HEADER TOXIN/TOXIN RECEPTOR 07-MAR-16 5IMY
TITLE TRAPPED TOXIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: VAGINOLYSIN;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: CD59 GLYCOPROTEIN;
COMPND 7 CHAIN: C, D;
COMPND 8 SYNONYM: 1F5 ANTIGEN,20 KDA HOMOLOGOUS RESTRICTION FACTOR,HRF20,MAC-
COMPND 9 INHIBITORY PROTEIN,MAC-IP,MEM43 ANTIGEN,MEMBRANE ATTACK COMPLEX
COMPND 10 INHIBITION FACTOR,MACIF,MEMBRANE INHIBITOR OF REACTIVE LYSIS,MIRL,
COMPND 11 PROTECTIN;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GARDNERELLA VAGINALIS;
SOURCE 3 ORGANISM_TAXID: 2702;
SOURCE 4 GENE: VLY, VLY;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 9 ORGANISM_COMMON: HUMAN;
SOURCE 10 ORGANISM_TAXID: 9606;
SOURCE 11 GENE: CD59, MIC11, MIN1, MIN2, MIN3, MSK21;
SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 13 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS TOXIN-TOXIN RECEPTOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR S.L.LAWRENCE,C.J.MORTON,M.W.PARKER
REVDAT 3 27-SEP-23 5IMY 1 JRNL REMARK
REVDAT 2 14-SEP-16 5IMY 1 JRNL
REVDAT 1 24-AUG-16 5IMY 0
JRNL AUTH S.L.LAWRENCE,M.A.GORMAN,S.C.FEIL,T.D.MULHERN,M.J.KUIPER,
JRNL AUTH 2 A.J.RATNER,R.K.TWETEN,C.J.MORTON,M.W.PARKER
JRNL TITL STRUCTURAL BASIS FOR RECEPTOR RECOGNITION BY THE HUMAN
JRNL TITL 2 CD59-RESPONSIVE CHOLESTEROL-DEPENDENT CYTOLYSINS.
JRNL REF STRUCTURE V. 24 1488 2016
JRNL REFN ISSN 0969-2126
JRNL PMID 27499440
JRNL DOI 10.1016/J.STR.2016.06.017
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10.1_2155: ???)
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.64
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 93023
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.235
REMARK 3 R VALUE (WORKING SET) : 0.234
REMARK 3 FREE R VALUE : 0.276
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.360
REMARK 3 FREE R VALUE TEST SET COUNT : 3128
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 42.6456 - 6.7166 0.98 4037 138 0.1842 0.2134
REMARK 3 2 6.7166 - 5.3344 0.99 4096 140 0.2024 0.2270
REMARK 3 3 5.3344 - 4.6611 0.98 4017 137 0.1653 0.2010
REMARK 3 4 4.6611 - 4.2353 0.98 4072 136 0.1748 0.2358
REMARK 3 5 4.2353 - 3.9320 0.99 4087 150 0.1947 0.2630
REMARK 3 6 3.9320 - 3.7003 0.99 4080 142 0.2179 0.3006
REMARK 3 7 3.7003 - 3.5151 0.99 4101 144 0.2288 0.2426
REMARK 3 8 3.5151 - 3.3621 0.99 4074 143 0.2364 0.2939
REMARK 3 9 3.3621 - 3.2327 0.99 4100 145 0.2471 0.2549
REMARK 3 10 3.2327 - 3.1212 1.00 4103 142 0.2640 0.3302
REMARK 3 11 3.1212 - 3.0237 0.99 4093 145 0.2883 0.3457
REMARK 3 12 3.0237 - 2.9372 1.00 4102 145 0.2947 0.3187
REMARK 3 13 2.9372 - 2.8599 0.99 4084 143 0.2974 0.2821
REMARK 3 14 2.8599 - 2.7902 0.99 4095 143 0.3030 0.3578
REMARK 3 15 2.7902 - 2.7268 1.00 4079 141 0.3051 0.3477
REMARK 3 16 2.7268 - 2.6687 0.99 4106 139 0.3150 0.3795
REMARK 3 17 2.6687 - 2.6154 0.99 4117 143 0.3206 0.3585
REMARK 3 18 2.6154 - 2.5660 0.99 4067 140 0.3228 0.3432
REMARK 3 19 2.5660 - 2.5202 0.99 4156 148 0.3385 0.3724
REMARK 3 20 2.5202 - 2.4775 0.99 4007 140 0.3407 0.3505
REMARK 3 21 2.4775 - 2.4375 0.99 4119 145 0.3398 0.3970
REMARK 3 22 2.4375 - 2.4000 0.99 4103 139 0.3499 0.3734
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.400
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.710
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
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 : 0.003 8869
REMARK 3 ANGLE : 0.716 12059
REMARK 3 CHIRALITY : 0.045 1336
REMARK 3 PLANARITY : 0.004 1561
REMARK 3 DIHEDRAL : 15.191 5341
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 5IMY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-MAR-16.
