HEADER STRUCTURAL PROTEIN 22-MAY-17 5VWK
TITLE CRYSTAL STRUCTURE OF HUMAN SCRIBBLE PDZ1:BETA-PIX COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN SCRIBBLE HOMOLOG;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: RESIDUES 700-816;
COMPND 5 SYNONYM: HSCRIB,PROTEIN LAP4;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: BETA-PIX;
COMPND 9 CHAIN: E, F, G, H;
COMPND 10 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: SCRIB, CRIB1, KIAA0147, LAP4, SCRB1, VARTUL;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 83333;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12;
SOURCE 13 EXPRESSION_SYSTEM_TAXID: 83333
KEYWDS POLARITY, STRUCTURAL PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR K.Y.B.LIM,M.KVANSAKUL
REVDAT 4 04-OCT-23 5VWK 1 REMARK
REVDAT 3 01-JAN-20 5VWK 1 REMARK
REVDAT 2 27-DEC-17 5VWK 1 JRNL
REVDAT 1 08-NOV-17 5VWK 0
JRNL AUTH K.Y.B.LIM,N.J.GODDE,P.O.HUMBERT,M.KVANSAKUL
JRNL TITL STRUCTURAL BASIS FOR THE DIFFERENTIAL INTERACTION OF
JRNL TITL 2 SCRIBBLE PDZ DOMAINS WITH THE GUANINE NUCLEOTIDE EXCHANGE
JRNL TITL 3 FACTOR BETA-PIX.
JRNL REF J. BIOL. CHEM. V. 292 20425 2017
JRNL REFN ESSN 1083-351X
JRNL PMID 29061852
JRNL DOI 10.1074/JBC.M117.799452
REMARK 2
REMARK 2 RESOLUTION. 2.35 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10_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) : 2.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.36
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.7
REMARK 3 NUMBER OF REFLECTIONS : 26411
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.225
REMARK 3 R VALUE (WORKING SET) : 0.223
REMARK 3 FREE R VALUE : 0.257
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1294
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 38.3620 - 4.8852 0.91 2833 160 0.2177 0.2835
REMARK 3 2 4.8852 - 3.8787 0.95 2797 138 0.1753 0.1955
REMARK 3 3 3.8787 - 3.3888 0.97 2799 144 0.2002 0.2209
REMARK 3 4 3.3888 - 3.0791 0.97 2799 123 0.2186 0.2533
REMARK 3 5 3.0791 - 2.8585 0.98 2791 127 0.2389 0.2619
REMARK 3 6 2.8585 - 2.6900 0.98 2770 164 0.2502 0.2828
REMARK 3 7 2.6900 - 2.5553 0.98 2775 147 0.2661 0.3003
REMARK 3 8 2.5553 - 2.4441 0.99 2766 150 0.2794 0.3108
REMARK 3 9 2.4441 - 2.3500 0.99 2787 141 0.2984 0.3395
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) : 0.310
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.940
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 : 0.004 3379
REMARK 3 ANGLE : 0.656 4566
REMARK 3 CHIRALITY : 0.048 504
REMARK 3 PLANARITY : 0.004 600
REMARK 3 DIHEDRAL : 19.482 1996
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 5VWK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-MAY-17.
