HEADER CELL ADHESION 03-DEC-15 5F4V
TITLE CRYSTAL STRUCTURE OF THE HUMAN SPERM IZUMO1 RESIDUES 22-268
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: IZUMO SPERM-EGG FUSION PROTEIN 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 22-268;
COMPND 5 SYNONYM: OOCYTE BINDING/FUSION FACTOR,OBF,SPERM-SPECIFIC PROTEIN
COMPND 6 IZUMO;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: IZUMO1;
SOURCE 6 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FRUIT FLY;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7227
KEYWDS GLYCOPROTEIN, MEMBRANE-BOUND, CYSTEINE-RICH, ADHESION, FUSION, CELL
KEYWDS 2 ADHESION
EXPDTA X-RAY DIFFRACTION
AUTHOR H.AYDIN,A.SULTANA,J.E.LEE
REVDAT 6 27-SEP-23 5F4V 1 HETSYN
REVDAT 5 29-JUL-20 5F4V 1 COMPND REMARK HETNAM LINK
REVDAT 5 2 1 SITE
REVDAT 4 28-DEC-16 5F4V 1 TITLE
REVDAT 3 06-JUL-16 5F4V 1 JRNL
REVDAT 2 29-JUN-16 5F4V 1 JRNL
REVDAT 1 15-JUN-16 5F4V 0
JRNL AUTH H.AYDIN,A.SULTANA,S.LI,A.THAVALINGAM,J.E.LEE
JRNL TITL MOLECULAR ARCHITECTURE OF THE HUMAN SPERM IZUMO1 AND EGG
JRNL TITL 2 JUNO FERTILIZATION COMPLEX.
JRNL REF NATURE V. 534 562 2016
JRNL REFN ESSN 1476-4687
JRNL PMID 27309818
JRNL DOI 10.1038/NATURE18595
REMARK 2
REMARK 2 RESOLUTION. 2.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
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) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.60
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 2.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 6482
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.191
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.232
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.660
REMARK 3 FREE R VALUE TEST SET COUNT : 367
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 47.6090 - 4.1822 1.00 2031 129 0.1707 0.2064
REMARK 3 2 4.1822 - 3.3198 1.00 2060 114 0.1895 0.2328
REMARK 3 3 3.3198 - 2.9002 1.00 2024 124 0.2305 0.2966
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
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) : 0.360
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.310
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 49.33
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 : 0.012 1873
REMARK 3 ANGLE : 1.270 2534
REMARK 3 CHIRALITY : 0.055 289
REMARK 3 PLANARITY : 0.006 320
REMARK 3 DIHEDRAL : 15.444 670
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 22 THROUGH 76 )
REMARK 3 ORIGIN FOR THE GROUP (A): 43.5649 45.8374 39.6646
REMARK 3 T TENSOR
REMARK 3 T11: 0.3486 T22: 0.3414
REMARK 3 T33: 0.3354 T12: 0.0051
REMARK 3 T13: -0.0199 T23: 0.0065
REMARK 3 L TENSOR
REMARK 3 L11: 1.8702 L22: 1.2099
REMARK 3 L33: 1.6804 L12: -0.3485
REMARK 3 L13: 1.3998 L23: -1.1245
REMARK 3 S TENSOR
REMARK 3 S11: -0.0756 S12: 0.1544 S13: -0.4615
REMARK 3 S21: -0.0955 S22: 0.1742 S23: 0.3675
REMARK 3 S31: -0.0150 S32: -0.3273 S33: -0.1318
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 77 THROUGH 132 )
REMARK 3 ORIGIN FOR THE GROUP (A): 40.9731 53.3630 45.2007
REMARK 3 T TENSOR
REMARK 3 T11: 0.3198 T22: 0.2641
REMARK 3 T33: 0.2550 T12: -0.0281
REMARK 3 T13: 0.0241 T23: -0.0343
REMARK 3 L TENSOR
REMARK 3 L11: 3.3071 L22: 2.2791
REMARK 3 L33: 2.3714 L12: -1.6930
REMARK 3 L13: 1.0590 L23: -0.7239
REMARK 3 S TENSOR
REMARK 3 S11: 0.0777 S12: -0.2670 S13: 0.0204
REMARK 3 S21: 0.2388 S22: -0.0339 S23: 0.2163
REMARK 3 S31: 0.0777 S32: -0.1476 S33: -0.0762
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 133 THROUGH 256 )
REMARK 3 ORIGIN FOR THE GROUP (A): 32.7244 85.3877 25.2586
REMARK 3 T TENSOR
REMARK 3 T11: 0.3199 T22: 0.3793
REMARK 3 T33: 0.2638 T12: -0.0322
REMARK 3 T13: -0.0284 T23: 0.0117
REMARK 3 L TENSOR
REMARK 3 L11: 1.5719 L22: 3.3587
REMARK 3 L33: 0.9678 L12: -0.0638
REMARK 3 L13: -0.6293 L23: -0.8508
REMARK 3 S TENSOR
REMARK 3 S11: 0.0950 S12: 0.1075 S13: 0.2795
REMARK 3 S21: 0.0576 S22: 0.0570 S23: 0.2423
REMARK 3 S31: -0.1929 S32: -0.0751 S33: -0.1434
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 5F4V COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-DEC-15.
