HEADER CELL ADHESION 15-OCT-13 4CBP
TITLE CRYSTAL STRUCTURE OF NEURAL ECTODERMAL DEVELOPMENT FACTOR IMP-L2.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NEURAL/ECTODERMAL DEVELOPMENT FACTOR IMP-L2;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: NEURAL ECTODERMAL DEVELOPMENT FACTOR IMP-L2;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;
SOURCE 3 ORGANISM_COMMON: FRUIT FLY;
SOURCE 4 ORGANISM_TAXID: 7227;
SOURCE 5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: SF9;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR: FLASHBAC;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PVL1392
KEYWDS CELL ADHESION, IMAGINAL MORPHOGENESIS PROTEIN-LATE 2, INSULIN
KEYWDS 2 BINDING, IMMUNOGLOBULIN DOMAIN, DEVELOPMENTAL PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR N.KULAHIN,O.KRISTENSEN,M.BRZOZOWSKI,G.SCHLUCKEBIER,P.D.MEYTS
REVDAT 3 29-MAY-19 4CBP 1 REMARK LINK
REVDAT 2 17-JAN-18 4CBP 1 REMARK
REVDAT 1 29-OCT-14 4CBP 0
JRNL AUTH N.KULAHIN,C.J.WATSON,J.P.TURKENBURG,O.KRISTENSEN,M.NORRMAN,
JRNL AUTH 2 W.SAJID,G.SCHLUCKEBIER,P.D.MEYTS,M.BRZOZOWSKI
JRNL TITL STRUCTURAL ANALYSIS OF IMP-L2 FUNCTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.54
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.910
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.7
REMARK 3 NUMBER OF REFLECTIONS : 69600
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.157
REMARK 3 R VALUE (WORKING SET) : 0.156
REMARK 3 FREE R VALUE : 0.188
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.800
REMARK 3 FREE R VALUE TEST SET COUNT : 3844
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 29.5474 - 4.2654 0.97 7113 220 0.1684 0.1953
REMARK 3 2 4.2654 - 3.3872 1.00 7304 216 0.1553 0.1663
REMARK 3 3 3.3872 - 2.9595 1.00 7286 204 0.1573 0.1834
REMARK 3 4 2.9595 - 2.6891 1.00 7320 216 0.1631 0.2054
REMARK 3 5 2.6891 - 2.4964 1.00 7316 211 0.1597 0.2238
REMARK 3 6 2.4964 - 2.3493 1.00 7290 220 0.1543 0.1670
REMARK 3 7 2.3493 - 2.2317 1.00 7335 207 0.1390 0.1926
REMARK 3 8 2.2317 - 2.1346 1.00 7351 200 0.1323 0.1562
REMARK 3 9 2.1346 - 2.0524 1.00 7284 210 0.1343 0.1800
REMARK 3 10 2.0524 - 1.9816 1.00 7291 210 0.1315 0.1776
REMARK 3 11 1.9816 - 1.9197 1.00 7258 210 0.1330 0.1650
REMARK 3 12 1.9197 - 1.8648 1.00 7327 213 0.1402 0.1924
REMARK 3 13 1.8648 - 1.8157 1.00 7219 225 0.1507 0.1678
REMARK 3 14 1.8157 - 1.7714 1.00 7303 208 0.1621 0.2019
REMARK 3 15 1.7714 - 1.7312 0.95 6992 198 0.1683 0.2315
REMARK 3 16 1.7312 - 1.6943 0.89 6518 200 0.1855 0.2180
REMARK 3 17 1.6943 - 1.6604 0.82 5908 173 0.2064 0.2450
REMARK 3 18 1.6604 - 1.6291 0.74 5512 170 0.2199 0.2638
REMARK 3 19 1.6291 - 1.6000 0.65 4669 133 0.2369 0.2820
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.00
REMARK 3 SHRINKAGE RADIUS : 0.70
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.160
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.620
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 18.48
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.006 3495
REMARK 3 ANGLE : 1.086 4762
REMARK 3 CHIRALITY : 0.040 535
REMARK 3 PLANARITY : 0.004 621
REMARK 3 DIHEDRAL : 11.782 1321
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: REFINED AGAINST ANOMALOUS DATA
REMARK 4
REMARK 4 4CBP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-OCT-13.
