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.2.25
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14667
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 85.900
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 200 DATA REDUNDANCY : 7.300
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : 0.08000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.32
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.1
REMARK 200 DATA REDUNDANCY IN SHELL : 7.40
REMARK 200 R MERGE FOR SHELL (I) : 0.62300
REMARK 200 R SYM FOR SHELL (I) : 0.62300
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.200
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: PBD ENTRY 1E0O, CHAIN B, RESIDUES 149-249
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.89
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M SODIUM ACETATE, 0.1 M TRIS-HCL,
REMARK 280 30% PEG 4000, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291.0K,
REMARK 280 PH 8.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 2 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 X,-Y,-Z
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 -X,-Y+1/2,Z+1/2
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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.12000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 42.95000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 39.12000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 42.95000
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 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 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 MET A 145
REMARK 465 GLU A 146
REMARK 465 ASN A 147
REMARK 465 SER A 148
REMARK 465 ASN A 149
REMARK 465 ASN A 150
REMARK 465 MET B 145
REMARK 465 GLU B 146
REMARK 465 ASN B 147
REMARK 465 SER B 148
REMARK 465 ASN B 149
REMARK 465 ASN B 150
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 LYS A 161 CE NZ
REMARK 470 GLU A 163 CD OE1 OE2
REMARK 470 ARG A 178 CZ NH1 NH2
REMARK 470 LYS A 196 CE NZ
REMARK 470 LYS A 199 CE NZ
REMARK 470 LYS A 208 CD CE NZ
REMARK 470 ARG A 210 CD NE CZ NH1 NH2
REMARK 470 GLN A 212 CG CD OE1 NE2
REMARK 470 LYS A 226 CG CD CE NZ
REMARK 470 GLU B 160 CG CD OE1 OE2
REMARK 470 LYS B 161 CD CE NZ
REMARK 470 GLU B 163 CG CD OE1 OE2
REMARK 470 LYS B 164 CE NZ
REMARK 470 LYS B 176 NZ
REMARK 470 ARG B 178 CZ NH1 NH2
REMARK 470 LYS B 196 CE NZ
REMARK 470 LYS B 208 CD CE NZ
REMARK 470 ARG B 210 CG CD NE CZ NH1 NH2
REMARK 470 GLN B 212 CG CD OE1 NE2
REMARK 470 LYS B 226 CD CE NZ
REMARK 470 GLU B 234 CG CD OE1 OE2
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 THR A 157 O THR A 157 2554 1.81
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 ALA A 171 151.92 -46.31
REMARK 500 ALA A 172 -14.61 80.32
REMARK 500 ASN B 158 83.29 -153.65
REMARK 500 ALA B 171 152.95 -47.51
REMARK 500 ALA B 172 -13.96 78.84
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1E0O RELATED DB: PDB
REMARK 900 FGF1-FGFR2-HEPARIN COMPLEX
REMARK 900 RELATED ID: 1WVZ RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF THE SAME DOMAIN
DBREF 3DAR A 146 249 UNP P21802 FGFR2_HUMAN 146 249
DBREF 3DAR B 146 249 UNP P21802 FGFR2_HUMAN 146 249
SEQADV 3DAR MET A 145 UNP P21802 INITIATING METHIONINE