REMARK 100 THE DEPOSITION ID IS D_1000219096.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-DEC-15
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 : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9537
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 49244
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 48.315
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 4.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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 : 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: 1S3R
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.45
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM ACETATE, PEG 10000, BIS-TRIS,
REMARK 280 MAGNESIUM CHLORIDE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 293K
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 40.94700
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 70.85650
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 40.94700
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 70.85650
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7500 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 51140 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, D, 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 SER A 27
REMARK 465 ASN A 28
REMARK 465 ALA A 29
REMARK 465 HIS A 30
REMARK 465 MET A 31
REMARK 465 ALA A 32
REMARK 465 PRO A 33
REMARK 465 SER A 34
REMARK 465 ALA A 35
REMARK 465 LYS A 36
REMARK 465 ASP A 37
REMARK 465 SER A 38
REMARK 465 GLU A 39
REMARK 465 PRO A 40
REMARK 465 ALA A 41
REMARK 465 ASP A 516
REMARK 465 SER B 27
REMARK 465 ASN B 28
REMARK 465 ALA B 29
REMARK 465 HIS B 30
REMARK 465 MET B 31
REMARK 465 ALA B 32
REMARK 465 PRO B 33
REMARK 465 SER B 34
REMARK 465 ALA B 35
REMARK 465 LYS B 36
REMARK 465 ASP B 37
REMARK 465 SER B 38
REMARK 465 GLU B 39
REMARK 465 PRO B 40
REMARK 465 ALA B 41
REMARK 465 THR B 42
REMARK 465 SER B 43
REMARK 465 ASP B 516
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 ASP C 22 CG OD1 OD2
REMARK 470 ASP D 22 CG OD1 OD2
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 O PHE D 47 HG1 THR D 51 1.36
REMARK 500 H GLN B 59 OD1 ASN B 275 1.43
REMARK 500 O THR B 264 HG SER B 267 1.48
REMARK 500 HG SER A 301 O THR A 302 1.50
REMARK 500 OE1 GLU B 479 HE ARG B 482 1.52
REMARK 500 O PRO A 319 H THR A 321 1.54
REMARK 500 O PRO A 149 HE1 TRP A 179 1.60
REMARK 500 OE1 GLU B 316 O HOH B 601 1.90
