HEADER PROTEIN BINDING 19-NOV-14 4RUG
TITLE CYRSTAL STRUCTURE OF SLIT-ROBO RHO GTPASE-ACTIVATING PROTEIN 2
TITLE 2 FRAGMENT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SLIT-ROBO RHO GTPASE-ACTIVATING PROTEIN 2;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 729-815;
COMPND 5 SYNONYM: SRGAP2, FORMIN-BINDING PROTEIN 2, RHO GTPASE-ACTIVATING
COMPND 6 PROTEIN 34;
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: SRGAP2, ARHGAP34, FNBP2, KIAA0456, SRGAP2A;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS SRGAP2, SH3, LIGAND BINDING, ROBO1, NUCLEAR, PLASMA MEMBRANE, PROTEIN
KEYWDS 2 BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.OPATOWSKY,J.GUEZ-HADAD
REVDAT 4 28-FEB-24 4RUG 1 SEQADV
REVDAT 3 22-NOV-17 4RUG 1 REMARK
REVDAT 2 18-NOV-15 4RUG 1 JRNL
REVDAT 1 04-NOV-15 4RUG 0
JRNL AUTH J.GUEZ-HADDAD,M.SPORNY,Y.SASSON,L.GEVORKYAN-AIRAPETOV,
JRNL AUTH 2 N.LAHAV-MANKOVSKI,D.MARGULIES,J.RADZIMANOWSKI,Y.OPATOWSKY
JRNL TITL THE NEURONAL MIGRATION FACTOR SRGAP2 ACHIEVES SPECIFICITY IN
JRNL TITL 2 LIGAND BINDING THROUGH A TWO-COMPONENT MOLECULAR MECHANISM.
JRNL REF STRUCTURE V. 23 1989 2015
JRNL REFN ISSN 0969-2126
JRNL PMID 26365803
JRNL DOI 10.1016/J.STR.2015.08.009
REMARK 2
REMARK 2 RESOLUTION. 1.73 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0049
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.73
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 57.81
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.9
REMARK 3 NUMBER OF REFLECTIONS : 17127
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.191
REMARK 3 R VALUE (WORKING SET) : 0.189
REMARK 3 FREE R VALUE : 0.222
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.400
REMARK 3 FREE R VALUE TEST SET COUNT : 980
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.73
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.78
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1127
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 83.74
REMARK 3 BIN R VALUE (WORKING SET) : 0.3900
REMARK 3 BIN FREE R VALUE SET COUNT : 47
REMARK 3 BIN FREE R VALUE : 0.4160
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1317
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 110
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.94
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.14000
REMARK 3 B22 (A**2) : 0.59000
REMARK 3 B33 (A**2) : -0.13000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.32000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.119
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.115
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.097
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.346
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.956
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.940
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1346 ; 0.014 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 1253 ; 0.005 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1822 ; 1.609 ; 1.958
REMARK 3 BOND ANGLES OTHERS (DEGREES): 2899 ; 1.070 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 164 ; 7.456 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 66 ;30.771 ;24.242
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 226 ;11.670 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 10 ;19.813 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 193 ; 0.116 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1516 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 294 ; 0.004 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 665 ; 5.628 ; 1.490