REMARK 100 THE DEPOSITION ID IS D_1000228080.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-SEP-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.09
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX1
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 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26459
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.350
REMARK 200 RESOLUTION RANGE LOW (A) : 47.770
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.5
REMARK 200 DATA REDUNDANCY : 4.100
REMARK 200 R MERGE (I) : 0.12600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.43
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.2
REMARK 200 DATA REDUNDANCY IN SHELL : 4.10
REMARK 200 R MERGE FOR SHELL (I) : 0.73800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.800
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: 2W4F
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.61
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.83
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.09M LITHIUM SULFATE AND 0.1M
REMARK 280 TRISODIUM CITRATE-CITRIC ACID PH5.09, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 111.48150
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 37.38000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 37.38000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 167.22225
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 37.38000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 37.38000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 55.74075
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 37.38000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 37.38000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 167.22225
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 37.38000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 37.38000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 55.74075
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 111.48150
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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: 1700 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 6900 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -53.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, H
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
REMARK 350 BIOMOLECULE: 2
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: 1660 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 6830 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -51.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, G
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
REMARK 350 BIOMOLECULE: 3
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: 1410 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 6930 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, F
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
REMARK 350 BIOMOLECULE: 4
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: 1420 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 6860 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E
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 GLY A 695
REMARK 465 PRO A 696
REMARK 465 LEU A 697
REMARK 465 GLY A 698
REMARK 465 SER A 699
REMARK 465 SER A 700
REMARK 465 ALA A 701
REMARK 465 PRO A 702
REMARK 465 SER A 703
REMARK 465 VAL A 704
REMARK 465 LYS A 705
REMARK 465 GLY A 706
REMARK 465 VAL A 707
REMARK 465 SER A 708
REMARK 465 PHE A 709
REMARK 465 ASP A 710
REMARK 465 GLN A 711
REMARK 465 ALA A 712
REMARK 465 ASN A 713
REMARK 465 MET A 816
REMARK 465 GLY B 695
REMARK 465 PRO B 696
REMARK 465 LEU B 697
REMARK 465 GLY B 698
REMARK 465 SER B 699
REMARK 465 SER B 700
REMARK 465 ALA B 701
REMARK 465 PRO B 702
REMARK 465 SER B 703
REMARK 465 VAL B 704
REMARK 465 LYS B 705
REMARK 465 GLY B 706
REMARK 465 VAL B 707
REMARK 465 SER B 708
REMARK 465 PHE B 709
REMARK 465 ASP B 710
REMARK 465 GLN B 711
REMARK 465 ALA B 712
REMARK 465 ASN B 713
REMARK 465 MET B 816
REMARK 465 GLY C 695
REMARK 465 PRO C 696
REMARK 465 LEU C 697
REMARK 465 GLY C 698
REMARK 465 SER C 699
REMARK 465 SER C 700
REMARK 465 ALA C 701
REMARK 465 PRO C 702
REMARK 465 SER C 703
REMARK 465 VAL C 704
REMARK 465 LYS C 705
REMARK 465 GLY C 706
REMARK 465 VAL C 707
REMARK 465 SER C 708
REMARK 465 PHE C 709
REMARK 465 ASP C 710
REMARK 465 GLN C 711
REMARK 465 ALA C 712
REMARK 465 ASN C 713
REMARK 465 ASN C 714
REMARK 465 MET C 816
REMARK 465 GLY D 695
REMARK 465 PRO D 696
REMARK 465 LEU D 697
REMARK 465 GLY D 698
REMARK 465 SER D 699
REMARK 465 SER D 700
REMARK 465 ALA D 701
REMARK 465 PRO D 702
REMARK 465 SER D 703
REMARK 465 VAL D 704
REMARK 465 LYS D 705
REMARK 465 GLY D 706
REMARK 465 VAL D 707
REMARK 465 SER D 708
REMARK 465 PHE D 709
REMARK 465 ASP D 710
REMARK 465 GLN D 711
REMARK 465 ALA D 712
REMARK 465 ASN D 713
REMARK 465 ASN D 714
REMARK 465 MET D 816
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 ASN A 714 CG OD1 ND2
REMARK 470 LEU A 716 CG CD1 CD2
REMARK 470 ASN B 714 CG OD1 ND2
REMARK 470 LEU B 716 CG CD1 CD2
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 OE1 GLU C 726 HE ARG C 810 1.51
REMARK 500 H GLU D 766 O HOH D 1002 1.51
REMARK 500 HH22 ARG A 801 OD2 ASP E 159 1.59
REMARK 500 O GLU B 766 O HOH B 1001 1.99
REMARK 500 O ALA C 720 O HOH C 1001 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 H GLY B 785 O1 SO4 C 904 5444 1.57
REMARK 500 O HOH A 1032 O HOH A 1034 8554 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 GLU B 766 49.17 -143.80
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 A1057 DISTANCE = 6.24 ANGSTROMS
REMARK 525 HOH A1058 DISTANCE = 6.94 ANGSTROMS
REMARK 525 HOH B1054 DISTANCE = 6.10 ANGSTROMS
REMARK 525 HOH B1055 DISTANCE = 6.16 ANGSTROMS
REMARK 525 HOH B1056 DISTANCE = 6.74 ANGSTROMS
REMARK 525 HOH B1057 DISTANCE = 8.24 ANGSTROMS
