HEADER TRANSFERASE/HORMONE 15-APR-08 3CU1
TITLE CRYSTAL STRUCTURE OF 2:2:2 FGFR2D2:FGF1:SOS COMPLEX
CAVEAT 3CU1 GLU D 91 HAS WRONG CHIRALITY AT ATOM CA ASN D 92 HAS WRONG
CAVEAT 2 3CU1 CHIRALITY AT ATOM CA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FIBROBLAST GROWTH FACTOR RECEPTOR 2;
COMPND 3 CHAIN: A, C;
COMPND 4 FRAGMENT: IG-LIKE C2-TYPE 2 DOMAIN, UNP RESIDUES 150-249;
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;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: HEPARIN-BINDING GROWTH FACTOR 1;
COMPND 11 CHAIN: B, D;
COMPND 12 FRAGMENT: UNP RESIDUES 22-152;
COMPND 13 SYNONYM: HBGF-1, ACIDIC FIBROBLAST GROWTH FACTOR, AFGF, BETA-
COMPND 14 ENDOTHELIAL CELL GROWTH FACTOR, ECGF- BETA;
COMPND 15 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 GENE: FGFR2, BEK, KGFR, KSAM;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 9 ORGANISM_COMMON: HUMAN;
SOURCE 10 GENE: FGF1, FGFA;
SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 12 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS FIBROBLAST GROWTH FACTOR 1, FIBROBLAST GROWTH FACTOR RECEPTOR 2, D2
KEYWDS 2 DOMAIN, SUCROSE OCTA SULFATE, ALTERNATIVE SPLICING, ATP-BINDING,
KEYWDS 3 DISEASE MUTATION, ECTODERMAL DYSPLASIA, GLYCOPROTEIN, HEPARIN-
KEYWDS 4 BINDING, IMMUNOGLOBULIN DOMAIN, KINASE, LACRIMO-AURICULO-DENTO-
KEYWDS 5 DIGITAL SYNDROME, MEMBRANE, NUCLEOTIDE-BINDING, PHOSPHOPROTEIN,
KEYWDS 6 POLYMORPHISM, SECRETED, TRANSFERASE, TRANSMEMBRANE, TYROSINE-PROTEIN
KEYWDS 7 KINASE, ACETYLATION, ANGIOGENESIS, DEVELOPMENTAL PROTEIN,
KEYWDS 8 DIFFERENTIATION, MITOGEN, TRANSFERASE-HORMONE COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR F.GUO,R.DAKSHINAMURTHY,S.K.K.THALLAPURANAM,J.SAKON
REVDAT 3 29-JUL-20 3CU1 1 CAVEAT COMPND REMARK HET
REVDAT 3 2 1 HETNAM FORMUL LINK SITE
REVDAT 3 3 1 ATOM
REVDAT 2 25-OCT-17 3CU1 1 REMARK
REVDAT 1 21-APR-09 3CU1 0
JRNL AUTH F.GUO,R.DAKSHINAMURTHY,S.K.K.THALLAPURANAM,J.SAKON
JRNL TITL CRYSTAL STRUCTURE OF 2:2:2 FGFR2D2:FGF1:SOS COMPLEX
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.95
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 90.0
REMARK 3 NUMBER OF REFLECTIONS : 19219
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.185
REMARK 3 R VALUE (WORKING SET) : 0.180
REMARK 3 FREE R VALUE : 0.277
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 1044
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.67
REMARK 3 REFLECTION IN BIN (WORKING SET) : 580
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 37.12
REMARK 3 BIN R VALUE (WORKING SET) : 0.2380
REMARK 3 BIN FREE R VALUE SET COUNT : 28
REMARK 3 BIN FREE R VALUE : 0.3460
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3701
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 110
REMARK 3 SOLVENT ATOMS : 343
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.98
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.42000
REMARK 3 B22 (A**2) : -1.49000
REMARK 3 B33 (A**2) : 1.07000
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 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.641
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.354
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.252
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 22.260
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.950
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.890
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3939 ; 0.053 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5355 ; 3.136 ; 1.980
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 455 ; 3.368 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 189 ;32.133 ;23.810
