HEADER SIGNALING PROTEIN 28-FEB-16 5IH2
TITLE STRUCTURE, THERMODYNAMICS, AND THE ROLE OF CONFORMATIONAL DYNAMICS IN
TITLE 2 THE INTERACTIONS BETWEEN THE N-TERMINAL SH3 DOMAIN OF CRKII AND
TITLE 3 PROLINE-RICH MOTIFS IN CABL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ADAPTER MOLECULE CRK;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 134-191;
COMPND 5 SYNONYM: PROTO-ONCOGENE C-CRK,P38;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: PROLINE RICH PEPTIDE;
COMPND 9 CHAIN: M, N;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: CRK, CRKO;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 SYNTHETIC: YES;
SOURCE 10 ORGANISM_SCIENTIFIC: ENDOTHIA GYROSA;
SOURCE 11 ORGANISM_TAXID: 40263
KEYWDS SH3 DOMAIN POLYPROLINE II MOTIF, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR V.S.BHATT,D.ZENG,I.KRIEGER,J.C.SACCHETTINI,J.-H.CHO
REVDAT 2 27-SEP-23 5IH2 1 JRNL REMARK LINK
REVDAT 1 29-JUN-16 5IH2 0
JRNL AUTH V.S.BHATT,D.ZENG,I.KRIEGER,J.C.SACCHETTINI,J.H.CHO
JRNL TITL BINDING MECHANISM OF THE N-TERMINAL SH3 DOMAIN OF CRKII AND
JRNL TITL 2 PROLINE-RICH MOTIFS IN CABL.
JRNL REF BIOPHYS.J. V. 110 2630 2016
JRNL REFN ESSN 1542-0086
JRNL PMID 27332121
JRNL DOI 10.1016/J.BPJ.2016.05.008
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0103
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.63
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 10714
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) : 0.173
REMARK 3 R VALUE (WORKING SET) : 0.170
REMARK 3 FREE R VALUE : 0.243
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.400
REMARK 3 FREE R VALUE TEST SET COUNT : 612
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) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.85
REMARK 3 REFLECTION IN BIN (WORKING SET) : 762
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.09
REMARK 3 BIN R VALUE (WORKING SET) : 0.1010
REMARK 3 BIN FREE R VALUE SET COUNT : 48
REMARK 3 BIN FREE R VALUE : 0.2730
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1146
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 26
REMARK 3 SOLVENT ATOMS : 181
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.53
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.52000
REMARK 3 B22 (A**2) : -0.03000
REMARK 3 B33 (A**2) : 0.53000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.10000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.163
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.161
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.956
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.900
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1238 ; 0.022 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 1168 ; 0.000 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1656 ; 2.039 ; 1.995
REMARK 3 BOND ANGLES OTHERS (DEGREES): 2710 ; 3.453 ; 3.012
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 138 ; 6.132 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 73 ;40.848 ;23.425
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 221 ;12.171 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 13 ;17.973 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 150 ; 0.113 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1381 ; 0.011 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 280 ; 0.024 ; 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): 556 ; 1.538 ; 1.776
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 555 ; 1.536 ; 1.774
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 694 ; 2.096 ; 2.642
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 695 ; 2.096 ; 2.645
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 682 ; 2.792 ; 2.144
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 683 ; 2.927 ; 2.142
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 963 ; 4.236 ; 3.090
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 1517 ; 6.450 ;16.411
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 1437 ; 5.884 ;15.548
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 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 5IH2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-MAR-16.