REMARK 500 O PHE D 47 OG1 THR D 51 1.96
REMARK 500 NZ LYS B 62 OD2 ASP B 383 2.04
REMARK 500 O ASN A 454 O HOH A 601 2.05
REMARK 500 O GLU B 155 O HOH B 602 2.05
REMARK 500 O ALA A 45 N LYS A 47 2.08
REMARK 500 O ASN A 445 O HOH A 602 2.10
REMARK 500 NZ LYS B 178 O HOH B 602 2.11
REMARK 500 OH TYR C 62 O HOH C 101 2.12
REMARK 500 O THR B 264 OG SER B 267 2.12
REMARK 500 OD1 ASP B 296 O HOH B 603 2.13
REMARK 500 O ASP A 266 ND2 ASN A 270 2.16
REMARK 500 N GLN B 59 OD1 ASN B 275 2.16
REMARK 500 O ALA A 341 N GLY A 343 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 HH22 ARG A 162 OD2 ASP B 353 3646 1.46
REMARK 500 NH2 ARG A 162 OD2 ASP B 353 3646 2.14
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 SER A 43 -110.32 -174.96
REMARK 500 CYS A 44 -167.33 -75.70
REMARK 500 ALA A 45 -125.64 83.75
REMARK 500 ALA A 46 -67.97 41.82
REMARK 500 LYS A 76 139.60 -10.32
REMARK 500 ASN A 85 -92.10 27.29
REMARK 500 GLU A 87 102.71 19.16
REMARK 500 ASP A 124 -162.47 -128.71
REMARK 500 ASP A 147 41.80 -94.24
REMARK 500 PHE A 151 159.37 63.11
REMARK 500 ARG A 162 89.78 59.79
REMARK 500 SER A 186 -88.74 -74.50
REMARK 500 LYS A 216 -56.41 85.50
REMARK 500 LYS A 222 69.89 34.56
REMARK 500 ASP A 253 -58.93 64.82
REMARK 500 ASP A 257 167.42 67.63
REMARK 500 PHE A 258 -43.92 88.42
REMARK 500 CYS A 262 67.66 -105.28
REMARK 500 THR A 264 129.78 48.28
REMARK 500 ARG A 271 -12.74 118.11
REMARK 500 VAL A 282 99.98 -68.51
REMARK 500 THR A 302 -173.04 -66.45
REMARK 500 ASP A 303 -2.26 65.77
REMARK 500 VAL A 315 133.29 64.99
REMARK 500 GLU A 316 78.02 -62.62
REMARK 500 ILE A 317 58.46 -64.86
REMARK 500 LYS A 318 126.38 152.67
REMARK 500 PRO A 319 87.59 8.08
REMARK 500 ASN A 320 54.85 -52.71
REMARK 500 THR A 321 -72.00 -152.56
REMARK 500 GLU A 322 -100.01 -39.60
REMARK 500 SER A 340 32.65 -93.54
REMARK 500 ASN A 342 -54.42 0.91
REMARK 500 ALA A 344 24.67 -155.65
REMARK 500 ALA A 345 -64.10 75.99
REMARK 500 LYS A 346 -96.89 151.94
REMARK 500 CYS A 348 115.71 73.05
REMARK 500 THR A 349 133.13 -175.97
REMARK 500 SER A 366 35.80 -75.62
REMARK 500 THR A 367 36.46 13.52
REMARK 500 SER A 368 -18.57 -145.12
REMARK 500 ASP A 432 -100.43 -68.73
REMARK 500 ASN A 445 -92.62 -78.64
REMARK 500 ALA A 451 -116.81 43.89
REMARK 500 VAL A 471 146.10 55.34
REMARK 500 TRP A 478 -26.57 136.95
REMARK 500 TYR A 485 100.05 52.82
REMARK 500 TRP A 501 -158.93 -150.38
REMARK 500 VAL A 513 168.79 45.44
REMARK 500 GLU C 73 0.49 -69.11
REMARK 500