REMARK 100 THE DEPOSITION ID IS D_1000216020.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-APR-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CLSI
REMARK 200 BEAMLINE : 08ID-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97949
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-300
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.5.8
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 6484
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 47.603
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 5.800
REMARK 200 R MERGE (I) : 0.12000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.08
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.80
REMARK 200 R MERGE FOR SHELL (I) : 0.52600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.700
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: 5F4E
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.46
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.83
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.085 M HEPES SODIUM SALT (PH 7.5),
REMARK 280 8.5% (V/V) ISOPROPANOL, 17% (W/V) PEG 4000 AND 15% (V/V)
REMARK 280 GLYCEROL, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 X+2/3,Y+1/3,Z+1/3
REMARK 290 5555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 6555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 7555 X+1/3,Y+2/3,Z+2/3
REMARK 290 8555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 9555 -X+Y+1/3,-X+2/3,Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 60.65000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 35.01629
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 17.80000
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 60.65000
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 35.01629
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 17.80000
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 60.65000
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 35.01629
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 17.80000
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 70.03259
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 35.60000
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 70.03259
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 35.60000
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 70.03259
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 35.60000
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 412 LIES ON A SPECIAL POSITION.
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 ILE A 257
REMARK 465 LYS A 258
REMARK 465 GLU A 259
REMARK 465 GLU A 260
REMARK 465 LYS A 261
REMARK 465 PRO A 262
REMARK 465 SER A 263
REMARK 465 PRO A 264
REMARK 465 ASN A 265
REMARK 465 ILE A 266
REMARK 465 VAL A 267
REMARK 465 THR A 268
REMARK 465 GLY A 269
REMARK 465 ARG A 270
REMARK 465 LEU A 271
REMARK 465 VAL A 272
REMARK 465 PRO A 273
REMARK 465 ARG A 274
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 51 CG CD CE NZ
REMARK 470 ASP A 63 CG OD1 OD2
REMARK 470 ASN A 70 CG OD1 ND2
REMARK 470 GLU A 71 CG CD OE1 OE2
REMARK 470 LYS A 131 CG CD CE NZ
REMARK 470 GLU A 132 CG CD OE1 OE2
REMARK 470 LYS A 153 CG CD CE NZ
REMARK 470 GLN A 174 CG CD OE1 NE2
REMARK 470 GLU A 176 CG CD OE1 OE2
REMARK 470 GLU A 215 CG CD OE1 OE2
REMARK 470 LYS A 220 CG CD CE NZ
REMARK 470 MET A 256 CG SD CE
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 NH1 ARG A 232 OE1 GLU A 234 2.17
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 NZ LYS A 85 OD1 ASN A 239 8655 2.03
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 CYS A 22 CB CYS A 22 SG 0.152
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 ASP A 46 CB - CA - C ANGL. DEV. = -19.7 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 HIS A 44 -3.77 -143.43