REMARK 100 THE DEPOSITION ID IS D_1000218776.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-FEB-14
REMARK 200 TEMPERATURE (KELVIN) : 113
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 11478
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
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 (%) : 99.1
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.14400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 38.0550
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.83
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: 1CKA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 33.21
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.84
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293K
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 14.73950
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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1550 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 5540 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, M
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: 1160 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 5220 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, N
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 TYR B 190
REMARK 465 ARG B 191
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 B 342 O HOH B 350 2.00
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 O HOH A 365 O HOH B 350 1545 1.98
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 ARG M 9 C NH2 M 10 N 0.154
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 ARG A 138 NE - CZ - NH1 ANGL. DEV. = 8.3 DEGREES
REMARK 500 ARG A 138 NE - CZ - NH2 ANGL. DEV. = -6.5 DEGREES
REMARK 500 ARG B 138 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ARG N 7 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 P4G B 201
REMARK 610 P4G N 101
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 203 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA A 134 O
REMARK 620 2 HOH A 351 O 97.7
REMARK 620 3 HOH A 362 O 83.3 85.2
REMARK 620 4 HOH A 365 O 94.4 163.9 85.7
REMARK 620 5 HOH A 381 O 177.3 82.2 94.0 85.2
REMARK 620 6 HOH B 342 O 91.9 90.5 173.0 99.8 90.8
REMARK 620 7 HOH B 350 O 101.7 135.6 136.2 50.8 80.1 49.7
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 202 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG A 179 O
REMARK 620 2 HOH A 305 O 90.7
REMARK 620 3 HOH A 309 O 97.6 98.6
REMARK 620 4 HOH B 335 O 85.7 85.6 174.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 202 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY B 145 O
REMARK 620 2 ASP B 147 O 81.1
REMARK 620 3 ASP B 150 O 100.2 91.0
REMARK 620 4 HOH B 319 O 84.7 92.7 174.3
REMARK 620 5 HOH B 324 O 134.3 144.5 82.0 92.5
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue P4G B 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue P4G N 101
DBREF 5IH2 A 134 191 UNP Q64010 CRK_MOUSE 134 191
DBREF 5IH2 B 134 191 UNP Q64010 CRK_MOUSE 134 191
DBREF 5IH2 M -1 10 PDB 5IH2 5IH2 -1 10
DBREF 5IH2 N -1 10 PDB 5IH2 5IH2 -1 10
SEQRES 1 A 58 ALA GLU TYR VAL ARG ALA LEU PHE ASP PHE ASN GLY ASN
SEQRES 2 A 58 ASP GLU GLU ASP LEU PRO PHE LYS LYS GLY ASP ILE LEU
SEQRES 3 A 58 ARG ILE ARG ASP LYS PRO GLU GLU GLN TRP TRP ASN ALA