REMARK 500 THIS ENTRY HAS 104 RAMACHANDRAN OUTLIERS.
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 ASP A 257 PHE A 258 -134.03
REMARK 500 ASP B 49 SER B 50 149.20
REMARK 500
REMARK 500 REMARK: NULL
DBREF 5IMY A 29 516 UNP B2YGA4 B2YGA4_GARVA 29 516
DBREF 5IMY C 1 77 UNP P13987 CD59_HUMAN 26 102
DBREF 5IMY D 1 77 UNP P13987 CD59_HUMAN 26 102
DBREF 5IMY B 29 516 UNP B2YGA4 B2YGA4_GARVA 29 516
SEQADV 5IMY SER A 27 UNP B2YGA4 EXPRESSION TAG
SEQADV 5IMY ASN A 28 UNP B2YGA4 EXPRESSION TAG
SEQADV 5IMY HIS A 30 UNP B2YGA4 MET 30 CONFLICT
SEQADV 5IMY MET A 31 UNP B2YGA4 ALA 31 CONFLICT
SEQADV 5IMY CYS A 333 UNP B2YGA4 THR 333 CONFLICT
SEQADV 5IMY CYS A 348 UNP B2YGA4 ILE 348 CONFLICT
SEQADV 5IMY MET C 0 UNP P13987 INITIATING METHIONINE
SEQADV 5IMY MET D 0 UNP P13987 INITIATING METHIONINE
SEQADV 5IMY SER B 27 UNP B2YGA4 EXPRESSION TAG
SEQADV 5IMY ASN B 28 UNP B2YGA4 EXPRESSION TAG
SEQADV 5IMY HIS B 30 UNP B2YGA4 MET 30 CONFLICT
SEQADV 5IMY MET B 31 UNP B2YGA4 ALA 31 CONFLICT
SEQADV 5IMY CYS B 333 UNP B2YGA4 THR 333 CONFLICT
SEQADV 5IMY CYS B 348 UNP B2YGA4 ILE 348 CONFLICT
SEQRES 1 A 490 SER ASN ALA HIS MET ALA PRO SER ALA LYS ASP SER GLU
SEQRES 2 A 490 PRO ALA THR SER CYS ALA ALA LYS LYS ASP SER LEU ASN
SEQRES 3 A 490 ASN TYR LEU TRP ASP LEU GLN TYR ASP LYS THR ASN ILE
SEQRES 4 A 490 LEU ALA ARG HIS GLY GLU THR ILE GLU ASN LYS PHE SER
SEQRES 5 A 490 SER ASP SER PHE ASN LYS ASN GLY GLU PHE VAL VAL VAL
SEQRES 6 A 490 GLU HIS GLN LYS LYS ASN ILE THR ASN THR THR SER ASN
SEQRES 7 A 490 LEU SER VAL THR SER ALA ASN ASP ASP ARG VAL TYR PRO
SEQRES 8 A 490 GLY ALA LEU PHE ARG ALA ASP LYS ASN LEU MET ASP ASN
SEQRES 9 A 490 MET PRO SER LEU ILE SER ALA ASN ARG ALA PRO ILE THR
SEQRES 10 A 490 LEU SER VAL ASP LEU PRO GLY PHE HIS GLY GLY GLU SER
SEQRES 11 A 490 ALA VAL THR VAL GLN ARG PRO THR LYS SER SER VAL THR
SEQRES 12 A 490 SER ALA VAL ASN GLY LEU VAL SER LYS TRP ASN ALA GLN
SEQRES 13 A 490 TYR GLY ALA SER HIS HIS VAL ALA ALA ARG MET GLN TYR
SEQRES 14 A 490 ASP SER ALA SER ALA GLN SER MET ASN GLN LEU LYS ALA
SEQRES 15 A 490 LYS PHE GLY ALA ASP PHE ALA LYS ILE GLY VAL PRO LEU
SEQRES 16 A 490 LYS ILE ASP PHE ASP ALA VAL HIS LYS GLY GLU LYS GLN
SEQRES 17 A 490 THR GLN ILE VAL ASN PHE LYS GLN THR TYR TYR THR VAL
SEQRES 18 A 490 SER VAL ASP ALA PRO ASP SER PRO ALA ASP PHE PHE ALA
SEQRES 19 A 490 PRO CYS THR THR PRO ASP SER LEU LYS ASN ARG GLY VAL
SEQRES 20 A 490 ASP ASN LYS ARG PRO PRO VAL TYR VAL SER ASN VAL ALA