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 677 ;16.752 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 25 ;15.920 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 572 ; 0.281 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2925 ; 0.013 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2057 ; 0.362 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2612 ; 0.357 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 283 ; 0.303 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 40 ; 0.319 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 10 ; 0.250 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2401 ; 0.977 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3687 ; 1.534 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1833 ; 1.158 ; 2.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1668 ; 1.981 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 2
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A C
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 150 A 249 2
REMARK 3 1 C 150 C 249 2
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 400 ; 0.08 ; 0.05
REMARK 3 MEDIUM POSITIONAL 1 A (A): 418 ; 0.61 ; 0.50
REMARK 3 TIGHT THERMAL 1 A (A**2): 400 ; 0.19 ; 0.50
REMARK 3 MEDIUM THERMAL 1 A (A**2): 418 ; 0.96 ; 2.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : B D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 6
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 B 10 B 11 6
REMARK 3 1 D 10 D 11 6
REMARK 3 2 B 12 B 47 2
REMARK 3 2 D 12 D 47 2
REMARK 3 3 B 48 B 52 6
REMARK 3 3 D 48 D 52 6
REMARK 3 4 B 53 B 90 2
REMARK 3 4 D 53 D 90 2
REMARK 3 5 B 91 B 93 3
REMARK 3 5 D 91 D 93 3
REMARK 3 6 B 94 B 137 2
REMARK 3 6 D 94 D 137 2
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 2 B (A): 484 ; 0.07 ; 0.05
REMARK 3 MEDIUM POSITIONAL 2 B (A): 476 ; 0.73 ; 0.50
REMARK 3 LOOSE POSITIONAL 2 B (A): 62 ; 1.19 ; 5.00
REMARK 3 TIGHT THERMAL 2 B (A**2): 484 ; 0.18 ; 0.50
REMARK 3 MEDIUM THERMAL 2 B (A**2): 476 ; 0.69 ; 2.00
REMARK 3 LOOSE THERMAL 2 B (A**2): 62 ; 2.96 ; 10.00
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3CU1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-APR-08.
REMARK 100 THE DEPOSITION ID IS D_1000047208.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-JUL-07
REMARK 200 TEMPERATURE (KELVIN) : 77
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9793
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-3000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21046
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.3
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : 0.06900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 67.9
REMARK 200 DATA REDUNDANCY IN SHELL : 2.90
REMARK 200 R MERGE FOR SHELL (I) : 0.28100
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.72
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 12% PEG3350, 4% TACSIMATE, PH 7.0,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
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+1/2,Y+1/2,-Z
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 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 42.96450
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 55.18750
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 42.96450
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 55.18750
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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, 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 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 ASN B 7
REMARK 465 TYR B 8
REMARK 465 LYS B 9