SEQRES 4 A 58 GLU ASP SER GLU GLY LYS ARG GLY MET ILE PRO VAL PRO
SEQRES 5 A 58 TYR VAL GLU LYS TYR ARG
SEQRES 1 B 58 ALA GLU TYR VAL ARG ALA LEU PHE ASP PHE ASN GLY ASN
SEQRES 2 B 58 ASP GLU GLU ASP LEU PRO PHE LYS LYS GLY ASP ILE LEU
SEQRES 3 B 58 ARG ILE ARG ASP LYS PRO GLU GLU GLN TRP TRP ASN ALA
SEQRES 4 B 58 GLU ASP SER GLU GLY LYS ARG GLY MET ILE PRO VAL PRO
SEQRES 5 B 58 TYR VAL GLU LYS TYR ARG
SEQRES 1 M 12 ACE TYR GLU LYS PRO ALA LEU PRO ARG LYS ARG NH2
SEQRES 1 N 12 ACE TYR GLU LYS PRO ALA LEU PRO ARG LYS ARG NH2
HET ACE M -1 3
HET NH2 M 10 1
HET ACE N -1 3
HET NH2 N 10 1
HET PEG A 201 7
HET NA A 202 1
HET NA A 203 1
HET NA A 204 1
HET P4G B 201 9
HET NA B 202 1
HET P4G N 101 6
HETNAM ACE ACETYL GROUP
HETNAM NH2 AMINO GROUP
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM NA SODIUM ION
HETNAM P4G 1-ETHOXY-2-(2-ETHOXYETHOXY)ETHANE
FORMUL 3 ACE 2(C2 H4 O)
FORMUL 3 NH2 2(H2 N)
FORMUL 5 PEG C4 H10 O3
FORMUL 6 NA 4(NA 1+)
FORMUL 9 P4G 2(C8 H18 O3)
FORMUL 12 HOH *181(H2 O)
SHEET 1 AA1 5 ARG A 179 PRO A 183 0
SHEET 2 AA1 5 TRP A 169 GLU A 173 -1 N ALA A 172 O GLY A 180
SHEET 3 AA1 5 ILE A 158 ASP A 163 -1 N ARG A 160 O GLU A 173
SHEET 4 AA1 5 GLU A 135 ALA A 139 -1 N GLU A 135 O ILE A 161
SHEET 5 AA1 5 VAL A 187 LYS A 189 -1 O GLU A 188 N ARG A 138
SHEET 1 AA2 5 ARG B 179 PRO B 183 0
SHEET 2 AA2 5 TRP B 169 GLU B 173 -1 N TRP B 170 O ILE B 182
SHEET 3 AA2 5 ILE B 158 ASP B 163 -1 N ARG B 162 O ASN B 171
SHEET 4 AA2 5 TYR B 136 ALA B 139 -1 N VAL B 137 O LEU B 159
SHEET 5 AA2 5 VAL B 187 GLU B 188 -1 O GLU B 188 N ARG B 138
LINK C ACE M -1 N TYR M 0 1555 1555 1.46
LINK C ARG M 9 N NH2 M 10 1555 1555 1.49
LINK C ACE N -1 N TYR N 0 1555 1555 1.47
LINK C ARG N 9 N NH2 N 10 1555 1555 1.30
LINK O ALA A 134 NA NA A 203 1555 1555 2.37
LINK O ARG A 179 NA NA A 202 1555 1555 2.45
LINK NA NA A 202 O HOH A 305 1555 1565 2.32
LINK NA NA A 202 O HOH A 309 1555 1555 2.37
LINK NA NA A 202 O HOH B 335 1555 1555 2.59
LINK NA NA A 203 O HOH A 351 1555 1555 2.77
LINK NA NA A 203 O HOH A 362 1555 1555 2.54
LINK NA NA A 203 O HOH A 365 1555 1555 2.35
LINK NA NA A 203 O HOH A 381 1555 1555 2.40
LINK NA NA A 203 O HOH B 342 1555 1545 2.48
LINK NA NA A 203 O HOH B 350 1555 1545 2.25
LINK NA NA A 204 O HOH M 116 1555 1555 3.11
LINK O GLY B 145 NA NA B 202 1555 1555 2.36
LINK O ASP B 147 NA NA B 202 1555 1555 2.43
LINK O ASP B 150 NA NA B 202 1555 1555 2.50
LINK NA NA B 202 O HOH B 319 1555 1555 2.34
LINK NA NA B 202 O HOH B 324 1555 1555 2.21
SITE 1 AC1 7 ILE A 158 GLU A 173 ASP A 174 SER A 175
SITE 2 AC1 7 HOH A 321 HOH A 326 HOH A 327
SITE 1 AC2 4 ARG A 179 HOH A 305 HOH A 309 HOH B 335
SITE 1 AC3 7 ALA A 134 HOH A 351 HOH A 362 HOH A 365
SITE 2 AC3 7 HOH A 381 HOH B 342 HOH B 350
SITE 1 AC4 2 ASN A 144 LYS A 154
SITE 1 AC5 3 ASP B 174 SER B 175 HOH B 337
SITE 1 AC6 6 GLY B 145 ASP B 147 GLU B 148 ASP B 150
SITE 2 AC6 6 HOH B 319 HOH B 324
SITE 1 AC7 5 PHE B 141 ASP B 142 TYR N 0 LYS N 2
SITE 2 AC7 5 HOH N 203
CRYST1 45.222 29.479 45.756 90.00 94.31 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 0.022113 0.000000 0.001668 0.00000
SCALE2 0.000000 0.033922 0.000000 0.00000
SCALE3 0.000000 0.000000 0.021917 0.00000
(ATOM LINES ARE NOT SHOWN.)
END