SEQRES 21 A 490 TYR GLY ARG SER MET TYR VAL LYS PHE ASP THR THR SER
SEQRES 22 A 490 LYS SER THR ASP PHE GLN ALA ALA VAL GLU ALA ALA ILE
SEQRES 23 A 490 LYS GLY VAL GLU ILE LYS PRO ASN THR GLU PHE HIS ARG
SEQRES 24 A 490 ILE LEU GLN ASN THR SER VAL CYS ALA VAL ILE LEU GLY
SEQRES 25 A 490 GLY SER ALA ASN GLY ALA ALA LYS VAL CYS THR GLY ASN
SEQRES 26 A 490 ILE ASP THR LEU LYS ALA LEU ILE GLN GLU GLY ALA ASN
SEQRES 27 A 490 LEU SER THR SER SER PRO ALA VAL PRO ILE ALA TYR THR
SEQRES 28 A 490 THR SER PHE VAL LYS ASP ASN GLU VAL ALA THR LEU GLN
SEQRES 29 A 490 SER ASN SER ASP TYR ILE GLU THR LYS VAL SER SER TYR
SEQRES 30 A 490 ARG ASN GLY TYR LEU THR LEU ASP HIS ARG GLY ALA TYR
SEQRES 31 A 490 VAL ALA ARG TYR TYR ILE TYR TRP ASP GLU TYR GLY THR
SEQRES 32 A 490 GLU ILE ASP GLY THR PRO TYR VAL ARG SER ARG ALA TRP
SEQRES 33 A 490 GLU GLY ASN GLY LYS TYR ARG THR ALA HIS PHE ASN THR
SEQRES 34 A 490 THR ILE GLN PHE LYS GLY ASN VAL ARG ASN LEU ARG ILE
SEQRES 35 A 490 LYS LEU VAL GLU LYS THR GLY LEU VAL TRP GLU PRO TRP
SEQRES 36 A 490 ARG THR VAL TYR ASP ARG SER ASP LEU PRO LEU VAL ARG
SEQRES 37 A 490 GLN ARG THR ILE SER ASN TRP GLY THR THR LEU TRP PRO
SEQRES 38 A 490 ARG VAL ALA GLU THR VAL LYS ASN ASP
SEQRES 1 C 78 MET LEU GLN CYS TYR ASN CYS PRO ASN PRO THR ALA ASP
SEQRES 2 C 78 CYS LYS THR ALA VAL ASN CYS SER SER ASP PHE ASP ALA
SEQRES 3 C 78 CYS LEU ILE THR LYS ALA GLY LEU GLN VAL TYR ASN LYS
SEQRES 4 C 78 CYS TRP LYS PHE GLU HIS CYS ASN PHE ASN ASP VAL THR
SEQRES 5 C 78 THR ARG LEU ARG GLU ASN GLU LEU THR TYR TYR CYS CYS
SEQRES 6 C 78 LYS LYS ASP LEU CYS ASN PHE ASN GLU GLN LEU GLU ASN
SEQRES 1 D 78 MET LEU GLN CYS TYR ASN CYS PRO ASN PRO THR ALA ASP
SEQRES 2 D 78 CYS LYS THR ALA VAL ASN CYS SER SER ASP PHE ASP ALA
SEQRES 3 D 78 CYS LEU ILE THR LYS ALA GLY LEU GLN VAL TYR ASN LYS
SEQRES 4 D 78 CYS TRP LYS PHE GLU HIS CYS ASN PHE ASN ASP VAL THR
SEQRES 5 D 78 THR ARG LEU ARG GLU ASN GLU LEU THR TYR TYR CYS CYS
SEQRES 6 D 78 LYS LYS ASP LEU CYS ASN PHE ASN GLU GLN LEU GLU ASN
SEQRES 1 B 490 SER ASN ALA HIS MET ALA PRO SER ALA LYS ASP SER GLU
SEQRES 2 B 490 PRO ALA THR SER CYS ALA ALA LYS LYS ASP SER LEU ASN
SEQRES 3 B 490 ASN TYR LEU TRP ASP LEU GLN TYR ASP LYS THR ASN ILE
SEQRES 4 B 490 LEU ALA ARG HIS GLY GLU THR ILE GLU ASN LYS PHE SER
SEQRES 5 B 490 SER ASP SER PHE ASN LYS ASN GLY GLU PHE VAL VAL VAL
SEQRES 6 B 490 GLU HIS GLN LYS LYS ASN ILE THR ASN THR THR SER ASN
SEQRES 7 B 490 LEU SER VAL THR SER ALA ASN ASP ASP ARG VAL TYR PRO