REMARK 100 THE DEPOSITION ID IS D_1290058732.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-FEB-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : MAX II
REMARK 200 BEAMLINE : I911-3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9800
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 : XIA2, MOSFLM
REMARK 200 DATA SCALING SOFTWARE : XIA2, AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 70546
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.590
REMARK 200 RESOLUTION RANGE LOW (A) : 56.250
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 6.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.7
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.05000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.59
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.65
REMARK 200 COMPLETENESS FOR SHELL (%) : 71.9
REMARK 200 DATA REDUNDANCY IN SHELL : 2.30
REMARK 200 R MERGE FOR SHELL (I) : 0.42000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: HKL2MAP
REMARK 200 STARTING MODEL: NONE
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: HANGING-DROP EXPERIMENTS BY MIXING 1
REMARK 280 UL PROTEIN (5.5. MG/ML IN 10 MM HEPES PH 7.4, 20 MM NACL) AND 1
REMARK 280 UL RESERVOIR SOLUTION (17% PEG-6000, 0.1 M TRIS HYDROCHLORIDE,
REMARK 280 PH 7.0), VAPOR DIFFUSION, HANGING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 49.86600
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2390 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21110 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.4 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 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 MSE A -20
REMARK 465 ASN A -19
REMARK 465 LEU A -18
REMARK 465 HIS A -17
REMARK 465 VAL A -16
REMARK 465 CYS A -15
REMARK 465 ALA A -14
REMARK 465 LEU A -13
REMARK 465 ALA A -12
REMARK 465 LEU A -11
REMARK 465 LEU A -10
REMARK 465 LEU A -9
REMARK 465 PHE A -8
REMARK 465 GLY A -7
REMARK 465 SER A -6
REMARK 465 ILE A -5
REMARK 465 ALA A -4
REMARK 465 THR A -3
REMARK 465 VAL A -2
REMARK 465 ARG A -1
REMARK 465 GLY A 0
REMARK 465 ARG A 1
REMARK 465 ALA A 2
REMARK 465 VAL A 3
REMARK 465 ASP A 4
REMARK 465 LEU A 5
REMARK 465 VAL A 6
REMARK 465 ASP A 7
REMARK 465 ASP A 8
REMARK 465 SER A 9
REMARK 465 ASN A 10
REMARK 465 ASP A 11
REMARK 465 VAL A 12
REMARK 465 ASP A 13
REMARK 465 ASN A 14
REMARK 465 SER A 15
REMARK 465 ILE A 16
REMARK 465 GLU A 17
REMARK 465 ALA A 18
REMARK 465 GLU A 19
REMARK 465 GLU A 20
REMARK 465 GLU A 21
REMARK 465 LYS A 22
REMARK 465 GLU A 76
REMARK 465 LEU A 77