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 CB LEU B 13 O HOH B 204 1.58
REMARK 500 O VAL D 137 O HOH D 211 1.68
REMARK 500 CB THR C 174 O HOH C 361 1.76
REMARK 500 O HOH B 195 O HOH B 206 1.79
REMARK 500 CB ALA C 171 O HOH C 372 1.80
REMARK 500 CG LEU B 13 O HOH B 204 1.83
REMARK 500 OE1 GLN C 212 O HOH C 381 1.87
REMARK 500 O HOH C 334 O HOH C 379 1.87
REMARK 500 CB THR A 174 O HOH A 306 1.88
REMARK 500 NZ LYS D 118 O26 GU4 F 1 1.91
REMARK 500 CB SER B 47 O HOH B 210 1.93
REMARK 500 C LYS D 9 O HOH D 239 1.99
REMARK 500 O HOH D 178 O HOH D 251 1.99
REMARK 500 NZ LYS B 128 O HOH B 162 2.02
REMARK 500 O1S3 YYJ F 2 O HOH D 259 2.02
REMARK 500 O HOH B 180 O HOH B 189 2.03
REMARK 500 N ASN C 150 O HOH C 380 2.04
REMARK 500 OG1 THR C 174 O HOH C 361 2.05
REMARK 500 O HOH A 302 O HOH A 325 2.05
REMARK 500 NH2 ARG D 37 O HOH D 215 2.07
REMARK 500 O VAL B 137 O HOH B 151 2.07
REMARK 500 NE2 GLN D 40 O HOH D 221 2.08
REMARK 500 O PRO D 134 O HOH D 265 2.09
REMARK 500 O HOH B 155 O HOH B 169 2.10
REMARK 500 CB SER C 220 O HOH C 356 2.12
REMARK 500 N LYS D 101 O HOH D 251 2.12
REMARK 500 N LYS D 10 O HOH D 239 2.12
REMARK 500 O HOH C 302 O HOH C 378 2.13
REMARK 500 OH TYR A 207 O HOH A 298 2.14
REMARK 500 O HOH A 304 O HOH A 315 2.15
REMARK 500 C VAL A 249 O HOH A 315 2.18
REMARK 500 O PRO A 154 O HOH A 250 2.18
REMARK 500 CD2 TYR D 125 O HOH D 206 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 ASN A 150 CB ASN A 150 CG -0.148
REMARK 500 ARG A 152 CB ARG A 152 CG -0.201
REMARK 500 ARG A 152 CG ARG A 152 CD -0.153
REMARK 500 ARG A 152 CZ ARG A 152 NH2 0.078
REMARK 500 TRP A 156 CZ3 TRP A 156 CH2 -0.143
REMARK 500 GLU A 160 CG GLU A 160 CD 0.142
REMARK 500 GLU A 160 CD GLU A 160 OE2 0.115
REMARK 500 LYS A 161 CB LYS A 161 CG 0.181
REMARK 500 LYS A 161 CD LYS A 161 CE 0.168
REMARK 500 LYS A 161 CE LYS A 161 NZ 0.157
REMARK 500 GLU A 163 CG GLU A 163 CD 0.100
REMARK 500 GLU A 163 CD GLU A 163 OE2 0.086
REMARK 500 HIS A 167 C HIS A 167 O 0.118
REMARK 500 VAL A 169 CB VAL A 169 CG1 -0.199
REMARK 500 CYS A 179 CA CYS A 179 CB -0.104
REMARK 500 MET A 189 CG MET A 189 SD 0.165
REMARK 500 ARG A 190 CB ARG A 190 CG -0.197
REMARK 500 LYS A 196 CD LYS A 196 CE 0.181
REMARK 500 LYS A 196 CE LYS A 196 NZ 0.238
REMARK 500 GLU A 197 CB GLU A 197 CG -0.151
REMARK 500 GLU A 197 CG GLU A 197 CD 0.091
REMARK 500 GLU A 197 CD GLU A 197 OE2 0.085
REMARK 500 GLU A 201 CD GLU A 201 OE2 0.072
REMARK 500 TYR A 207 CB TYR A 207 CG -0.099
REMARK 500 TYR A 207 CE2 TYR A 207 CD2 -0.118
REMARK 500 LYS A 208 CD LYS A 208 CE 0.182
REMARK 500 GLN A 212 CB GLN A 212 CG 0.343
REMARK 500 GLN A 212 CG GLN A 212 CD 0.159
REMARK 500 GLU A 219 CG GLU A 219 CD 0.147
REMARK 500 GLU A 219 CD GLU A 219 OE1 0.093
REMARK 500 VAL A 221 CB VAL A 221 CG2 -0.217
REMARK 500 VAL A 232 CA VAL A 232 CB -0.133
REMARK 500 GLU A 234 CG GLU A 234 CD 0.118
REMARK 500 GLU A 234 CD GLU A 234 OE1 0.101
REMARK 500 GLU A 234 CD GLU A 234 OE2 0.077
REMARK 500 GLU A 236 CD GLU A 236 OE1 0.072
REMARK 500 TYR A 237 CD1 TYR A 237 CE1 -0.132
REMARK 500 TYR A 237 CE2 TYR A 237 CD2 -0.096
REMARK 500 VAL A 248 CB VAL A 248 CG1 0.144
REMARK 500 VAL A 249 CB VAL A 249 CG1 -0.159
REMARK 500 LYS B 10 CD LYS B 10 CE 0.168
REMARK 500 LEU B 14 CG LEU B 14 CD1 -0.296
REMARK 500 TYR B 15 CE2 TYR B 15 CD2 -0.093
REMARK 500 PHE B 22 CB PHE B 22 CG -0.126
REMARK 500 GLU B 49 CG GLU B 49 CD 0.096
REMARK 500 LYS B 57 CE LYS B 57 NZ 0.219
REMARK 500 GLU B 60 CB GLU B 60 CG -0.150
REMARK 500 TYR B 64 CE1 TYR B 64 CZ 0.083
REMARK 500 GLU B 91 CG GLU B 91 CD 0.124
REMARK 500 GLU B 91 C GLU B 91 O -0.129
REMARK 500
REMARK 500 THIS ENTRY HAS 124 BOND DEVIATIONS.
