HEADER PROTEIN BINDING 28-NOV-13 4NSO
TITLE CRYSTAL STRUCTURE OF THE EFFECTOR-IMMUNITY PROTEIN COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EFFECTOR PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 731-981;
COMPND 5 SYNONYM: VGRG PROTEIN;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: IMMUNITY PROTEIN;
COMPND 9 CHAIN: B;
COMPND 10 FRAGMENT: UNP RESIDUES 26-122;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: VIBRIO CHOLERAE O1 BIOVAR EL TOR;
SOURCE 3 ORGANISM_TAXID: 243277;
SOURCE 4 STRAIN: N16961;
SOURCE 5 GENE: VCPCS023_003519, VC_A0123;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: VIBRIO CHOLERAE O1 BIOVAR EL TOR;
SOURCE 10 ORGANISM_TAXID: 243277;
SOURCE 11 STRAIN: N16961;
SOURCE 12 GENE: VC_A0124;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HELIX, PEPTIDOGLYCAN, PROTEIN BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR C.DONG
REVDAT 3 11-JUN-14 4NSO 1 JRNL
REVDAT 2 21-MAY-14 4NSO 1 JRNL
REVDAT 1 16-APR-14 4NSO 0
JRNL AUTH J.ZHANG,H.ZHANG,Z.GAO,H.HU,C.DONG,Y.H.DONG
JRNL TITL STRUCTURAL BASIS FOR RECOGNITION OF THE TYPE VI SPIKE
JRNL TITL 2 PROTEIN VGRG3 BY A COGNATE IMMUNITY PROTEIN.
JRNL REF FEBS LETT. V. 588 1891 2014
JRNL REFN ISSN 0014-5793
JRNL PMID 24751834
JRNL DOI 10.1016/J.FEBSLET.2014.04.016
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7.3_928)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : MLHL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.16
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.8
REMARK 3 NUMBER OF REFLECTIONS : 18466
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.220
REMARK 3 R VALUE (WORKING SET) : 0.215
REMARK 3 FREE R VALUE : 0.259
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1847
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 38.1701 - 5.6377 0.99 1356 149 0.2049 0.2417
REMARK 3 2 5.6377 - 4.4770 0.99 1330 148 0.1772 0.2055
REMARK 3 3 4.4770 - 3.9117 0.99 1311 147 0.1710 0.2090
REMARK 3 4 3.9117 - 3.5544 0.98 1297 145 0.2161 0.2683
REMARK 3 5 3.5544 - 3.2998 0.97 1291 144 0.2308 0.2419
REMARK 3 6 3.2998 - 3.1053 0.99 1289 145 0.2266 0.2754
REMARK 3 7 3.1053 - 2.9498 0.98 1292 144 0.2210 0.2919
REMARK 3 8 2.9498 - 2.8215 0.98 1301 146 0.2388 0.2889
REMARK 3 9 2.8215 - 2.7129 0.97 1270 142 0.2457 0.3072
REMARK 3 10 2.7129 - 2.6193 0.96 1253 140 0.2505 0.3265
REMARK 3 11 2.6193 - 2.5374 0.96 1261 143 0.2680 0.3306
REMARK 3 12 2.5374 - 2.4649 0.94 1241 132 0.2837 0.3633
REMARK 3 13 2.4649 - 2.4000 0.87 1127 122 0.3104 0.3576
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 : 0.73
REMARK 3 K_SOL : 0.30
REMARK 3 B_SOL : 34.44
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.360
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.750
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) : -9.49640
REMARK 3 B22 (A**2) : 10.02300
REMARK 3 B33 (A**2) : -0.52660
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 7.31880
REMARK 3 B23 (A**2) : 0.00000
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 : 0.009 2390
REMARK 3 ANGLE : 1.048 3218
REMARK 3 CHIRALITY : 0.076 343
REMARK 3 PLANARITY : 0.006 415
REMARK 3 DIHEDRAL : 14.828 890
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: all
REMARK 3 ORIGIN FOR THE GROUP (A): 42.9516 47.7970 36.6877
REMARK 3 T TENSOR
REMARK 3 T11: 0.3119 T22: 0.3100
REMARK 3 T33: 0.1917 T12: -0.0354
REMARK 3 T13: -0.0265 T23: 0.0454
REMARK 3 L TENSOR
REMARK 3 L11: 4.0665 L22: 0.8748
REMARK 3 L33: 1.8228 L12: -0.1037
REMARK 3 L13: -1.4440 L23: 0.0681
REMARK 3 S TENSOR
REMARK 3 S11: -0.1215 S12: 0.2736 S13: -0.1459
REMARK 3 S21: -0.0588 S22: 0.1283 S23: 0.1587
REMARK 3 S31: 0.1983 S32: -0.3371 S33: -0.0025
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 4NSO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-DEC-13.