REMARK 465 ASP A 78
REMARK 465 ASP A 79
REMARK 465 LEU A 80
REMARK 465 ASP A 81
REMARK 465 SER A 82
REMARK 465 ASN A 83
REMARK 465 GLN A 84
REMARK 465 VAL A 85
REMARK 465 GLU A 240
REMARK 465 GLU A 241
REMARK 465 ASP A 242
REMARK 465 GLU A 243
REMARK 465 VAL A 244
REMARK 465 LEU A 245
REMARK 465 PHE A 246
REMARK 465 GLN A 247
REMARK 465 MSE B -20
REMARK 465 ASN B -19
REMARK 465 LEU B -18
REMARK 465 HIS B -17
REMARK 465 VAL B -16
REMARK 465 CYS B -15
REMARK 465 ALA B -14
REMARK 465 LEU B -13
REMARK 465 ALA B -12
REMARK 465 LEU B -11
REMARK 465 LEU B -10
REMARK 465 LEU B -9
REMARK 465 PHE B -8
REMARK 465 GLY B -7
REMARK 465 SER B -6
REMARK 465 ILE B -5
REMARK 465 ALA B -4
REMARK 465 THR B -3
REMARK 465 VAL B -2
REMARK 465 ARG B -1
REMARK 465 GLY B 0
REMARK 465 ARG B 1
REMARK 465 ALA B 2
REMARK 465 VAL B 3
REMARK 465 ASP B 4
REMARK 465 LEU B 5
REMARK 465 VAL B 6
REMARK 465 ASP B 7
REMARK 465 ASP B 8
REMARK 465 SER B 9
REMARK 465 ASN B 10
REMARK 465 ASP B 11
REMARK 465 VAL B 12
REMARK 465 ASP B 13
REMARK 465 ASN B 14
REMARK 465 SER B 15
REMARK 465 ILE B 16
REMARK 465 GLU B 17
REMARK 465 ALA B 18
REMARK 465 GLU B 19
REMARK 465 GLU B 20
REMARK 465 GLU B 21
REMARK 465 LYS B 22
REMARK 465 PRO B 23
REMARK 465 ARG B 24
REMARK 465 ASN B 25
REMARK 465 ARG B 26
REMARK 465 ALA B 27
REMARK 465 PHE B 28
REMARK 465 GLU B 29
REMARK 465 GLU B 76
REMARK 465 LEU B 77
REMARK 465 ASP B 78
REMARK 465 ASP B 79
REMARK 465 LEU B 80
REMARK 465 ASP B 81
REMARK 465 SER B 82
REMARK 465 ASN B 83
REMARK 465 GLN B 84
REMARK 465 VAL B 85
REMARK 465 ALA B 86
REMARK 465 GLN B 247
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 OD1 ASP B 203 O HOH B 2143 1.92
REMARK 500 OD1 ASP A 203 O HOH A 2180 1.92
REMARK 500 O HOH B 2144 O HOH B 2148 2.14
REMARK 500 OE1 GLN A 147 NH1 ARG A 175 2.14
REMARK 500 O HOH B 2031 O HOH B 2032 2.19
REMARK 500 O HOH A 2080 O HOH A 2081 2.19
REMARK 500 O HOH B 2137 O HOH B 2207 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 OE2 GLU B 241 O HOH A 2034 2547 2.16
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 ARG A 24 7.02 12.07
REMARK 500 GLN A 61 -139.39 54.62
REMARK 500 GLN B 61 -142.89 54.02
REMARK 500 ALA B 89 73.89 -150.36
REMARK 500 SER B 91 -11.06 80.72
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ARG A 24 ASN A 25 145.33
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A2101 DISTANCE = 6.01 ANGSTROMS
REMARK 525 HOH A2126 DISTANCE = 5.83 ANGSTROMS
REMARK 525 HOH B2209 DISTANCE = 6.39 ANGSTROMS
REMARK 525 HOH B2210 DISTANCE = 6.84 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1240
