HEADER TRANSCRIPTION 02-NOV-15 5FM9
TITLE HUMAN NOTCH 1, EGF 4-7
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NEUROGENIC LOCUS NOTCH HOMOLOG PROTEIN 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: EGF DOMAINS 4-7, UNP RESIDUES 140-294;
COMPND 5 SYNONYM: NOTCH 1, HN1, TRANSLOCATION-ASSOCIATED NOTCH PROTEIN TAN-1,
COMPND 6 NOTCH 1 EXTRACELLULAR TRUNCATION, NEXT, NOTCH 1 INTRACELLULAR DOMAIN,
COMPND 7 NICD;
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 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PQE30
KEYWDS TRANSCRIPTION, TRANSMEMBRANE, DEVELOPMENTAL, PROTEIN, NOTCH SIGNALING
KEYWDS 2 PATHWAY, DIFFERENTIATION, PHOSPHORYLATION, EGF- LIKE DOMAIN,
KEYWDS 3 REGULATION, RECEPTOR, ACTIVATOR, ANK REPEAT, SIGNALLING,
KEYWDS 4 GLYCOPROTEIN, EXTRACELLULAR, EGF, NOTCH, JAGGED, MEMBRANE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.C.WEISSHUHN,D.SHEPPARD,P.TAYLOR,P.WHITEMAN,S.M.LEA,P.A.HANDFORD,
AUTHOR 2 C.REDFIELD
REVDAT 3 10-JAN-24 5FM9 1 REMARK LINK
REVDAT 2 07-FEB-18 5FM9 1 AUTHOR
REVDAT 1 20-APR-16 5FM9 0
JRNL AUTH P.C.WEISSHUHN,D.SHEPPARD,P.TAYLOR,P.WHITEMAN,S.M.LEA,
JRNL AUTH 2 P.A.HANDFORD,C.REDFIELD
JRNL TITL NON-LINEAR AND FLEXIBLE REGIONS OF THE HUMAN NOTCH1
JRNL TITL 2 EXTRACELLULAR DOMAIN REVEALED BY HIGH-RESOLUTION STRUCTURAL
JRNL TITL 3 STUDIES.
JRNL REF STRUCTURE V. 24 555 2016
JRNL REFN ISSN 0969-2126
JRNL PMID 26996961
JRNL DOI 10.1016/J.STR.2016.02.010
REMARK 2
REMARK 2 RESOLUTION. 2.92 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.2
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.92
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 64.73
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.7
REMARK 3 NUMBER OF REFLECTIONS : 5014
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) : 0.214
REMARK 3 R VALUE (WORKING SET) : 0.213
REMARK 3 FREE R VALUE : 0.237
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.650
REMARK 3 FREE R VALUE TEST SET COUNT : 233
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 5
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.92
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 3.26
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.67
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 1377
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2453
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1302
REMARK 3 BIN R VALUE (WORKING SET) : 0.2435
REMARK 3 BIN FREE R VALUE : 0.2754
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.45
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 75
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1125
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 2
REMARK 3 SOLVENT ATOMS : 6
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 39.62
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -15.57360
REMARK 3 B22 (A**2) : 5.41930
REMARK 3 B33 (A**2) : 10.15430
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -8.46850
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.426
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 1.558
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.338
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.884
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.864
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 2143 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 3853 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 416 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 34 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 353 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 2143 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : 2 ; 5.000 ; SEMIHARMONIC
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 148 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 2243 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.23
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.27
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 18.82
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: IDEAL-DIST CONTACT TERM CONTACT SETUP.
REMARK 3 RESIDUE TYPES WITHOUT CCP4 ATOM TYPE IN LIBRARY=CA. NUMBER OF
REMARK 3 ATOMS WITH PROPER CCP4 ATOM TYPE=2105. NUMBER WITH APPROX
REMARK 3 DEFAULT CCP4 ATOM TYPE=0. NUMBER TREATED BY BAD NON-BONDED
REMARK 3 CONTACTS=2.
REMARK 4
REMARK 4 5FM9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-NOV-15.