SEQRES 8 B 490 GLY ALA LEU PHE ARG ALA ASP LYS ASN LEU MET ASP ASN
SEQRES 9 B 490 MET PRO SER LEU ILE SER ALA ASN ARG ALA PRO ILE THR
SEQRES 10 B 490 LEU SER VAL ASP LEU PRO GLY PHE HIS GLY GLY GLU SER
SEQRES 11 B 490 ALA VAL THR VAL GLN ARG PRO THR LYS SER SER VAL THR
SEQRES 12 B 490 SER ALA VAL ASN GLY LEU VAL SER LYS TRP ASN ALA GLN
SEQRES 13 B 490 TYR GLY ALA SER HIS HIS VAL ALA ALA ARG MET GLN TYR
SEQRES 14 B 490 ASP SER ALA SER ALA GLN SER MET ASN GLN LEU LYS ALA
SEQRES 15 B 490 LYS PHE GLY ALA ASP PHE ALA LYS ILE GLY VAL PRO LEU
SEQRES 16 B 490 LYS ILE ASP PHE ASP ALA VAL HIS LYS GLY GLU LYS GLN
SEQRES 17 B 490 THR GLN ILE VAL ASN PHE LYS GLN THR TYR TYR THR VAL
SEQRES 18 B 490 SER VAL ASP ALA PRO ASP SER PRO ALA ASP PHE PHE ALA
SEQRES 19 B 490 PRO CYS THR THR PRO ASP SER LEU LYS ASN ARG GLY VAL
SEQRES 20 B 490 ASP ASN LYS ARG PRO PRO VAL TYR VAL SER ASN VAL ALA
SEQRES 21 B 490 TYR GLY ARG SER MET TYR VAL LYS PHE ASP THR THR SER
SEQRES 22 B 490 LYS SER THR ASP PHE GLN ALA ALA VAL GLU ALA ALA ILE
SEQRES 23 B 490 LYS GLY VAL GLU ILE LYS PRO ASN THR GLU PHE HIS ARG
SEQRES 24 B 490 ILE LEU GLN ASN THR SER VAL CYS ALA VAL ILE LEU GLY
SEQRES 25 B 490 GLY SER ALA ASN GLY ALA ALA LYS VAL CYS THR GLY ASN
SEQRES 26 B 490 ILE ASP THR LEU LYS ALA LEU ILE GLN GLU GLY ALA ASN
SEQRES 27 B 490 LEU SER THR SER SER PRO ALA VAL PRO ILE ALA TYR THR
SEQRES 28 B 490 THR SER PHE VAL LYS ASP ASN GLU VAL ALA THR LEU GLN
SEQRES 29 B 490 SER ASN SER ASP TYR ILE GLU THR LYS VAL SER SER TYR
SEQRES 30 B 490 ARG ASN GLY TYR LEU THR LEU ASP HIS ARG GLY ALA TYR
SEQRES 31 B 490 VAL ALA ARG TYR TYR ILE TYR TRP ASP GLU TYR GLY THR
SEQRES 32 B 490 GLU ILE ASP GLY THR PRO TYR VAL ARG SER ARG ALA TRP
SEQRES 33 B 490 GLU GLY ASN GLY LYS TYR ARG THR ALA HIS PHE ASN THR
SEQRES 34 B 490 THR ILE GLN PHE LYS GLY ASN VAL ARG ASN LEU ARG ILE
SEQRES 35 B 490 LYS LEU VAL GLU LYS THR GLY LEU VAL TRP GLU PRO TRP
SEQRES 36 B 490 ARG THR VAL TYR ASP ARG SER ASP LEU PRO LEU VAL ARG
SEQRES 37 B 490 GLN ARG THR ILE SER ASN TRP GLY THR THR LEU TRP PRO
SEQRES 38 B 490 ARG VAL ALA GLU THR VAL LYS ASN ASP
FORMUL 5 HOH *137(H2 O)
HELIX 1 AA1 LYS A 47 ASP A 57 1 11
HELIX 2 AA2 THR A 63 ILE A 65 5 3
HELIX 3 AA3 ASN A 111 VAL A 115 5 5
HELIX 4 AA4 ASP A 124 ASP A 129 1 6
HELIX 5 AA5 THR A 164 GLY A 184 1 21
HELIX 6 AA6 SER A 202 GLY A 211 1 10
HELIX 7 AA7 ASP A 213 GLY A 218 1 6
HELIX 8 AA8 VAL A 219 LYS A 222 5 4