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 664 ; 5.629 ; 1.486
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 826 ; 8.232 ; 2.171
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 827 ; 8.227 ; 2.176
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 681 ; 8.950 ; 2.141
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 679 ; 8.893 ; 2.122
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 996 ;11.739 ; 2.898
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 1483 ;15.324 ;13.132
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 1436 ;15.388 ;12.609
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 1
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 B 728 808 A 728 808 4349 0.10 0.05
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 728 B 809
REMARK 3 ORIGIN FOR THE GROUP (A): 2.3230 -4.8870 -24.5520
REMARK 3 T TENSOR
REMARK 3 T11: 0.0131 T22: 0.0119
REMARK 3 T33: 0.0399 T12: -0.0032
REMARK 3 T13: 0.0121 T23: 0.0125
REMARK 3 L TENSOR
REMARK 3 L11: 2.2053 L22: 3.4809
REMARK 3 L33: 1.8027 L12: -1.2161
REMARK 3 L13: -0.9397 L23: 0.9031
REMARK 3 S TENSOR
REMARK 3 S11: -0.0664 S12: 0.0437 S13: -0.1019
REMARK 3 S21: 0.0560 S22: 0.0624 S23: 0.1708
REMARK 3 S31: 0.0271 S32: -0.0677 S33: 0.0040
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 724 A 809
REMARK 3 ORIGIN FOR THE GROUP (A): -6.6790 -9.2020 -48.6980
REMARK 3 T TENSOR
REMARK 3 T11: 0.0550 T22: 0.0073
REMARK 3 T33: 0.0490 T12: 0.0017
REMARK 3 T13: 0.0377 T23: -0.0070
REMARK 3 L TENSOR
REMARK 3 L11: 2.1801 L22: 3.0855
REMARK 3 L33: 1.8469 L12: 1.3613
REMARK 3 L13: -1.2322 L23: -0.8047
REMARK 3 S TENSOR
REMARK 3 S11: 0.0415 S12: -0.0887 S13: 0.0601
REMARK 3 S21: 0.1792 S22: -0.0452 S23: 0.0275
REMARK 3 S31: -0.0524 S32: 0.0018 S33: 0.0037
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.10
REMARK 3 ION PROBE RADIUS : 0.70
REMARK 3 SHRINKAGE RADIUS : 0.70
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4RUG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-NOV-14.
REMARK 100 THE DEPOSITION ID IS D_1000087809.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-APR-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.25
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.976
REMARK 200 MONOCHROMATOR : SI(311)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18107
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.730
REMARK 200 RESOLUTION RANGE LOW (A) : 57.810
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.0
REMARK 200 DATA REDUNDANCY : 6.500
REMARK 200 R MERGE (I) : 0.11800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.0900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.73
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.84
REMARK 200 COMPLETENESS FOR SHELL (%) : 0.9
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: BALBES
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.68
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.35M AMMONIUM SULPHATE; 0.1M MES, PH
REMARK 280 6.25, VAPOR DIFFUSION, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 15.67500
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 GLU A 810
REMARK 465 LYS A 811
REMARK 465 VAL A 812
REMARK 465 THR A 813
REMARK 465 ALA A 814