REMARK 100 THE RCSB ID CODE IS RCSB083606.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-OCT-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BSRF
REMARK 200 BEAMLINE : 3W1A
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 : DOUBLE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19076
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : 7.500
REMARK 200 R MERGE (I) : 0.07300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.1
REMARK 200 DATA REDUNDANCY IN SHELL : 6.10
REMARK 200 R MERGE FOR SHELL (I) : 0.54800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.25
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.63
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1MM HEPES PH7.6, 12%(W/V)PEG3350,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
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 66.81550
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.33000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 66.81550
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 39.33000
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 300 REMARK: THE SECOND PART OF THE BIOLOGICAL ASSEMBLY IS GENERATED BY
REMARK 300 THE TWO FOLD AXIS: -X+1,Y,-Z+1
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: 8290 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26710 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.0 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 350 BIOMT1 2 -1.000000 0.000000 0.000000 124.07288
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 46.89586
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 717
REMARK 465 ALA A 718
REMARK 465 SER A 719
REMARK 465 MSE A 720
REMARK 465 THR A 721
REMARK 465 GLY A 722
REMARK 465 GLY A 723
REMARK 465 GLN A 724
REMARK 465 GLN A 725
REMARK 465 MSE A 726
REMARK 465 GLY A 727
REMARK 465 ARG A 728
REMARK 465 GLY A 729
REMARK 465 SER A 730
REMARK 465 SER A 731
REMARK 465 ASP A 732
REMARK 465 GLU A 733
REMARK 465 VAL A 734
REMARK 465 LYS A 735
REMARK 465 LEU A 736
REMARK 465 LEU A 737
REMARK 465 GLN A 738
REMARK 465 GLU A 739
REMARK 465 ALA A 740
REMARK 465 LEU A 741
REMARK 465 ILE A 742
REMARK 465 LYS A 743
REMARK 465 LEU A 744
REMARK 465 GLY A 745
REMARK 465 PHE A 746
REMARK 465 ASP A 747
REMARK 465 LEU A 748
REMARK 465 GLY A 749
REMARK 465 LYS A 750
REMARK 465 ALA A 751
REMARK 465 GLY A 752
REMARK 465 ALA A 753
REMARK 465 ASP A 754
REMARK 465 GLY A 755
REMARK 465 ASP A 756
REMARK 465 PHE A 757
REMARK 465 GLY A 758
REMARK 465 SER A 759
REMARK 465 LYS A 760
REMARK 465 THR A 761
REMARK 465 LYS A 762
REMARK 465 THR A 763
REMARK 465 ALA A 764
REMARK 465 ILE A 765
REMARK 465 GLU A 766
REMARK 465 GLN A 767
REMARK 465 PHE A 768
REMARK 465 GLN A 769
REMARK 465 LYS A 770