HELIX 9 AA9 ASP A 224 LYS A 230 1 7
HELIX 10 AB1 PRO A 265 ASN A 270 1 6
HELIX 11 AB2 ASP A 303 LYS A 313 1 11
HELIX 12 AB3 PHE A 323 GLN A 328 1 6
HELIX 13 AB4 ASN A 351 GLY A 362 1 12
HELIX 14 AB5 LYS C 41 CYS C 45 5 5
HELIX 15 AB6 ASN C 46 ARG C 55 1 10
HELIX 16 AB7 PHE C 71 LEU C 75 5 5
HELIX 17 AB8 LYS D 41 CYS D 45 5 5
HELIX 18 AB9 ASN D 46 ARG D 55 1 10
HELIX 19 AC1 PHE D 71 LEU D 75 5 5
HELIX 20 AC2 THR B 108 ASP B 113 1 6
HELIX 21 AC3 ASP B 124 ASP B 129 1 6
HELIX 22 AC4 THR B 164 TYR B 183 1 20
HELIX 23 AC5 SER B 202 GLY B 211 1 10
HELIX 24 AC6 ASP B 213 GLY B 218 1 6
HELIX 25 AC7 PHE B 225 LYS B 230 1 6
HELIX 26 AC8 THR B 264 LYS B 269 1 6
HELIX 27 AC9 ASP B 303 LYS B 313 1 11
HELIX 28 AD1 THR B 321 GLN B 328 1 8
HELIX 29 AD2 ASN B 351 ALA B 363 1 13
SHEET 1 AA1 4 ALA A 67 HIS A 69 0
SHEET 2 AA1 4 LEU A 389 TYR A 403 1 O GLN A 390 N ARG A 68
SHEET 3 AA1 4 PHE A 88 THR A 102 -1 N ASN A 100 O SER A 391
SHEET 4 AA1 4 PHE A 77 ASN A 83 -1 N SER A 78 O HIS A 93
SHEET 1 AA2 5 LEU A 105 SER A 106 0
SHEET 2 AA2 5 PRO A 373 PHE A 380 -1 O TYR A 376 N LEU A 105
SHEET 3 AA2 5 PRO A 279 THR A 297 -1 N TYR A 281 O SER A 379
SHEET 4 AA2 5 GLN A 234 VAL A 249 -1 N GLN A 236 O PHE A 295
SHEET 5 AA2 5 ARG A 192 SER A 199 -1 N ALA A 198 O ILE A 237
SHEET 1 AA3 4 ARG A 192 SER A 199 0
SHEET 2 AA3 4 GLN A 234 VAL A 249 -1 O ILE A 237 N ALA A 198
SHEET 3 AA3 4 ILE A 142 VAL A 146 -1 N SER A 145 O SER A 248
SHEET 4 AA3 4 ALA A 157 VAL A 160 -1 O VAL A 158 N LEU A 144
SHEET 1 AA4 3 LEU A 120 ARG A 122 0
SHEET 2 AA4 3 PRO A 279 THR A 297 -1 O VAL A 280 N PHE A 121
SHEET 3 AA4 3 SER A 331 LEU A 337 -1 O CYS A 333 N LYS A 294
SHEET 1 AA5 4 HIS A 452 PHE A 459 0
SHEET 2 AA5 4 GLY A 406 ALA A 415 -1 N LEU A 408 O ILE A 457
SHEET 3 AA5 4 GLN A 495 THR A 503 1 O ARG A 496 N THR A 409
SHEET 4 AA5 4 TRP A 506 GLU A 511 -1 O ARG A 508 N TRP A 501
SHEET 1 AA6 7 ASP A 486 LEU A 490 0
SHEET 2 AA6 7 ARG A 464 LYS A 469 -1 N ILE A 468 O ARG A 487
SHEET 3 AA6 7 TYR A 421 THR A 429 -1 N ASP A 425 O ARG A 464
SHEET 4 AA6 7 PRO A 435 ALA A 441 -1 O TYR A 436 N GLY A 428
SHEET 5 AA6 7 THR C 60 CYS C 64 -1 O TYR C 61 N SER A 439
SHEET 6 AA6 7 ALA C 25 ALA C 31 -1 N ILE C 28 O TYR C 62
SHEET 7 AA6 7 GLN C 34 TRP C 40 -1 O LYS C 38 N LEU C 27
SHEET 1 AA7 2 GLN C 2 TYR C 4 0
SHEET 2 AA7 2 ALA C 16 ASN C 18 -1 O VAL C 17 N CYS C 3
SHEET 1 AA8 2 GLN D 2 TYR D 4 0
SHEET 2 AA8 2 ALA D 16 ASN D 18 -1 O VAL D 17 N CYS D 3