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 ARG A 152 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 LYS A 161 CD - CE - NZ ANGL. DEV. = 16.9 DEGREES
REMARK 500 PRO A 187 C - N - CA ANGL. DEV. = -9.2 DEGREES
REMARK 500 ARG A 190 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 ARG A 210 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 SER A 224 CB - CA - C ANGL. DEV. = -13.4 DEGREES
REMARK 500 ASP A 247 CB - CG - OD1 ANGL. DEV. = -9.2 DEGREES
REMARK 500 ASP A 247 CB - CG - OD2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 LEU B 13 CB - CG - CD2 ANGL. DEV. = -10.5 DEGREES
REMARK 500 ASP B 36 CB - CG - OD1 ANGL. DEV. = 6.4 DEGREES
REMARK 500 ASN B 92 N - CA - C ANGL. DEV. = 19.8 DEGREES
REMARK 500 CYS B 117 CB - CA - C ANGL. DEV. = -14.2 DEGREES
REMARK 500 TYR B 125 CB - CA - C ANGL. DEV. = 12.7 DEGREES
REMARK 500 TYR B 125 CA - CB - CG ANGL. DEV. = 14.5 DEGREES
REMARK 500 LYS C 151 N - CA - CB ANGL. DEV. = -13.4 DEGREES
REMARK 500 ARG C 165 NE - CZ - NH1 ANGL. DEV. = -3.8 DEGREES
REMARK 500 ARG C 190 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG C 203 CB - CA - C ANGL. DEV. = -12.2 DEGREES
REMARK 500 ILE C 204 CB - CA - C ANGL. DEV. = 12.5 DEGREES
REMARK 500 GLU C 234 CB - CA - C ANGL. DEV. = -14.6 DEGREES
REMARK 500 ASP C 247 N - CA - CB ANGL. DEV. = -12.2 DEGREES
REMARK 500 LEU D 26 CA - CB - CG ANGL. DEV. = 16.8 DEGREES
REMARK 500 ASP D 32 N - CA - CB ANGL. DEV. = -15.2 DEGREES
REMARK 500 VAL D 51 N - CA - C ANGL. DEV. = -23.4 DEGREES
REMARK 500 VAL D 54 CB - CA - C ANGL. DEV. = -15.0 DEGREES
REMARK 500 ASP D 68 CB - CA - C ANGL. DEV. = -19.7 DEGREES
REMARK 500 GLU D 91 N - CA - C ANGL. DEV. = 20.9 DEGREES
REMARK 500 GLU D 91 CA - C - N ANGL. DEV. = 17.0 DEGREES
REMARK 500 GLU D 91 O - C - N ANGL. DEV. = -9.7 DEGREES
REMARK 500 ASN D 92 C - N - CA ANGL. DEV. = 22.0 DEGREES
REMARK 500 ASN D 92 N - CA - CB ANGL. DEV. = 13.1 DEGREES
REMARK 500 CYS D 117 CB - CA - C ANGL. DEV. = -15.6 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 A 158 58.14 -146.62
REMARK 500 ASP B 32 -158.41 -159.46
REMARK 500 ALA B 48 -148.33 -97.57
REMARK 500 GLU B 49 102.18 -56.08
REMARK 500 SER B 50 -165.33 -66.11
REMARK 500 GLU B 53 116.10 -169.36
REMARK 500 ASN B 80 167.50 169.79
REMARK 500 GLU B 91 39.09 -71.41
REMARK 500 HIS B 93 70.94 -107.10