REMARK 525 HOH C1047 DISTANCE = 6.37 ANGSTROMS
REMARK 525 HOH C1048 DISTANCE = 6.47 ANGSTROMS
REMARK 525 HOH D1053 DISTANCE = 7.38 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 903
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 904
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 903
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 G 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 H 201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5VWI RELATED DB: PDB
DBREF 5VWK A 700 816 UNP Q14160 SCRIB_HUMAN 700 816
DBREF 5VWK B 700 816 UNP Q14160 SCRIB_HUMAN 700 816
DBREF 5VWK C 700 816 UNP Q14160 SCRIB_HUMAN 700 816
DBREF 5VWK D 700 816 UNP Q14160 SCRIB_HUMAN 700 816
DBREF 5VWK E 156 163 PDB 5VWK 5VWK 156 163
DBREF 5VWK F 156 163 PDB 5VWK 5VWK 156 163
DBREF 5VWK G 156 163 PDB 5VWK 5VWK 156 163
DBREF 5VWK H 156 163 PDB 5VWK 5VWK 156 163
SEQADV 5VWK GLY A 695 UNP Q14160 EXPRESSION TAG
SEQADV 5VWK PRO A 696 UNP Q14160 EXPRESSION TAG
SEQADV 5VWK LEU A 697 UNP Q14160 EXPRESSION TAG
SEQADV 5VWK GLY A 698 UNP Q14160 EXPRESSION TAG
SEQADV 5VWK SER A 699 UNP Q14160 EXPRESSION TAG
SEQADV 5VWK GLY B 695 UNP Q14160 EXPRESSION TAG
SEQADV 5VWK PRO B 696 UNP Q14160 EXPRESSION TAG
SEQADV 5VWK LEU B 697 UNP Q14160 EXPRESSION TAG
SEQADV 5VWK GLY B 698 UNP Q14160 EXPRESSION TAG
SEQADV 5VWK SER B 699 UNP Q14160 EXPRESSION TAG
SEQADV 5VWK GLY C 695 UNP Q14160 EXPRESSION TAG
SEQADV 5VWK PRO C 696 UNP Q14160 EXPRESSION TAG
SEQADV 5VWK LEU C 697 UNP Q14160 EXPRESSION TAG
SEQADV 5VWK GLY C 698 UNP Q14160 EXPRESSION TAG
SEQADV 5VWK SER C 699 UNP Q14160 EXPRESSION TAG
SEQADV 5VWK GLY D 695 UNP Q14160 EXPRESSION TAG
SEQADV 5VWK PRO D 696 UNP Q14160 EXPRESSION TAG
SEQADV 5VWK LEU D 697 UNP Q14160 EXPRESSION TAG
SEQADV 5VWK GLY D 698 UNP Q14160 EXPRESSION TAG
SEQADV 5VWK SER D 699 UNP Q14160 EXPRESSION TAG
SEQRES 1 A 122 GLY PRO LEU GLY SER SER ALA PRO SER VAL LYS GLY VAL
SEQRES 2 A 122 SER PHE ASP GLN ALA ASN ASN LEU LEU ILE GLU PRO ALA
SEQRES 3 A 122 ARG ILE GLU GLU GLU GLU LEU THR LEU THR ILE LEU ARG
SEQRES 4 A 122 GLN THR GLY GLY LEU GLY ILE SER ILE ALA GLY GLY LYS
SEQRES 5 A 122 GLY SER THR PRO TYR LYS GLY ASP ASP GLU GLY ILE PHE
SEQRES 6 A 122 ILE SER ARG VAL SER GLU GLU GLY PRO ALA ALA ARG ALA
SEQRES 7 A 122 GLY VAL ARG VAL GLY ASP LYS LEU LEU GLU VAL ASN GLY
SEQRES 8 A 122 VAL ALA LEU GLN GLY ALA GLU HIS HIS GLU ALA VAL GLU
SEQRES 9 A 122 ALA LEU ARG GLY ALA GLY THR ALA VAL GLN MET ARG VAL
SEQRES 10 A 122 TRP ARG GLU ARG MET
SEQRES 1 B 122 GLY PRO LEU GLY SER SER ALA PRO SER VAL LYS GLY VAL
SEQRES 2 B 122 SER PHE ASP GLN ALA ASN ASN LEU LEU ILE GLU PRO ALA
SEQRES 3 B 122 ARG ILE GLU GLU GLU GLU LEU THR LEU THR ILE LEU ARG
SEQRES 4 B 122 GLN THR GLY GLY LEU GLY ILE SER ILE ALA GLY GLY LYS
SEQRES 5 B 122 GLY SER THR PRO TYR LYS GLY ASP ASP GLU GLY ILE PHE
SEQRES 6 B 122 ILE SER ARG VAL SER GLU GLU GLY PRO ALA ALA ARG ALA
SEQRES 7 B 122 GLY VAL ARG VAL GLY ASP LYS LEU LEU GLU VAL ASN GLY