SHEET 1 AA9 7 GLN D 34 TRP D 40 0
SHEET 2 AA9 7 ALA D 25 ALA D 31 -1 N ALA D 31 O GLN D 34
SHEET 3 AA9 7 THR D 60 CYS D 64 -1 O THR D 60 N LYS D 30
SHEET 4 AA9 7 PRO B 435 ALA B 441 -1 O SER B 439 N TYR D 61
SHEET 5 AA9 7 VAL B 417 THR B 429 -1 N TRP B 424 O ARG B 440
SHEET 6 AA9 7 ARG B 464 LYS B 473 -1 O ARG B 464 N ASP B 425
SHEET 7 AA9 7 THR B 483 LEU B 490 -1 O TYR B 485 N LEU B 470
SHEET 1 AB1 4 ALA B 67 HIS B 69 0
SHEET 2 AB1 4 LEU B 389 SER B 401 1 O GLN B 390 N ARG B 68
SHEET 3 AB1 4 VAL B 90 THR B 102 -1 N GLN B 94 O GLU B 397
SHEET 4 AB1 4 PHE B 77 SER B 81 -1 N ASP B 80 O VAL B 91
SHEET 1 AB2 5 LEU B 105 SER B 106 0
SHEET 2 AB2 5 PRO B 373 PHE B 380 -1 O TYR B 376 N LEU B 105
SHEET 3 AB2 5 PRO B 279 THR B 297 -1 N ALA B 286 O ILE B 374
SHEET 4 AB2 5 GLN B 234 VAL B 249 -1 N GLN B 236 O PHE B 295
SHEET 5 AB2 5 ARG B 192 SER B 199 -1 N ALA B 198 O ILE B 237
SHEET 1 AB3 4 ARG B 192 SER B 199 0
SHEET 2 AB3 4 GLN B 234 VAL B 249 -1 O ILE B 237 N ALA B 198
SHEET 3 AB3 4 ILE B 142 VAL B 146 -1 N SER B 145 O SER B 248
SHEET 4 AB3 4 ALA B 157 VAL B 160 -1 O VAL B 158 N LEU B 144
SHEET 1 AB4 3 LEU B 120 ARG B 122 0
SHEET 2 AB4 3 PRO B 279 THR B 297 -1 O VAL B 280 N PHE B 121
SHEET 3 AB4 3 SER B 331 ILE B 336 -1 O SER B 331 N ASP B 296
SHEET 1 AB5 4 PHE B 453 PHE B 459 0
SHEET 2 AB5 4 GLY B 406 HIS B 412 -1 N HIS B 412 O PHE B 453
SHEET 3 AB5 4 GLN B 495 GLY B 502 1 O ARG B 496 N THR B 409
SHEET 4 AB5 4 PRO B 507 LYS B 514 -1 O ARG B 508 N TRP B 501
SSBOND 1 CYS A 44 CYS A 262 1555 1555 2.04
SSBOND 2 CYS A 333 CYS A 348 1555 1555 2.03
SSBOND 3 CYS C 3 CYS C 26 1555 1555 2.02
SSBOND 4 CYS C 6 CYS C 13 1555 1555 2.03
SSBOND 5 CYS C 19 CYS C 39 1555 1555 2.03
SSBOND 6 CYS C 45 CYS C 63 1555 1555 2.03
SSBOND 7 CYS C 64 CYS C 69 1555 1555 2.03
SSBOND 8 CYS D 3 CYS D 26 1555 1555 2.01
SSBOND 9 CYS D 6 CYS D 13 1555 1555 2.03
SSBOND 10 CYS D 19 CYS D 39 1555 1555 2.03
SSBOND 11 CYS D 45 CYS D 63 1555 1555 2.03
SSBOND 12 CYS D 64 CYS D 69 1555 1555 2.03
SSBOND 13 CYS B 44 CYS B 262 1555 1555 2.03
SSBOND 14 CYS B 333 CYS B 348 1555 1555 2.02
CISPEP 1 LYS A 318 PRO A 319 0 13.56
CISPEP 2 PRO A 370 ALA A 371 0 10.99
CISPEP 3 PRO B 370 ALA B 371 0 -0.36
CRYST1 81.894 141.713 106.732 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 0.012211 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007057 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009369 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