REMARK 465 SER A 771
REMARK 465 TYR A 772
REMARK 465 GLN A 773
REMARK 465 PRO A 774
REMARK 465 SER A 775
REMARK 465 HIS A 776
REMARK 465 GLN A 777
REMARK 465 THR A 778
REMARK 465 HIS A 779
REMARK 465 PRO A 780
REMARK 465 SER A 781
REMARK 465 TYR A 782
REMARK 465 SER A 783
REMARK 465 ILE A 784
REMARK 465 GLY A 785
REMARK 465 ALA A 786
REMARK 465 VAL A 787
REMARK 465 ASP A 788
REMARK 465 GLY A 789
REMARK 465 ILE A 790
REMARK 465 VAL A 791
REMARK 465 GLY A 792
REMARK 465 LYS A 793
REMARK 465 GLY A 794
REMARK 465 THR A 795
REMARK 465 LEU A 796
REMARK 465 LEU A 797
REMARK 465 ALA A 798
REMARK 465 LEU A 799
REMARK 465 ASP A 800
REMARK 465 GLU A 801
REMARK 465 ALA A 802
REMARK 465 LEU A 803
REMARK 465 MSE A 804
REMARK 465 ASP A 805
REMARK 465 GLY A 806
REMARK 465 TRP A 807
REMARK 465 VAL A 808
REMARK 465 TYR A 809
REMARK 465 GLU A 810
REMARK 465 ASN A 811
REMARK 465 ASN A 812
REMARK 465 ILE A 813
REMARK 465 TYR A 814
REMARK 465 GLN A 815
REMARK 465 HIS A 1013
REMARK 465 HIS A 1014
REMARK 465 HIS A 1015
REMARK 465 HIS A 1016
REMARK 465 HIS A 1017
REMARK 465 MSE B 24
REMARK 465 GLY B 25
REMARK 465 GLU B 26
REMARK 465 ASN B 27
REMARK 465 CYS B 28
REMARK 465 ASN B 29
REMARK 465 ASP B 30
REMARK 465 GLU B 125
REMARK 465 HIS B 126
REMARK 465 HIS B 127
REMARK 465 HIS B 128
REMARK 465 HIS B 129
REMARK 465 HIS B 130
REMARK 465 HIS B 131
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 ARG A 929 OE1 GLU A 1011 1.73
REMARK 500 CG ARG A 929 OE1 GLU A 1011 1.74
REMARK 500 O GLU A 1008 CG GLU A 1011 1.74
REMARK 500 NZ LYS A 975 O HOH A 1161 1.79
REMARK 500 CG GLU A 1008 OE2 GLU A 1011 1.86
REMARK 500 NZ LYS A 907 O HOH A 1151 1.92
REMARK 500 CD GLU A 1008 OE2 GLU A 1011 2.16
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 921 CD2 LEU B 124 2656 0.51
REMARK 500 NZ LYS A 921 CG LEU B 124 2656 1.10
REMARK 500 CE LYS A 921 CD2 LEU B 124 2656 1.71
REMARK 500 NZ LYS A 921 CD1 LEU B 124 2656 2.07
REMARK 500 NZ LYS A 921 CB LEU B 124 2656 2.10
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 910 -71.62 -137.73
REMARK 500 ASN A 928 -162.70 -118.27
REMARK 500 GLN A 957 117.11 -161.57
REMARK 500 SER A 961 6.12 84.28
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 960 SER A 961 -145.12
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4NSR RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE IMMUNITY PROTEIN
DBREF 4NSO A 731 1009 UNP Q9KN42 Q9KN42_VIBCH 731 1009
DBREF 4NSO B 26 122 UNP Q9KN41 Q9KN41_VIBCH 26 122
SEQADV 4NSO MSE A 717 UNP Q9KN42 EXPRESSION TAG
SEQADV 4NSO ALA A 718 UNP Q9KN42 EXPRESSION TAG
SEQADV 4NSO SER A 719 UNP Q9KN42 EXPRESSION TAG
SEQADV 4NSO MSE A 720 UNP Q9KN42 EXPRESSION TAG
SEQADV 4NSO THR A 721 UNP Q9KN42 EXPRESSION TAG
SEQADV 4NSO GLY A 722 UNP Q9KN42 EXPRESSION TAG