REMARK 500 HIS B 102 43.42 -102.86
REMARK 500 LYS C 151 105.63 -48.86
REMARK 500 ASN C 158 58.15 -149.35
REMARK 500 ALA C 172 37.66 -90.20
REMARK 500 ASN C 173 -176.60 -66.94
REMARK 500 CYS C 179 64.95 -153.30
REMARK 500 LYS C 226 143.38 -37.34
REMARK 500 LYS D 9 57.32 -64.01
REMARK 500 LYS D 10 -149.36 -139.78
REMARK 500 LYS D 12 171.23 -51.88
REMARK 500 ASP D 32 -174.43 -173.89
REMARK 500 ALA D 48 -145.58 -89.78
REMARK 500 SER D 50 143.34 164.10
REMARK 500 ASN D 80 164.48 159.58
REMARK 500 GLU D 81 -35.51 -35.33
REMARK 500 ASN D 92 -89.82 157.98
REMARK 500 HIS D 93 67.42 -107.71
REMARK 500 HIS D 102 44.95 -105.80
REMARK 500
REMARK 500 REMARK: NULL
DBREF 3CU1 A 150 249 UNP P21802 FGFR2_HUMAN 150 249
DBREF 3CU1 B 7 137 UNP P05230 FGF1_HUMAN 22 152
DBREF 3CU1 C 150 249 UNP P21802 FGFR2_HUMAN 150 249
DBREF 3CU1 D 7 137 UNP P05230 FGF1_HUMAN 22 152
SEQRES 1 A 100 ASN LYS ARG ALA PRO TYR TRP THR ASN THR GLU LYS MET
SEQRES 2 A 100 GLU LYS ARG LEU HIS ALA VAL PRO ALA ALA ASN THR VAL
SEQRES 3 A 100 LYS PHE ARG CYS PRO ALA GLY GLY ASN PRO MET PRO THR
SEQRES 4 A 100 MET ARG TRP LEU LYS ASN GLY LYS GLU PHE LYS GLN GLU
SEQRES 5 A 100 HIS ARG ILE GLY GLY TYR LYS VAL ARG ASN GLN HIS TRP
SEQRES 6 A 100 SER LEU ILE MET GLU SER VAL VAL PRO SER ASP LYS GLY
SEQRES 7 A 100 ASN TYR THR CYS VAL VAL GLU ASN GLU TYR GLY SER ILE
SEQRES 8 A 100 ASN HIS THR TYR HIS LEU ASP VAL VAL
SEQRES 1 B 131 ASN TYR LYS LYS PRO LYS LEU LEU TYR CYS SER ASN GLY
SEQRES 2 B 131 GLY HIS PHE LEU ARG ILE LEU PRO ASP GLY THR VAL ASP
SEQRES 3 B 131 GLY THR ARG ASP ARG SER ASP GLN HIS ILE GLN LEU GLN
SEQRES 4 B 131 LEU SER ALA GLU SER VAL GLY GLU VAL TYR ILE LYS SER
SEQRES 5 B 131 THR GLU THR GLY GLN TYR LEU ALA MET ASP THR ASP GLY
SEQRES 6 B 131 LEU LEU TYR GLY SER GLN THR PRO ASN GLU GLU CYS LEU
SEQRES 7 B 131 PHE LEU GLU ARG LEU GLU GLU ASN HIS TYR ASN THR TYR
SEQRES 8 B 131 ILE SER LYS LYS HIS ALA GLU LYS ASN TRP PHE VAL GLY
SEQRES 9 B 131 LEU LYS LYS ASN GLY SER CYS LYS ARG GLY PRO ARG THR
SEQRES 10 B 131 HIS TYR GLY GLN LYS ALA ILE LEU PHE LEU PRO LEU PRO
SEQRES 11 B 131 VAL
SEQRES 1 C 100 ASN LYS ARG ALA PRO TYR TRP THR ASN THR GLU LYS MET
SEQRES 2 C 100 GLU LYS ARG LEU HIS ALA VAL PRO ALA ALA ASN THR VAL
SEQRES 3 C 100 LYS PHE ARG CYS PRO ALA GLY GLY ASN PRO MET PRO THR