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1241
DBREF 4CBP A -20 242 UNP Q09024 IMPL2_DROME 5 267
DBREF 4CBP B -20 242 UNP Q09024 IMPL2_DROME 5 267
SEQADV 4CBP GLU A 243 UNP Q09024 EXPRESSION TAG
SEQADV 4CBP VAL A 244 UNP Q09024 EXPRESSION TAG
SEQADV 4CBP LEU A 245 UNP Q09024 EXPRESSION TAG
SEQADV 4CBP PHE A 246 UNP Q09024 EXPRESSION TAG
SEQADV 4CBP GLN A 247 UNP Q09024 EXPRESSION TAG
SEQADV 4CBP GLU B 243 UNP Q09024 EXPRESSION TAG
SEQADV 4CBP VAL B 244 UNP Q09024 EXPRESSION TAG
SEQADV 4CBP LEU B 245 UNP Q09024 EXPRESSION TAG
SEQADV 4CBP PHE B 246 UNP Q09024 EXPRESSION TAG
SEQADV 4CBP GLN B 247 UNP Q09024 EXPRESSION TAG
SEQRES 1 A 268 MSE ASN LEU HIS VAL CYS ALA LEU ALA LEU LEU LEU PHE
SEQRES 2 A 268 GLY SER ILE ALA THR VAL ARG GLY ARG ALA VAL ASP LEU
SEQRES 3 A 268 VAL ASP ASP SER ASN ASP VAL ASP ASN SER ILE GLU ALA
SEQRES 4 A 268 GLU GLU GLU LYS PRO ARG ASN ARG ALA PHE GLU ALA ASP
SEQRES 5 A 268 TRP LEU LYS PHE THR LYS THR PRO PRO THR LYS LEU GLN
SEQRES 6 A 268 GLN ALA ASP GLY ALA THR ILE GLU ILE VAL CYS GLU MSE
SEQRES 7 A 268 MSE GLY SER GLN VAL PRO SER ILE GLN TRP VAL VAL GLY
SEQRES 8 A 268 HIS LEU PRO ARG SER GLU LEU ASP ASP LEU ASP SER ASN
SEQRES 9 A 268 GLN VAL ALA GLU GLU ALA PRO SER ALA ILE VAL ARG VAL
SEQRES 10 A 268 ARG SER SER HIS ILE ILE ASP HIS VAL LEU SER GLU ALA
SEQRES 11 A 268 ARG THR TYR THR CYS VAL GLY ARG THR GLY SER LYS THR
SEQRES 12 A 268 ILE TYR ALA SER THR VAL VAL HIS PRO PRO ARG SER SER
SEQRES 13 A 268 ARG LEU THR PRO GLU LYS THR TYR PRO GLY ALA GLN LYS
SEQRES 14 A 268 PRO ARG ILE ILE TYR THR GLU LYS THR HIS LEU ASP LEU
SEQRES 15 A 268 MSE GLY SER ASN ILE GLN LEU PRO CYS ARG VAL HIS ALA
SEQRES 16 A 268 ARG PRO ARG ALA GLU ILE THR TRP LEU ASN ASN GLU ASN
SEQRES 17 A 268 LYS GLU ILE VAL GLN GLY HIS ARG HIS ARG VAL LEU ALA
SEQRES 18 A 268 ASN GLY ASP LEU LEU ILE SER GLU ILE LYS TRP GLU ASP
SEQRES 19 A 268 MSE GLY ASN TYR LYS CYS ILE ALA ARG ASN VAL VAL GLY
SEQRES 20 A 268 LYS ASP THR ALA ASP THR PHE VAL TYR PRO VAL LEU ASN
SEQRES 21 A 268 GLU GLU ASP GLU VAL LEU PHE GLN
SEQRES 1 B 268 MSE ASN LEU HIS VAL CYS ALA LEU ALA LEU LEU LEU PHE
SEQRES 2 B 268 GLY SER ILE ALA THR VAL ARG GLY ARG ALA VAL ASP LEU
SEQRES 3 B 268 VAL ASP ASP SER ASN ASP VAL ASP ASN SER ILE GLU ALA
SEQRES 4 B 268 GLU GLU GLU LYS PRO ARG ASN ARG ALA PHE GLU ALA ASP
SEQRES 5 B 268 TRP LEU LYS PHE THR LYS THR PRO PRO THR LYS LEU GLN
SEQRES 6 B 268 GLN ALA ASP GLY ALA THR ILE GLU ILE VAL CYS GLU MSE
SEQRES 7 B 268 MSE GLY SER GLN VAL PRO SER ILE GLN TRP VAL VAL GLY
SEQRES 8 B 268 HIS LEU PRO ARG SER GLU LEU ASP ASP LEU ASP SER ASN