SEQADV 4NSO GLY A 723 UNP Q9KN42 EXPRESSION TAG
SEQADV 4NSO GLN A 724 UNP Q9KN42 EXPRESSION TAG
SEQADV 4NSO GLN A 725 UNP Q9KN42 EXPRESSION TAG
SEQADV 4NSO MSE A 726 UNP Q9KN42 EXPRESSION TAG
SEQADV 4NSO GLY A 727 UNP Q9KN42 EXPRESSION TAG
SEQADV 4NSO ARG A 728 UNP Q9KN42 EXPRESSION TAG
SEQADV 4NSO GLY A 729 UNP Q9KN42 EXPRESSION TAG
SEQADV 4NSO SER A 730 UNP Q9KN42 EXPRESSION TAG
SEQADV 4NSO LEU A 1010 UNP Q9KN42 EXPRESSION TAG
SEQADV 4NSO GLU A 1011 UNP Q9KN42 EXPRESSION TAG
SEQADV 4NSO HIS A 1012 UNP Q9KN42 EXPRESSION TAG
SEQADV 4NSO HIS A 1013 UNP Q9KN42 EXPRESSION TAG
SEQADV 4NSO HIS A 1014 UNP Q9KN42 EXPRESSION TAG
SEQADV 4NSO HIS A 1015 UNP Q9KN42 EXPRESSION TAG
SEQADV 4NSO HIS A 1016 UNP Q9KN42 EXPRESSION TAG
SEQADV 4NSO HIS A 1017 UNP Q9KN42 EXPRESSION TAG
SEQADV 4NSO MSE B 24 UNP Q9KN41 EXPRESSION TAG
SEQADV 4NSO GLY B 25 UNP Q9KN41 EXPRESSION TAG
SEQADV 4NSO LEU B 123 UNP Q9KN41 EXPRESSION TAG
SEQADV 4NSO LEU B 124 UNP Q9KN41 EXPRESSION TAG
SEQADV 4NSO GLU B 125 UNP Q9KN41 EXPRESSION TAG
SEQADV 4NSO HIS B 126 UNP Q9KN41 EXPRESSION TAG
SEQADV 4NSO HIS B 127 UNP Q9KN41 EXPRESSION TAG
SEQADV 4NSO HIS B 128 UNP Q9KN41 EXPRESSION TAG
SEQADV 4NSO HIS B 129 UNP Q9KN41 EXPRESSION TAG
SEQADV 4NSO HIS B 130 UNP Q9KN41 EXPRESSION TAG
SEQADV 4NSO HIS B 131 UNP Q9KN41 EXPRESSION TAG
SEQRES 1 A 301 MSE ALA SER MSE THR GLY GLY GLN GLN MSE GLY ARG GLY
SEQRES 2 A 301 SER SER ASP GLU VAL LYS LEU LEU GLN GLU ALA LEU ILE
SEQRES 3 A 301 LYS LEU GLY PHE ASP LEU GLY LYS ALA GLY ALA ASP GLY
SEQRES 4 A 301 ASP PHE GLY SER LYS THR LYS THR ALA ILE GLU GLN PHE
SEQRES 5 A 301 GLN LYS SER TYR GLN PRO SER HIS GLN THR HIS PRO SER
SEQRES 6 A 301 TYR SER ILE GLY ALA VAL ASP GLY ILE VAL GLY LYS GLY
SEQRES 7 A 301 THR LEU LEU ALA LEU ASP GLU ALA LEU MSE ASP GLY TRP
SEQRES 8 A 301 VAL TYR GLU ASN ASN ILE TYR GLN ILE TRP PRO LEU GLY
SEQRES 9 A 301 LYS THR SER GLU LYS TYR GLU SER ALA GLY ARG GLY PRO
SEQRES 10 A 301 GLY VAL ILE SER THR GLY ASN GLY ASP TYR GLY GLY ALA
SEQRES 11 A 301 SER TYR GLY CYS TYR GLN MSE SER SER ASN LEU GLY VAL
SEQRES 12 A 301 VAL GLN LYS TYR ILE GLN SER SER LYS PHE LYS GLU PHE
SEQRES 13 A 301 PHE SER GLY LEU ASN PRO ALA THR LYS GLU PHE ASN VAL
SEQRES 14 A 301 VAL TRP GLN ASP ILE ALA SER ARG TYR PRO GLN GLU PHE
SEQRES 15 A 301 ARG GLU GLU GLN HIS GLN PHE ILE LYS ARG THR HIS TYR
SEQRES 16 A 301 ASP ILE GLN ILE GLY HIS LEU ARG GLY LYS GLY LEU LEU
SEQRES 17 A 301 PHE GLU HIS ASN ARG ALA ALA VAL HIS ASP LEU ILE TRP
SEQRES 18 A 301 SER THR SER VAL GLN PHE GLY GLY ARG THR ASN LEU ILE
SEQRES 19 A 301 PHE ASN ALA LEU ASN GLY GLN ASN MSE GLU SER MSE THR
SEQRES 20 A 301 ASP LYS ASP ILE ILE ILE LEU VAL GLN ASP TYR LYS LEU
SEQRES 21 A 301 VAL ASN THR GLU ARG LEU PHE LYS SER SER PRO SER TRP