REMARK 500 LEU A 69 6.65 85.15
REMARK 500 ASN A 70 -128.16 60.28
REMARK 500 GLU A 132 -32.35 -136.69
REMARK 500 LYS A 161 -168.63 -116.38
REMARK 500 THR A 194 -79.56 -116.41
REMARK 500 MET A 222 56.15 35.74
REMARK 500 SER A 240 -162.56 -163.32
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 GLU A 71 ASP A 72 47.11
REMARK 500 VAL A 238 ASN A 239 -46.62
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5F4E RELATED DB: PDB
REMARK 900 RELATED ID: 5F4Q RELATED DB: PDB
REMARK 900 RELATED ID: 5F4T RELATED DB: PDB
DBREF 5F4V A 22 268 UNP Q8IYV9 IZUM1_HUMAN 22 268
SEQADV 5F4V GLY A 269 UNP Q8IYV9 EXPRESSION TAG
SEQADV 5F4V ARG A 270 UNP Q8IYV9 EXPRESSION TAG
SEQADV 5F4V LEU A 271 UNP Q8IYV9 EXPRESSION TAG
SEQADV 5F4V VAL A 272 UNP Q8IYV9 EXPRESSION TAG
SEQADV 5F4V PRO A 273 UNP Q8IYV9 EXPRESSION TAG
SEQADV 5F4V ARG A 274 UNP Q8IYV9 EXPRESSION TAG
SEQRES 1 A 253 CYS VAL ILE CYS ASP PRO SER VAL VAL LEU ALA LEU LYS
SEQRES 2 A 253 SER LEU GLU LYS ASP TYR LEU PRO GLY HIS LEU ASP ALA
SEQRES 3 A 253 LYS HIS HIS LYS ALA MET MET GLU ARG VAL GLU ASN ALA
SEQRES 4 A 253 VAL LYS ASP PHE GLN GLU LEU SER LEU ASN GLU ASP ALA
SEQRES 5 A 253 TYR MET GLY VAL VAL ASP GLU ALA THR LEU GLN LYS GLY
SEQRES 6 A 253 SER TRP SER LEU LEU LYS ASP LEU LYS ARG ILE THR ASP
SEQRES 7 A 253 SER ASP VAL LYS GLY ASP LEU PHE VAL LYS GLU LEU PHE
SEQRES 8 A 253 TRP MET LEU HIS LEU GLN LYS GLU THR PHE ALA THR TYR
SEQRES 9 A 253 VAL ALA ARG PHE GLN LYS GLU ALA TYR CYS PRO ASN LYS
SEQRES 10 A 253 CYS GLY VAL MET LEU GLN THR LEU ILE TRP CYS LYS ASN
SEQRES 11 A 253 CYS LYS LYS GLU VAL HIS ALA CYS ARG LYS SER TYR ASP
SEQRES 12 A 253 CYS GLY GLU ARG ASN VAL GLU VAL PRO GLN MET GLU ASP
SEQRES 13 A 253 MET ILE LEU ASP CYS GLU LEU ASN TRP HIS GLN ALA SER
SEQRES 14 A 253 GLU GLY LEU THR ASP TYR SER PHE TYR ARG VAL TRP GLY
SEQRES 15 A 253 ASN ASN THR GLU THR LEU VAL SER LYS GLY LYS GLU ALA
SEQRES 16 A 253 THR LEU THR LYS PRO MET VAL GLY PRO GLU ASP ALA GLY
SEQRES 17 A 253 SER TYR ARG CYS GLU LEU GLY SER VAL ASN SER SER PRO
SEQRES 18 A 253 ALA THR ILE ILE ASN PHE HIS VAL THR VAL LEU PRO LYS
SEQRES 19 A 253 MET ILE LYS GLU GLU LYS PRO SER PRO ASN ILE VAL THR
SEQRES 20 A 253 GLY ARG LEU VAL PRO ARG
HET NAG A 301 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
FORMUL 2 NAG C8 H15 N O6
FORMUL 3 HOH *13(H2 O)
HELIX 1 AA1 CYS A 22 CYS A 25 5 4
HELIX 2 AA2 ASP A 26 TYR A 40 1 15
HELIX 3 AA3 LEU A 41 HIS A 44 5 4
HELIX 4 AA4 ASP A 46 ASP A 63 1 18
HELIX 5 AA5 PHE A 64 GLU A 66 5 3
HELIX 6 AA6 GLU A 80 ASP A 101 1 22
HELIX 7 AA7 LYS A 103 ALA A 133 1 31
HELIX 8 AA8 LEU A 184 SER A 190 5 7
HELIX 9 AA9 GLY A 224 ALA A 228 5 5
SHEET 1 AA1 3 VAL A 77 ASP A 79 0
SHEET 2 AA1 3 VAL A 141 TRP A 148 -1 O ILE A 147 N VAL A 78
SHEET 3 AA1 3 LYS A 154 ARG A 160 -1 O HIS A 157 N GLN A 144
SHEET 1 AA2 5 ARG A 168 PRO A 173 0
SHEET 2 AA2 5 SER A 240 LEU A 253 1 O HIS A 249 N ARG A 168
SHEET 3 AA2 5 GLY A 229 SER A 237 -1 N GLY A 229 O VAL A 250
SHEET 4 AA2 5 LEU A 193 VAL A 201 -1 N TYR A 199 O ARG A 232
SHEET 5 AA2 5 GLU A 207 GLY A 213 -1 O VAL A 210 N PHE A 198
SHEET 1 AA3 2 MET A 178 ASP A 181 0
SHEET 2 AA3 2 THR A 217 LYS A 220 -1 O LEU A 218 N LEU A 180
SSBOND 1 CYS A 22 CYS A 149 1555 1555 2.07
SSBOND 2 CYS A 25 CYS A 152 1555 1555 2.05
SSBOND 3 CYS A 135 CYS A 159 1555 1555 2.06
SSBOND 4 CYS A 139 CYS A 165 1555 1555 2.11
SSBOND 5 CYS A 182 CYS A 233 1555 1555 1.93
LINK ND2 ASN A 204 C1 NAG A 301 1555 1555 1.46
CRYST1 121.300 121.300 53.400 90.00 90.00 120.00 H 3 9
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 0.008244 0.004760 0.000000 0.00000
SCALE2 0.000000 0.009519 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018727 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