SEQRES 8 B 122 VAL ALA LEU GLN GLY ALA GLU HIS HIS GLU ALA VAL GLU
SEQRES 9 B 122 ALA LEU ARG GLY ALA GLY THR ALA VAL GLN MET ARG VAL
SEQRES 10 B 122 TRP ARG GLU ARG MET
SEQRES 1 C 122 GLY PRO LEU GLY SER SER ALA PRO SER VAL LYS GLY VAL
SEQRES 2 C 122 SER PHE ASP GLN ALA ASN ASN LEU LEU ILE GLU PRO ALA
SEQRES 3 C 122 ARG ILE GLU GLU GLU GLU LEU THR LEU THR ILE LEU ARG
SEQRES 4 C 122 GLN THR GLY GLY LEU GLY ILE SER ILE ALA GLY GLY LYS
SEQRES 5 C 122 GLY SER THR PRO TYR LYS GLY ASP ASP GLU GLY ILE PHE
SEQRES 6 C 122 ILE SER ARG VAL SER GLU GLU GLY PRO ALA ALA ARG ALA
SEQRES 7 C 122 GLY VAL ARG VAL GLY ASP LYS LEU LEU GLU VAL ASN GLY
SEQRES 8 C 122 VAL ALA LEU GLN GLY ALA GLU HIS HIS GLU ALA VAL GLU
SEQRES 9 C 122 ALA LEU ARG GLY ALA GLY THR ALA VAL GLN MET ARG VAL
SEQRES 10 C 122 TRP ARG GLU ARG MET
SEQRES 1 D 122 GLY PRO LEU GLY SER SER ALA PRO SER VAL LYS GLY VAL
SEQRES 2 D 122 SER PHE ASP GLN ALA ASN ASN LEU LEU ILE GLU PRO ALA
SEQRES 3 D 122 ARG ILE GLU GLU GLU GLU LEU THR LEU THR ILE LEU ARG
SEQRES 4 D 122 GLN THR GLY GLY LEU GLY ILE SER ILE ALA GLY GLY LYS
SEQRES 5 D 122 GLY SER THR PRO TYR LYS GLY ASP ASP GLU GLY ILE PHE
SEQRES 6 D 122 ILE SER ARG VAL SER GLU GLU GLY PRO ALA ALA ARG ALA
SEQRES 7 D 122 GLY VAL ARG VAL GLY ASP LYS LEU LEU GLU VAL ASN GLY
SEQRES 8 D 122 VAL ALA LEU GLN GLY ALA GLU HIS HIS GLU ALA VAL GLU
SEQRES 9 D 122 ALA LEU ARG GLY ALA GLY THR ALA VAL GLN MET ARG VAL
SEQRES 10 D 122 TRP ARG GLU ARG MET
SEQRES 1 E 8 PRO ALA TRP ASP GLU THR ASN LEU
SEQRES 1 F 8 PRO ALA TRP ASP GLU THR ASN LEU
SEQRES 1 G 8 PRO ALA TRP ASP GLU THR ASN LEU
SEQRES 1 H 8 PRO ALA TRP ASP GLU THR ASN LEU
HET SO4 A 901 5
HET SO4 A 902 5
HET SO4 B 901 5
HET SO4 C 901 5
HET SO4 C 902 5
HET SO4 C 903 5
HET SO4 C 904 5
HET SO4 D 901 5
HET SO4 D 902 5
HET SO4 D 903 5
HET SO4 G 201 5
HET SO4 H 201 5
HETNAM SO4 SULFATE ION
FORMUL 9 SO4 12(O4 S 2-)
FORMUL 21 HOH *246(H2 O)
HELIX 1 AA1 GLY A 767 ALA A 772 1 6
HELIX 2 AA2 GLU A 792 GLY A 802 1 11
HELIX 3 AA3 GLY B 767 GLY B 773 1 7
HELIX 4 AA4 GLU B 792 GLY B 802 1 11
HELIX 5 AA5 GLY C 767 ALA C 772 1 6
HELIX 6 AA6 GLU C 792 GLY C 802 1 11
HELIX 7 AA7 GLY D 767 ALA D 772 1 6
HELIX 8 AA8 GLU D 792 GLY D 802 1 11
SHEET 1 AA1 4 GLU A 724 LEU A 732 0
SHEET 2 AA1 4 ALA A 806 GLU A 814 -1 O VAL A 807 N ILE A 731
SHEET 3 AA1 4 LYS A 779 VAL A 783 -1 N LEU A 781 O ARG A 810
SHEET 4 AA1 4 VAL A 786 ALA A 787 -1 O VAL A 786 N VAL A 783
SHEET 1 AA2 6 GLU A 724 LEU A 732 0
SHEET 2 AA2 6 ALA A 806 GLU A 814 -1 O VAL A 807 N ILE A 731
SHEET 3 AA2 6 LYS A 779 VAL A 783 -1 N LEU A 781 O ARG A 810
SHEET 4 AA2 6 ILE A 758 VAL A 763 -1 N ILE A 758 O LEU A 780
SHEET 5 AA2 6 ILE A 740 GLY A 744 -1 N ALA A 743 O PHE A 759
SHEET 6 AA2 6 GLU H 160 ASN H 162 -1 O THR H 161 N ILE A 742
SHEET 1 AA3 4 GLU B 725 LEU B 732 0
SHEET 2 AA3 4 ALA B 806 ARG B 813 -1 O VAL B 807 N ILE B 731
SHEET 3 AA3 4 LYS B 779 VAL B 783 -1 N LYS B 779 O TRP B 812