SEQRES 22 A 301 TRP SER ASP LEU LYS LYS ARG ALA VAL SER GLU LYS LYS
SEQRES 23 A 301 ALA LEU LEU GLU LEU GLU ILE LEU GLU HIS HIS HIS HIS
SEQRES 24 A 301 HIS HIS
SEQRES 1 B 108 MSE GLY GLU ASN CYS ASN ASP THR SER GLY VAL HIS GLN
SEQRES 2 B 108 LYS ILE LEU VAL CYS ILE GLN ASN GLU ILE ALA LYS SER
SEQRES 3 B 108 GLU THR GLN ILE ARG ASN ASN ILE SER SER LYS SER ILE
SEQRES 4 B 108 ASP TYR GLY PHE PRO ASP ASP PHE TYR SER LYS GLN ARG
SEQRES 5 B 108 LEU ALA ILE HIS GLU LYS CYS MSE LEU TYR ILE ASN VAL
SEQRES 6 B 108 GLY GLY GLN ARG GLY GLU LEU LEU MSE ASN GLN CYS GLU
SEQRES 7 B 108 LEU SER MSE LEU GLN GLY LEU ASP ILE TYR ILE GLN GLN
SEQRES 8 B 108 TYR ILE GLU ASP VAL ASP ASN SER LEU LEU GLU HIS HIS
SEQRES 9 B 108 HIS HIS HIS HIS
MODRES 4NSO MSE A 853 MET SELENOMETHIONINE
MODRES 4NSO MSE A 959 MET SELENOMETHIONINE
MODRES 4NSO MSE A 962 MET SELENOMETHIONINE
MODRES 4NSO MSE B 83 MET SELENOMETHIONINE
MODRES 4NSO MSE B 97 MET SELENOMETHIONINE
MODRES 4NSO MSE B 104 MET SELENOMETHIONINE
HET MSE A 853 8
HET MSE A 959 8
HET MSE A 962 8
HET MSE B 83 8
HET MSE B 97 8
HET MSE B 104 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 6(C5 H11 N O2 SE)
FORMUL 3 HOH *107(H2 O)
HELIX 1 1 GLY A 820 THR A 822 5 3
HELIX 2 2 SER A 823 SER A 828 1 6
HELIX 3 3 GLY A 858 SER A 867 1 10
HELIX 4 4 PHE A 869 SER A 874 5 6
HELIX 5 5 THR A 880 TYR A 894 1 15
HELIX 6 6 TYR A 894 HIS A 910 1 17
HELIX 7 7 HIS A 910 LYS A 921 1 12
HELIX 8 8 ARG A 929 GLY A 944 1 16
HELIX 9 9 ASN A 948 LEU A 954 1 7
HELIX 10 10 THR A 963 ASN A 978 1 16
HELIX 11 11 ASN A 978 PHE A 983 1 6
HELIX 12 12 SER A 986 SER A 988 5 3
HELIX 13 13 TRP A 989 HIS A 1012 1 24
HELIX 14 14 VAL B 34 SER B 59 1 26
HELIX 15 15 ASP B 69 LEU B 84 1 16
HELIX 16 16 TYR B 85 VAL B 88 5 4
HELIX 17 17 GLY B 89 ASN B 98 1 10
SHEET 1 A 3 ILE A 836 THR A 838 0
SHEET 2 A 3 ALA A 846 TYR A 848 -1 O SER A 847 N SER A 837
SHEET 3 A 3 MSE A 853 SER A 854 -1 O MSE A 853 N TYR A 848
LINK C MSE A 853 N SER A 854 1555 1555 1.33
LINK C ASN A 958 N MSE A 959 1555 1555 1.33
LINK C MSE A 959 N GLU A 960 1555 1555 1.32
LINK C SER A 961 N MSE A 962 1555 1555 1.33
LINK C MSE A 962 N THR A 963 1555 1555 1.33
LINK C CYS B 82 N MSE B 83 1555 1555 1.33
LINK C MSE B 83 N LEU B 84 1555 1555 1.33
LINK C LEU B 96 N MSE B 97 1555 1555 1.34
LINK C MSE B 97 N ASN B 98 1555 1555 1.34
LINK C SER B 103 N MSE B 104 1555 1555 1.34
LINK C MSE B 104 N LEU B 105 1555 1555 1.34
LINK C GLN A 852 N MSE A 853 1555 1555 1.33
CISPEP 1 GLU A 926 HIS A 927 0 -15.97
CRYST1 133.631 78.660 47.860 90.00 101.52 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 0.007483 0.000000 0.001525 0.00000
SCALE2 0.000000 0.012713 0.000000 0.00000
SCALE3 0.000000 0.000000 0.021323 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