SEQRES 9 B 268 GLN VAL ALA GLU GLU ALA PRO SER ALA ILE VAL ARG VAL
SEQRES 10 B 268 ARG SER SER HIS ILE ILE ASP HIS VAL LEU SER GLU ALA
SEQRES 11 B 268 ARG THR TYR THR CYS VAL GLY ARG THR GLY SER LYS THR
SEQRES 12 B 268 ILE TYR ALA SER THR VAL VAL HIS PRO PRO ARG SER SER
SEQRES 13 B 268 ARG LEU THR PRO GLU LYS THR TYR PRO GLY ALA GLN LYS
SEQRES 14 B 268 PRO ARG ILE ILE TYR THR GLU LYS THR HIS LEU ASP LEU
SEQRES 15 B 268 MSE GLY SER ASN ILE GLN LEU PRO CYS ARG VAL HIS ALA
SEQRES 16 B 268 ARG PRO ARG ALA GLU ILE THR TRP LEU ASN ASN GLU ASN
SEQRES 17 B 268 LYS GLU ILE VAL GLN GLY HIS ARG HIS ARG VAL LEU ALA
SEQRES 18 B 268 ASN GLY ASP LEU LEU ILE SER GLU ILE LYS TRP GLU ASP
SEQRES 19 B 268 MSE GLY ASN TYR LYS CYS ILE ALA ARG ASN VAL VAL GLY
SEQRES 20 B 268 LYS ASP THR ALA ASP THR PHE VAL TYR PRO VAL LEU ASN
SEQRES 21 B 268 GLU GLU ASP GLU VAL LEU PHE GLN
MODRES 4CBP MSE A 57 MET SELENOMETHIONINE
MODRES 4CBP MSE A 58 MET SELENOMETHIONINE
MODRES 4CBP MSE A 162 MET SELENOMETHIONINE
MODRES 4CBP MSE A 214 MET SELENOMETHIONINE
MODRES 4CBP MSE B 57 MET SELENOMETHIONINE
MODRES 4CBP MSE B 58 MET SELENOMETHIONINE
MODRES 4CBP MSE B 162 MET SELENOMETHIONINE
MODRES 4CBP MSE B 214 MET SELENOMETHIONINE
HET MSE A 57 8
HET MSE A 58 8
HET MSE A 162 8
HET MSE A 214 8
HET MSE B 57 8
HET MSE B 58 8
HET MSE B 162 8
HET MSE B 214 8
HET GOL A1240 6
HET GOL A1241 6
HETNAM MSE SELENOMETHIONINE
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 1 MSE 8(C5 H11 N O2 SE)
FORMUL 3 GOL 2(C3 H8 O3)
FORMUL 5 HOH *457(H2 O)
HELIX 1 1 ASN A 25 GLU A 29 5 5
HELIX 2 2 LYS A 210 MSE A 214 5 5
HELIX 3 3 LYS B 210 MSE B 214 5 5
SHEET 1 AA 7 LEU A 33 LYS A 37 0
SHEET 2 AA 7 ILE A 51 SER A 60 1 O GLU A 56 N THR A 36
SHEET 3 AA 7 ILE A 93 ILE A 102 1 O VAL A 94 N GLY A 59
SHEET 4 AA 7 GLN A 147 ASP A 160 -1 O ILE A 152 N SER A 99
SHEET 5 AA 7 LYS A 227 PRO A 236 1 O PHE A 233 N HIS A 158
SHEET 6 AA 7 GLY A 215 ARG A 222 -1 O GLY A 215 N VAL A 234
SHEET 7 AA 7 GLU A 179 LEU A 183 -1 O GLU A 179 N ARG A 222
SHEET 1 AB 5 LEU A 33 LYS A 37 0
SHEET 2 AB 5 ILE A 51 SER A 60 1 O GLU A 56 N THR A 36
SHEET 3 AB 5 ILE A 93 ILE A 102 1 O VAL A 94 N GLY A 59
SHEET 4 AB 5 GLN A 147 ASP A 160 -1 O ILE A 152 N SER A 99
SHEET 5 AB 5 CYS A 170 ARG A 175 -1 O ARG A 171 N ILE A 152
SHEET 1 AC 4 LYS A 42 GLN A 44 0
SHEET 2 AC 4 LYS A 121 HIS A 130 1 O VAL A 128 N LEU A 43
SHEET 3 AC 4 ARG A 110 THR A 118 -1 O ARG A 110 N VAL A 129
SHEET 4 AC 4 SER A 64 VAL A 69 -1 O SER A 64 N ARG A 117
SHEET 1 AD 3 ILE A 166 LEU A 168 0
SHEET 2 AD 3 LEU A 204 ILE A 206 -1 O LEU A 204 N LEU A 168