SEQRES 4 C 100 MET ARG TRP LEU LYS ASN GLY LYS GLU PHE LYS GLN GLU
SEQRES 5 C 100 HIS ARG ILE GLY GLY TYR LYS VAL ARG ASN GLN HIS TRP
SEQRES 6 C 100 SER LEU ILE MET GLU SER VAL VAL PRO SER ASP LYS GLY
SEQRES 7 C 100 ASN TYR THR CYS VAL VAL GLU ASN GLU TYR GLY SER ILE
SEQRES 8 C 100 ASN HIS THR TYR HIS LEU ASP VAL VAL
SEQRES 1 D 131 ASN TYR LYS LYS PRO LYS LEU LEU TYR CYS SER ASN GLY
SEQRES 2 D 131 GLY HIS PHE LEU ARG ILE LEU PRO ASP GLY THR VAL ASP
SEQRES 3 D 131 GLY THR ARG ASP ARG SER ASP GLN HIS ILE GLN LEU GLN
SEQRES 4 D 131 LEU SER ALA GLU SER VAL GLY GLU VAL TYR ILE LYS SER
SEQRES 5 D 131 THR GLU THR GLY GLN TYR LEU ALA MET ASP THR ASP GLY
SEQRES 6 D 131 LEU LEU TYR GLY SER GLN THR PRO ASN GLU GLU CYS LEU
SEQRES 7 D 131 PHE LEU GLU ARG LEU GLU GLU ASN HIS TYR ASN THR TYR
SEQRES 8 D 131 ILE SER LYS LYS HIS ALA GLU LYS ASN TRP PHE VAL GLY
SEQRES 9 D 131 LEU LYS LYS ASN GLY SER CYS LYS ARG GLY PRO ARG THR
SEQRES 10 D 131 HIS TYR GLY GLN LYS ALA ILE LEU PHE LEU PRO LEU PRO
SEQRES 11 D 131 VAL
HET GU4 E 1 27
HET YYJ E 2 28
HET GU4 F 1 27
HET YYJ F 2 28
HETNAM GU4 2,3,4,6-TETRA-O-SULFONATO-ALPHA-D-GLUCOPYRANOSE
HETNAM YYJ 1,3,4,6-TETRA-O-SULFO-BETA-D-FRUCTOFURANOSE
FORMUL 5 GU4 2(C6 H12 O18 S4)
FORMUL 5 YYJ 2(C6 H12 O18 S4)
FORMUL 7 HOH *343(H2 O)
HELIX 1 1 ASN A 158 GLU A 163 1 6
HELIX 2 2 LYS A 199 ARG A 203 5 5
HELIX 3 3 ASN A 211 HIS A 213 5 3
HELIX 4 4 VAL A 222 LYS A 226 5 5
HELIX 5 5 ASN B 80 CYS B 83 5 4
HELIX 6 6 HIS B 102 ASN B 106 5 5
HELIX 7 7 ARG B 119 THR B 123 5 5
HELIX 8 8 GLN B 127 ILE B 130 5 4
HELIX 9 9 ASN C 158 GLU C 163 1 6
HELIX 10 10 LYS C 199 ARG C 203 5 5
HELIX 11 11 VAL C 222 LYS C 226 5 5
HELIX 12 12 ASN D 80 CYS D 83 5 4
HELIX 13 13 HIS D 102 ASN D 106 5 5
HELIX 14 14 ARG D 119 THR D 123 5 5
HELIX 15 15 GLN D 127 ILE D 130 5 4
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 5 LEU A 166 PRO A 170 0
SHEET 2 B 5 SER A 239 VAL A 249 1 O ASP A 247 N HIS A 167
SHEET 3 B 5 GLY A 227 GLU A 234 -1 N TYR A 229 O TYR A 244
SHEET 4 B 5 THR A 188 LYS A 193 -1 N THR A 188 O GLU A 234
SHEET 5 B 5 LYS A 196 GLU A 197 -1 O LYS A 196 N LYS A 193
SHEET 1 C 3 VAL A 175 ARG A 178 0
SHEET 2 C 3 SER A 215 MET A 218 -1 O LEU A 216 N PHE A 177
SHEET 3 C 3 LYS A 208 ARG A 210 -1 N LYS A 208 O ILE A 217
SHEET 1 D 4 VAL B 31 THR B 34 0
SHEET 2 D 4 HIS B 21 ILE B 25 -1 N PHE B 22 O THR B 34