SEQADV 3DAR MET B 145 UNP P21802 INITIATING METHIONINE
SEQRES 1 A 105 MET GLU ASN SER ASN ASN LYS ARG ALA PRO TYR TRP THR
SEQRES 2 A 105 ASN THR GLU LYS MET GLU LYS ARG LEU HIS ALA VAL PRO
SEQRES 3 A 105 ALA ALA ASN THR VAL LYS PHE ARG CYS PRO ALA GLY GLY
SEQRES 4 A 105 ASN PRO MET PRO THR MET ARG TRP LEU LYS ASN GLY LYS
SEQRES 5 A 105 GLU PHE LYS GLN GLU HIS ARG ILE GLY GLY TYR LYS VAL
SEQRES 6 A 105 ARG ASN GLN HIS TRP SER LEU ILE MET GLU SER VAL VAL
SEQRES 7 A 105 PRO SER ASP LYS GLY ASN TYR THR CYS VAL VAL GLU ASN
SEQRES 8 A 105 GLU TYR GLY SER ILE ASN HIS THR TYR HIS LEU ASP VAL
SEQRES 9 A 105 VAL
SEQRES 1 B 105 MET GLU ASN SER ASN ASN LYS ARG ALA PRO TYR TRP THR
SEQRES 2 B 105 ASN THR GLU LYS MET GLU LYS ARG LEU HIS ALA VAL PRO
SEQRES 3 B 105 ALA ALA ASN THR VAL LYS PHE ARG CYS PRO ALA GLY GLY
SEQRES 4 B 105 ASN PRO MET PRO THR MET ARG TRP LEU LYS ASN GLY LYS
SEQRES 5 B 105 GLU PHE LYS GLN GLU HIS ARG ILE GLY GLY TYR LYS VAL
SEQRES 6 B 105 ARG ASN GLN HIS TRP SER LEU ILE MET GLU SER VAL VAL
SEQRES 7 B 105 PRO SER ASP LYS GLY ASN TYR THR CYS VAL VAL GLU ASN
SEQRES 8 B 105 GLU TYR GLY SER ILE ASN HIS THR TYR HIS LEU ASP VAL
SEQRES 9 B 105 VAL
FORMUL 3 HOH *122(H2 O)
HELIX 1 1 LYS A 199 ARG A 203 5 5
HELIX 2 2 ASN A 211 HIS A 213 5 3
HELIX 3 3 VAL A 222 LYS A 226 5 5
HELIX 4 4 LYS B 199 ARG B 203 5 5
HELIX 5 5 ASN B 211 HIS B 213 5 3
HELIX 6 6 VAL B 222 LYS B 226 5 5
SHEET 1 A 2 ARG A 152 TRP A 156 0
SHEET 2 A 2 ALA A 181 ASN A 184 -1 O ASN A 184 N ARG A 152
SHEET 1 B 4 LEU A 166 PRO A 170 0
SHEET 2 B 4 GLY A 238 VAL A 249 1 O ASP A 247 N HIS A 167
SHEET 3 B 4 GLY B 238 VAL B 249 -1 O SER B 239 N SER A 239
SHEET 4 B 4 LEU B 166 PRO B 170 1 N HIS B 167 O ASP B 247
SHEET 1 C 8 LYS A 196 GLU A 197 0
SHEET 2 C 8 THR A 188 LYS A 193 -1 N LYS A 193 O LYS A 196
SHEET 3 C 8 GLY A 227 ASN A 235 -1 O VAL A 232 N ARG A 190
SHEET 4 C 8 GLY A 238 VAL A 249 -1 O TYR A 244 N TYR A 229
SHEET 5 C 8 GLY B 238 VAL B 249 -1 O SER B 239 N SER A 239
SHEET 6 C 8 GLY B 227 ASN B 235 -1 N TYR B 229 O TYR B 244
SHEET 7 C 8 THR B 188 LYS B 193 -1 N ARG B 190 O VAL B 232
SHEET 8 C 8 LYS B 196 GLU B 197 -1 O LYS B 196 N LYS B 193
SHEET 1 D 3 VAL A 175 ARG A 178 0
SHEET 2 D 3 SER A 215 MET A 218 -1 O MET A 218 N VAL A 175
SHEET 3 D 3 LYS A 208 ARG A 210 -1 N LYS A 208 O ILE A 217
SHEET 1 E 2 ARG B 152 TRP B 156 0
SHEET 2 E 2 ALA B 181 ASN B 184 -1 O ASN B 184 N ARG B 152
SHEET 1 F 3 VAL B 175 ARG B 178 0
SHEET 2 F 3 SER B 215 MET B 218 -1 O MET B 218 N VAL B 175
SHEET 3 F 3 LYS B 208 ARG B 210 -1 N LYS B 208 O ILE B 217
SSBOND 1 CYS A 179 CYS A 231 1555 1555 2.04
SSBOND 2 CYS B 179 CYS B 231 1555 1555 2.05
CISPEP 1 ASN A 184 PRO A 185 0 3.52
CISPEP 2 ASN B 184 PRO B 185 0 4.64
CRYST1 41.870 78.240 85.900 90.00 90.00 90.00 P 2 21 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.023883 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012781 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011641 0.00000
MTRIX1 1 1.000000 0.000000 0.000000 0.00000 1
MTRIX2 1 0.000000 1.000000 0.000000 0.00000 1
MTRIX3 1 0.000000 0.000000 1.000000 0.00000 1
MTRIX1 2 -0.999991 0.000375 -0.004142 20.79990 1
MTRIX2 2 -0.000457 -0.999800 0.019971 9.90785 1
MTRIX3 2 -0.004133 0.019973 0.999792 0.16898 1
(ATOM LINES ARE NOT SHOWN.)
END