SHEET 3 AD 3 HIS A 196 VAL A 198 -1 O ARG A 197 N LEU A 205
SHEET 1 BA 7 LEU B 33 LYS B 37 0
SHEET 2 BA 7 ILE B 51 SER B 60 1 O GLU B 56 N THR B 36
SHEET 3 BA 7 ILE B 93 ILE B 102 1 O VAL B 94 N GLY B 59
SHEET 4 BA 7 GLN B 147 LEU B 161 -1 O ILE B 152 N SER B 99
SHEET 5 BA 7 LYS B 227 VAL B 237 1 O PHE B 233 N HIS B 158
SHEET 6 BA 7 GLY B 215 ARG B 222 -1 O GLY B 215 N VAL B 234
SHEET 7 BA 7 GLU B 179 LEU B 183 -1 O GLU B 179 N ARG B 222
SHEET 1 BB 5 LEU B 33 LYS B 37 0
SHEET 2 BB 5 ILE B 51 SER B 60 1 O GLU B 56 N THR B 36
SHEET 3 BB 5 ILE B 93 ILE B 102 1 O VAL B 94 N GLY B 59
SHEET 4 BB 5 GLN B 147 LEU B 161 -1 O ILE B 152 N SER B 99
SHEET 5 BB 5 CYS B 170 ARG B 175 -1 O ARG B 171 N ILE B 152
SHEET 1 BC 4 LYS B 42 GLN B 44 0
SHEET 2 BC 4 LYS B 121 HIS B 130 1 O VAL B 128 N LEU B 43
SHEET 3 BC 4 ARG B 110 THR B 118 -1 O ARG B 110 N VAL B 129
SHEET 4 BC 4 SER B 64 VAL B 69 -1 O SER B 64 N ARG B 117
SHEET 1 BD 3 ILE B 166 LEU B 168 0
SHEET 2 BD 3 LEU B 204 ILE B 206 -1 O LEU B 204 N LEU B 168
SHEET 3 BD 3 HIS B 196 VAL B 198 -1 O ARG B 197 N LEU B 205
SSBOND 1 CYS A 55 CYS A 114 1555 1555 2.02
SSBOND 2 CYS A 170 CYS A 219 1555 1555 2.05
SSBOND 3 CYS B 55 CYS B 114 1555 1555 2.04
SSBOND 4 CYS B 170 CYS B 219 1555 1555 2.05
LINK C GLU A 56 N MSE A 57 1555 1555 1.32
LINK C MSE A 57 N MSE A 58 1555 1555 1.33
LINK C MSE A 58 N GLY A 59 1555 1555 1.32
LINK C LEU A 161 N MSE A 162 1555 1555 1.33
LINK C MSE A 162 N GLY A 163 1555 1555 1.33
LINK C ASP A 213 N MSE A 214 1555 1555 1.33
LINK C MSE A 214 N GLY A 215 1555 1555 1.33
LINK C GLU B 56 N MSE B 57 1555 1555 1.33
LINK C MSE B 57 N MSE B 58 1555 1555 1.33
LINK C MSE B 58 N GLY B 59 1555 1555 1.32
LINK C LEU B 161 N MSE B 162 1555 1555 1.33
LINK C MSE B 162 N GLY B 163 1555 1555 1.33
LINK C ASP B 213 N MSE B 214 1555 1555 1.33
LINK C MSE B 214 N GLY B 215 1555 1555 1.33
CISPEP 1 ALA A 30 ASP A 31 0 0.46
CISPEP 2 ARG A 175 PRO A 176 0 -3.07
CISPEP 3 ARG B 175 PRO B 176 0 -5.35
SITE 1 AC1 4 VAL A 237 HOH A2249 HOH A2251 VAL B 237
SITE 1 AC2 5 ASN A 184 GLU A 189 ILE A 190 VAL A 191
SITE 2 AC2 5 GLY A 193
CRYST1 49.856 99.732 56.280 90.00 91.99 90.00 P 1 21 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 0.020058 0.000000 0.000697 0.00000
SCALE2 0.000000 0.010027 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017779 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 -0.987200 -0.157000 0.029500 7.29400 1
MTRIX2 2 -0.151800 0.979400 0.132900 -10.72200 1
MTRIX3 2 -0.049700 0.126700 -0.990700 118.34840 1
(ATOM LINES ARE NOT SHOWN.)
END