SHEET 4 AA3 4 VAL B 786 ALA B 787 -1 O VAL B 786 N VAL B 783
SHEET 1 AA4 6 GLU B 725 LEU B 732 0
SHEET 2 AA4 6 ALA B 806 ARG B 813 -1 O VAL B 807 N ILE B 731
SHEET 3 AA4 6 LYS B 779 VAL B 783 -1 N LYS B 779 O TRP B 812
SHEET 4 AA4 6 ILE B 758 VAL B 763 -1 N ILE B 758 O LEU B 780
SHEET 5 AA4 6 ILE B 740 GLY B 744 -1 N SER B 741 O SER B 761
SHEET 6 AA4 6 GLU G 160 LEU G 163 -1 O LEU G 163 N ILE B 740
SHEET 1 AA5 4 GLU C 724 LEU C 732 0
SHEET 2 AA5 4 ALA C 806 GLU C 814 -1 O MET C 809 N LEU C 729
SHEET 3 AA5 4 LYS C 779 VAL C 783 -1 N LEU C 781 O ARG C 810
SHEET 4 AA5 4 VAL C 786 ALA C 787 -1 O VAL C 786 N VAL C 783
SHEET 1 AA6 6 GLU C 724 LEU C 732 0
SHEET 2 AA6 6 ALA C 806 GLU C 814 -1 O MET C 809 N LEU C 729
SHEET 3 AA6 6 LYS C 779 VAL C 783 -1 N LEU C 781 O ARG C 810
SHEET 4 AA6 6 ILE C 758 VAL C 763 -1 N ILE C 758 O LEU C 780
SHEET 5 AA6 6 ILE C 740 GLY C 744 -1 N ALA C 743 O PHE C 759
SHEET 6 AA6 6 GLU F 160 ASN F 162 -1 O THR F 161 N ILE C 742
SHEET 1 AA7 4 GLU D 724 LEU D 732 0
SHEET 2 AA7 4 ALA D 806 GLU D 814 -1 O ARG D 813 N GLU D 725
SHEET 3 AA7 4 LYS D 779 VAL D 783 -1 N LYS D 779 O TRP D 812
SHEET 4 AA7 4 VAL D 786 ALA D 787 -1 O VAL D 786 N VAL D 783
SHEET 1 AA8 6 GLU D 724 LEU D 732 0
SHEET 2 AA8 6 ALA D 806 GLU D 814 -1 O ARG D 813 N GLU D 725
SHEET 3 AA8 6 LYS D 779 VAL D 783 -1 N LYS D 779 O TRP D 812
SHEET 4 AA8 6 ILE D 758 VAL D 763 -1 N ILE D 758 O LEU D 780
SHEET 5 AA8 6 ILE D 740 GLY D 744 -1 N ALA D 743 O PHE D 759
SHEET 6 AA8 6 GLU E 160 ASN E 162 -1 O THR E 161 N ILE D 742
LINK NH2 ARG B 762 O4 SO4 B 901 1555 1555 1.30
SITE 1 AC1 6 ARG A 762 VAL A 763 SER A 764 GLU A 765
SITE 2 AC1 6 GLY C 736 PRO G 156
SITE 1 AC2 7 GLU A 782 ASN A 784 GLY A 785 GLN A 808
SITE 2 AC2 7 MET A 809 ARG A 810 GLN D 808
SITE 1 AC3 5 ARG B 762 VAL B 763 SER B 764 GLY D 736
SITE 2 AC3 5 PRO H 156
SITE 1 AC4 9 GLU B 792 HIS B 793 HIS B 794 HOH B1010
SITE 2 AC4 9 HIS C 794 VAL C 797 ARG C 801 HOH F 202
SITE 3 AC4 9 ASP G 159
SITE 1 AC5 5 ARG A 762 ARG C 762 SER C 764 ASN H 162
SITE 2 AC5 5 HOH H 305
SITE 1 AC6 3 LYS C 779 LEU C 781 TRP C 812
SITE 1 AC7 9 GLU B 782 VAL B 783 ASN B 784 GLY B 785
SITE 2 AC7 9 GLN B 808 MET B 809 ARG B 810 GLN C 808
SITE 3 AC7 9 HOH C1003
SITE 1 AC8 8 GLU A 792 HIS A 793 HIS A 794 HIS D 794
SITE 2 AC8 8 ARG D 801 HOH D1004 HOH D1017 HOH H 303
SITE 1 AC9 8 ARG B 762 ARG D 762 SER D 764 HOH D1008
SITE 2 AC9 8 HOH D1021 HOH D1034 HOH D1037 ASN G 162
SITE 1 AD1 2 LYS D 779 TRP D 812
SITE 1 AD2 6 TRP G 158 GLU G 160 HOH G 306 ALA H 157
SITE 2 AD2 6 TRP H 158 SO4 H 201
SITE 1 AD3 5 ALA G 157 TRP G 158 SO4 G 201 TRP H 158
SITE 2 AD3 5 GLU H 160
CRYST1 74.760 74.760 222.963 90.00 90.00 90.00 P 43 21 2 32
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 0.013376 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013376 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004485 0.00000
(ATOM LINES ARE NOT SHOWN.)
END