REMARK 465 ARG A 815
REMARK 465 GLY B 724
REMARK 465 ALA B 725
REMARK 465 MET B 726
REMARK 465 GLY B 727
REMARK 465 GLU B 788
REMARK 465 GLU B 810
REMARK 465 LYS B 811
REMARK 465 VAL B 812
REMARK 465 THR B 813
REMARK 465 ALA B 814
REMARK 465 ARG B 815
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 A 789 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 HOH A 925 O HOH A 943 2.04
REMARK 500 O HOH A 922 O HOH A 925 2.12
REMARK 500 O HOH A 919 O HOH A 926 2.13
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 THR A 787 161.35 97.50
REMARK 500 GLU A 788 169.22 82.83
REMARK 500 ASP A 789 70.83 -178.72
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ASP A 786 THR A 787 144.91
REMARK 500 ASP B 786 THR B 787 148.25
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4RTT RELATED DB: PDB
DBREF 4RUG A 729 815 UNP O75044 SRGP2_HUMAN 729 815
DBREF 4RUG B 729 815 UNP O75044 SRGP2_HUMAN 729 815
SEQADV 4RUG GLY A 724 UNP O75044 EXPRESSION TAG
SEQADV 4RUG ALA A 725 UNP O75044 EXPRESSION TAG
SEQADV 4RUG MET A 726 UNP O75044 EXPRESSION TAG
SEQADV 4RUG GLY A 727 UNP O75044 EXPRESSION TAG
SEQADV 4RUG SER A 728 UNP O75044 EXPRESSION TAG
SEQADV 4RUG GLY B 724 UNP O75044 EXPRESSION TAG
SEQADV 4RUG ALA B 725 UNP O75044 EXPRESSION TAG
SEQADV 4RUG MET B 726 UNP O75044 EXPRESSION TAG
SEQADV 4RUG GLY B 727 UNP O75044 EXPRESSION TAG
SEQADV 4RUG SER B 728 UNP O75044 EXPRESSION TAG
SEQRES 1 A 92 GLY ALA MET GLY SER GLU PRO ILE GLU ALA ILE ALA LYS
SEQRES 2 A 92 PHE ASP TYR VAL GLY ARG THR ALA ARG GLU LEU SER PHE
SEQRES 3 A 92 LYS LYS GLY ALA SER LEU LEU LEU TYR GLN ARG ALA SER
SEQRES 4 A 92 ASP ASP TRP TRP GLU GLY ARG HIS ASN GLY ILE ASP GLY
SEQRES 5 A 92 LEU ILE PRO HIS GLN TYR ILE VAL VAL GLN ASP THR GLU
SEQRES 6 A 92 ASP GLY VAL VAL GLU ARG SER SER PRO LYS SER GLU ILE
SEQRES 7 A 92 GLU VAL ILE SER GLU PRO PRO GLU GLU LYS VAL THR ALA
SEQRES 8 A 92 ARG
SEQRES 1 B 92 GLY ALA MET GLY SER GLU PRO ILE GLU ALA ILE ALA LYS
SEQRES 2 B 92 PHE ASP TYR VAL GLY ARG THR ALA ARG GLU LEU SER PHE
SEQRES 3 B 92 LYS LYS GLY ALA SER LEU LEU LEU TYR GLN ARG ALA SER
SEQRES 4 B 92 ASP ASP TRP TRP GLU GLY ARG HIS ASN GLY ILE ASP GLY
SEQRES 5 B 92 LEU ILE PRO HIS GLN TYR ILE VAL VAL GLN ASP THR GLU
SEQRES 6 B 92 ASP GLY VAL VAL GLU ARG SER SER PRO LYS SER GLU ILE
SEQRES 7 B 92 GLU VAL ILE SER GLU PRO PRO GLU GLU LYS VAL THR ALA
SEQRES 8 B 92 ARG
FORMUL 3 HOH *110(H2 O)
HELIX 1 1 GLY A 790 SER A 796 1 7
HELIX 2 2 SER A 799 SER A 805 1 7
HELIX 3 3 GLY B 790 SER B 796 1 7
HELIX 4 4 SER B 799 SER B 805 1 7
SHEET 1 A 5 ILE A 773 PRO A 778 0
SHEET 2 A 5 TRP A 765 HIS A 770 -1 N TRP A 766 O ILE A 777
SHEET 3 A 5 SER A 754 SER A 762 -1 N GLN A 759 O GLU A 767
SHEET 4 A 5 ILE A 731 ALA A 735 -1 N ILE A 731 O LEU A 757
SHEET 5 A 5 ILE A 782 VAL A 784 -1 O VAL A 783 N ILE A 734
SHEET 1 B 5 ILE B 773 PRO B 778 0
SHEET 2 B 5 TRP B 765 HIS B 770 -1 N TRP B 766 O ILE B 777
SHEET 3 B 5 SER B 754 SER B 762 -1 N GLN B 759 O GLU B 767
SHEET 4 B 5 ILE B 731 ALA B 735 -1 N ILE B 731 O LEU B 757
SHEET 5 B 5 ILE B 782 VAL B 784 -1 O VAL B 783 N ILE B 734
CISPEP 1 GLY A 724 ALA A 725 0 8.43
CISPEP 2 ASP A 789 GLY A 790 0 -5.90
CRYST1 49.510 31.350 62.830 90.00 113.07 90.00 P 1 21 1 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.020198 0.000000 0.008603 0.00000
SCALE2 0.000000 0.031898 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017299 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