SHEET 3 D 4 LYS B 12 CYS B 16 -1 N CYS B 16 O HIS B 21
SHEET 4 D 4 PHE B 132 PRO B 136 -1 O LEU B 135 N LEU B 13
SHEET 1 E 2 LEU B 44 SER B 47 0
SHEET 2 E 2 TYR B 55 SER B 58 -1 O LYS B 57 N GLN B 45
SHEET 1 F 2 TYR B 64 MET B 67 0
SHEET 2 F 2 LEU B 73 SER B 76 -1 O SER B 76 N TYR B 64
SHEET 1 G 2 PHE B 85 LEU B 89 0
SHEET 2 G 2 ASN B 95 SER B 99 -1 O ILE B 98 N LEU B 86
SHEET 1 H 2 ARG C 152 TRP C 156 0
SHEET 2 H 2 ALA C 181 ASN C 184 -1 O ASN C 184 N ARG C 152
SHEET 1 I 5 LEU C 166 PRO C 170 0
SHEET 2 I 5 SER C 239 VAL C 249 1 O HIS C 245 N HIS C 167
SHEET 3 I 5 GLY C 227 GLU C 234 -1 N TYR C 229 O TYR C 244
SHEET 4 I 5 THR C 188 LYS C 193 -1 N THR C 188 O GLU C 234
SHEET 5 I 5 LYS C 196 GLU C 197 -1 O LYS C 196 N LYS C 193
SHEET 1 J 3 VAL C 175 ARG C 178 0
SHEET 2 J 3 SER C 215 MET C 218 -1 O LEU C 216 N PHE C 177
SHEET 3 J 3 LYS C 208 ARG C 210 -1 N LYS C 208 O ILE C 217
SHEET 1 K 4 VAL D 31 THR D 34 0
SHEET 2 K 4 HIS D 21 ILE D 25 -1 N PHE D 22 O THR D 34
SHEET 3 K 4 LEU D 13 CYS D 16 -1 N CYS D 16 O HIS D 21
SHEET 4 K 4 PHE D 132 LEU D 135 -1 O LEU D 135 N LEU D 13
SHEET 1 L 4 LEU D 44 SER D 47 0
SHEET 2 L 4 GLU D 53 SER D 58 -1 O LYS D 57 N GLN D 45
SHEET 3 L 4 PHE D 85 LEU D 89 -1 O PHE D 85 N VAL D 54
SHEET 4 L 4 ASN D 95 SER D 99 -1 O ILE D 98 N LEU D 86
SHEET 1 M 2 TYR D 64 MET D 67 0
SHEET 2 M 2 LEU D 73 SER D 76 -1 O SER D 76 N TYR D 64
SSBOND 1 CYS A 179 CYS A 231 1555 1555 2.28
SSBOND 2 CYS C 179 CYS C 231 1555 1555 2.15
LINK C1 GU4 E 1 O2 YYJ E 2 1555 1555 1.44
LINK C1 GU4 F 1 O2 YYJ F 2 1555 1555 1.46
CISPEP 1 ALA A 171 ALA A 172 0 -1.52
CISPEP 2 ASN A 184 PRO A 185 0 -2.28
CISPEP 3 ALA B 48 GLU B 49 0 0.42
CISPEP 4 SER B 50 VAL B 51 0 1.20
CISPEP 5 ASN B 92 HIS B 93 0 0.44
CISPEP 6 ALA C 171 ALA C 172 0 -1.79
CISPEP 7 ASN C 184 PRO C 185 0 -0.31
CISPEP 8 ALA D 48 GLU D 49 0 1.37
CISPEP 9 GLU D 49 SER D 50 0 1.01
CISPEP 10 SER D 50 VAL D 51 0 1.17
CISPEP 11 VAL D 51 GLY D 52 0 -0.96
CISPEP 12 GLU D 91 ASN D 92 0 -6.96
CISPEP 13 ASN D 92 HIS D 93 0 0.77
CRYST1 85.929 110.375 74.699 90.00 90.00 90.00 P 21 21 2 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 0.011638 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009060 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013387 0.00000
(ATOM LINES ARE NOT SHOWN.)
END