REMARK 100 THE DEPOSITION ID IS D_1290065332.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-FEB-11
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 : DIAMOND
REMARK 200 BEAMLINE : I03
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.75
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 5015
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.920
REMARK 200 RESOLUTION RANGE LOW (A) : 64.730
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 200 DATA REDUNDANCY : 3.000
REMARK 200 R MERGE (I) : 0.12000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.92
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.10
REMARK 200 R MERGE FOR SHELL (I) : 0.37000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
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: 2VJ3.PDB
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.23
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.44
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 8.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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 71.13000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 10.57500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 71.13000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 10.57500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 920 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19210 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.4 KCAL/MOL
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 BIOMT1 2 -1.000000 0.000000 0.000000 -105.27620
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -74.92978
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 138
REMARK 465 ALA A 139
REMARK 465 GLN A 140
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 151 36.47 39.54
REMARK 500 GLU A 159 -134.18 52.65
REMARK 500 SER A 161 -143.43 -96.58
REMARK 500 SER A 201 -163.22 -174.49
REMARK 500 SER A 223 103.62 -161.88
REMARK 500 PRO A 285 1.87 -60.60
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A1295 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 178 OD2
REMARK 620 2 ASP A 178 OD1 45.4
REMARK 620 3 VAL A 179 O 67.3 71.2
REMARK 620 4 GLU A 181 OE1 141.9 132.5 76.8
REMARK 620 5 ASN A 197 OD1 70.4 115.5 79.5 91.5
REMARK 620 6 GLU A 198 O 61.4 77.1 128.4 149.4 78.6
REMARK 620 7 SER A 201 O 131.5 134.7 153.7 79.5 89.8 71.6
REMARK 620 8 HOH A2001 O 104.4 59.5 84.6 83.7 164.1 112.8 104.2
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A1296 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 257 OD1
REMARK 620 2 ILE A 258 O 86.8
REMARK 620 3 ASP A 260 OD1 147.2 72.8
REMARK 620 4 ASP A 274 OD1 116.7 87.9 88.5
REMARK 620 5 ASP A 274 OD2 70.5 66.8 120.9 49.9
REMARK 620 6 GLY A 275 O 88.5 172.9 109.0 99.0 116.5
REMARK 620 7 HOH A2006 O 87.1 103.7 73.7 154.3 155.7 70.7
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1295
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1296
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5FMA RELATED DB: PDB
REMARK 900 HUMAN NOTCH 1, EGF 4-7
DBREF 5FM9 A 140 294 UNP P46531 NOTC1_HUMAN 140 294
SEQADV 5FM9 SER A 138 UNP P46531 EXPRESSION TAG
SEQADV 5FM9 ALA A 139 UNP P46531 EXPRESSION TAG
SEQRES 1 A 157 SER ALA GLN ALA ASP PRO CYS ALA SER ASN PRO CYS ALA
SEQRES 2 A 157 ASN GLY GLY GLN CYS LEU PRO PHE GLU ALA SER TYR ILE
SEQRES 3 A 157 CYS HIS CYS PRO PRO SER PHE HIS GLY PRO THR CYS ARG
SEQRES 4 A 157 GLN ASP VAL ASN GLU CYS GLY GLN LYS PRO GLY LEU CYS
SEQRES 5 A 157 ARG HIS GLY GLY THR CYS HIS ASN GLU VAL GLY SER TYR
SEQRES 6 A 157 ARG CYS VAL CYS ARG ALA THR HIS THR GLY PRO ASN CYS
SEQRES 7 A 157 GLU ARG PRO TYR VAL PRO CYS SER PRO SER PRO CYS GLN
SEQRES 8 A 157 ASN GLY GLY THR CYS ARG PRO THR GLY ASP VAL THR HIS
SEQRES 9 A 157 GLU CYS ALA CYS LEU PRO GLY PHE THR GLY GLN ASN CYS
SEQRES 10 A 157 GLU GLU ASN ILE ASP ASP CYS PRO GLY ASN ASN CYS LYS
SEQRES 11 A 157 ASN GLY GLY ALA CYS VAL ASP GLY VAL ASN THR TYR ASN
SEQRES 12 A 157 CYS ARG CYS PRO PRO GLU TRP THR GLY GLN TYR CYS THR
SEQRES 13 A 157 GLU
HET CA A1295 1
HET CA A1296 1
HETNAM CA CALCIUM ION
FORMUL 2 CA 2(CA 2+)
FORMUL 4 HOH *6(H2 O)
HELIX 1 1 ASP A 142 ASN A 147 5 6
HELIX 2 2 ASN A 180 LYS A 185 1 6
SHEET 1 AA 2 GLN A 154 PHE A 158 0
SHEET 2 AA 2 SER A 161 HIS A 165 -1 O SER A 161 N PHE A 158
SHEET 1 AB 2 PHE A 170 HIS A 171 0
SHEET 2 AB 2 GLN A 177 ASP A 178 -1 O GLN A 177 N HIS A 171
SHEET 1 AC 2 THR A 194 GLU A 198 0
SHEET 2 AC 2 SER A 201 VAL A 205 -1 O SER A 201 N GLU A 198
SHEET 1 AD 2 HIS A 210 THR A 211 0
SHEET 2 AD 2 ARG A 217 PRO A 218 -1 O ARG A 217 N THR A 211
SHEET 1 AE 2 THR A 232 CYS A 233 0
SHEET 2 AE 2 CYS A 243 ALA A 244 -1 O ALA A 244 N THR A 232
SHEET 1 AF 2 PHE A 249 THR A 250 0
SHEET 2 AF 2 GLU A 256 ASN A 257 -1 O GLU A 256 N THR A 250
SHEET 1 AG 2 ALA A 271 ASP A 274 0
SHEET 2 AG 2 TYR A 279 ARG A 282 -1 O ASN A 280 N VAL A 273
SSBOND 1 CYS A 144 CYS A 155 1555 1555 2.08
SSBOND 2 CYS A 149 CYS A 164 1555 1555 2.02
SSBOND 3 CYS A 166 CYS A 175 1555 1555 2.05
SSBOND 4 CYS A 182 CYS A 195 1555 1555 2.05
SSBOND 5 CYS A 189 CYS A 204 1555 1555 2.04
SSBOND 6 CYS A 206 CYS A 215 1555 1555 2.06
SSBOND 7 CYS A 222 CYS A 233 1555 1555 2.05
SSBOND 8 CYS A 227 CYS A 243 1555 1555 2.03
SSBOND 9 CYS A 245 CYS A 254 1555 1555 2.05
SSBOND 10 CYS A 261 CYS A 272 1555 1555 2.07
SSBOND 11 CYS A 266 CYS A 281 1555 1555 2.04
SSBOND 12 CYS A 283 CYS A 292 1555 1555 2.04
LINK OD2 ASP A 178 CA CA A1295 1555 1555 3.01
LINK OD1 ASP A 178 CA CA A1295 1555 1555 2.57
LINK O VAL A 179 CA CA A1295 1555 1555 2.69
LINK OE1 GLU A 181 CA CA A1295 1555 1555 2.14
LINK OD1 ASN A 197 CA CA A1295 1555 1555 2.32
LINK O GLU A 198 CA CA A1295 1555 1555 2.39
LINK O SER A 201 CA CA A1295 1555 1555 2.45
LINK OD1 ASN A 257 CA CA A1296 1555 1555 2.32
LINK O ILE A 258 CA CA A1296 1555 1555 2.50
LINK OD1 ASP A 260 CA CA A1296 1555 1555 2.17
LINK OD1 ASP A 274 CA CA A1296 1555 1555 2.08
LINK OD2 ASP A 274 CA CA A1296 1555 1555 2.86
LINK O GLY A 275 CA CA A1296 1555 1555 2.42
LINK CA CA A1295 O HOH A2001 1555 1555 2.55
LINK CA CA A1296 O HOH A2006 1555 1555 2.31
CISPEP 1 SER A 223 PRO A 224 0 -0.62
SITE 1 AC1 7 ASP A 178 VAL A 179 GLU A 181 ASN A 197
SITE 2 AC1 7 GLU A 198 SER A 201 HOH A2001
SITE 1 AC2 6 ASN A 257 ILE A 258 ASP A 260 ASP A 274
SITE 2 AC2 6 GLY A 275 HOH A2006
CRYST1 142.260 21.150 83.560 90.00 116.27 90.00 C 1 2 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 0.007029 0.000000 0.003470 0.00000
SCALE2 0.000000 0.047281 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013346 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
