HEADER SIGNALING PROTEIN 25-JUL-06 2HT6
TITLE CRYSTAL STRUCTURE OF HUMAN GEM G-DOMAIN BOUND TO GDP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GTP-BINDING PROTEIN GEM;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: G-DOMAIN;
COMPND 5 SYNONYM: GTP-BINDING MITOGEN-INDUCED T-CELL PROTEIN, RAS-
COMPND 6 LIKE PROTEIN KIR;
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: GEM, KIR;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET-21
KEYWDS SMALL G-PROTEIN, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.OPATOWSKY,J.A.HIRSCH
REVDAT 2 24-FEB-09 2HT6 1 VERSN
REVDAT 1 31-OCT-06 2HT6 0
JRNL AUTH Y.OPATOWSKY,Y.SASSON,I.SHAKED,Y.WARD,
JRNL AUTH 2 O.CHOMSKY-HECHT,Y.LITVAK,Z.SELINGER,K.KELLY,
JRNL AUTH 3 J.A.HIRSCH
JRNL TITL STRUCTURE-FUNCTION STUDIES OF THE G-DOMAIN FROM
JRNL TITL 2 HUMAN GEM, A NOVEL SMALL G-PROTEIN.
JRNL REF FEBS LETT. V. 580 5959 2006
JRNL REFN ISSN 0014-5793
JRNL PMID 17052716
JRNL DOI 10.1016/J.FEBSLET.2006.09.067
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 16384
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) : 0.229
REMARK 3 R VALUE (WORKING SET) : 0.226
REMARK 3 FREE R VALUE : 0.287
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 830
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) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.46
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1111
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.91
REMARK 3 BIN R VALUE (WORKING SET) : 0.2830
REMARK 3 BIN FREE R VALUE SET COUNT : 71
REMARK 3 BIN FREE R VALUE : 0.3760
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2622
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 58
REMARK 3 SOLVENT ATOMS : 85
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 42.62
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.10000
REMARK 3 B22 (A**2) : 0.34000
REMARK 3 B33 (A**2) : -0.24000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.433
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.296
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.202
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.561
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.934
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.897
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2710 ; 0.011 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3663 ; 1.407 ; 1.977
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 325 ; 7.456 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 132 ;37.783 ;23.485
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 480 ;17.723 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 28 ;18.445 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 420 ; 0.111 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1994 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1223 ; 0.212 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1825 ; 0.302 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 143 ; 0.197 ; 0.200
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): 37 ; 0.295 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 12 ; 0.397 ; 0.200
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): 1676 ; 0.952 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2623 ; 1.652 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1184 ; 1.602 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1040 ; 2.665 ; 4.500
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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 3
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 76 A 96 2
REMARK 3 1 B 76 B 96 2
REMARK 3 2 A 106 A 135 2
REMARK 3 2 B 106 B 135 2
REMARK 3 3 A 141 A 240 2
REMARK 3 3 B 141 B 240 2
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 604 ; 0.060 ; 0.050
REMARK 3 MEDIUM POSITIONAL 1 A (A): 592 ; 0.430 ; 0.500
REMARK 3 TIGHT THERMAL 1 A (A**2): 604 ; 0.240 ; 0.500
REMARK 3 MEDIUM THERMAL 1 A (A**2): 592 ; 0.570 ; 2.000
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
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
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 2HT6 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-JUL-06.
REMARK 100 THE RCSB ID CODE IS RCSB038731.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-DEC-04
REMARK 200 TEMPERATURE (KELVIN) : 110
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9788
REMARK 200 MONOCHROMATOR : SI111 OR SI311 CRYSTALS
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16469
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.07300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 21.8000
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 (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.28200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 9.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SAD - INVERSE BEAM
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.07
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 8000, 0.1 M HEPES, 0.1 M
REMARK 280 SODIUM CHLORIDE, 0.5 MM MAGNESIUM CHLORIDE, 1 MM DTT, PH 7.5,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 292K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 19.92150
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 62.04750
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.71650
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 62.04750
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 19.92150
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 40.71650
REMARK 290 SMTRY3 4 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: MONOMERIC
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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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 GLY A 70
REMARK 465 SER A 71
REMARK 465 HIS A 99
REMARK 465 ASP A 100
REMARK 465 SER A 101
REMARK 465 MET A 102
REMARK 465 GLY A 137
REMARK 465 GLU A 138
REMARK 465 GLY B 70
REMARK 465 SER B 71
REMARK 465 GLY B 72
REMARK 465 ASN B 73
REMARK 465 ASP B 100
REMARK 465 SER B 101
REMARK 465 MET B 102
REMARK 465 ASP B 103
REMARK 465 GLY B 137
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 HIS B 99 CG ND1 CD2 CE1 NE2
REMARK 470 GLU B 138 CG CD OE1 OE2
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 THR A 74 CG2
REMARK 480 THR B 74 CG2
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 OE2 GLU B 83 ND2 ASN B 135 1.96
REMARK 500 OG SER A 169 O HOH A 843 2.18
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 835 O HOH B 827 2555 2.00
REMARK 500 CZ ARG B 177 O HOH A 844 3655 2.01
REMARK 500 NH2 ARG B 177 O HOH A 844 3655 2.04
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 THR A 74 OG1 - CB - CG2 ANGL. DEV. = -23.8 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 ASN A 73 -43.13 130.50
REMARK 500 GLU A 111 -91.89 -26.48
REMARK 500 LYS A 192 33.78 75.80
REMARK 500 ARG A 242 54.96 -104.98
REMARK 500 VAL B 98 -95.78 -116.23
REMARK 500 GLU B 111 -79.25 -36.30
REMARK 500 ASN B 139 178.98 126.97
REMARK 500 LYS B 192 38.45 74.10
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 B 138 ASN B 139 147.58
REMARK 500 ASN B 139 GLU B 140 -117.77
REMARK 500
REMARK 500 REMARK: NULL
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 MG A 344 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GDP A 545 O3B
REMARK 620 2 SER A 89 OG 85.3
REMARK 620 3 HOH A 808 O 84.1 81.1
REMARK 620 4 HOH A 834 O 96.3 95.6 176.6
REMARK 620 5 HOH A 874 O 168.5 86.8 86.4 92.8
REMARK 620 6 HOH A 884 O 94.3 173.2 92.1 91.1 92.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 444 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER B 89 OG
REMARK 620 2 HOH B 821 O 173.8
REMARK 620 3 HOH B 822 O 90.7 83.4
REMARK 620 4 GDP B 645 O3B 92.7 84.6 79.5
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 344
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 444
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP A 545
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP B 645
DBREF 2HT6 A 71 243 UNP P55040 GEM_HUMAN 71 243
DBREF 2HT6 B 71 243 UNP P55040 GEM_HUMAN 71 243
SEQADV 2HT6 GLY A 70 UNP P55040 CLONING ARTIFACT
SEQADV 2HT6 GLY B 70 UNP P55040 CLONING ARTIFACT
SEQRES 1 A 174 GLY SER GLY ASN THR TYR TYR ARG VAL VAL LEU ILE GLY
SEQRES 2 A 174 GLU GLN GLY VAL GLY LYS SER THR LEU ALA ASN ILE PHE
SEQRES 3 A 174 ALA GLY VAL HIS ASP SER MET ASP SER ASP CYS GLU VAL
SEQRES 4 A 174 LEU GLY GLU ASP THR TYR GLU ARG THR LEU MET VAL ASP
SEQRES 5 A 174 GLY GLU SER ALA THR ILE ILE LEU LEU ASP MET TRP GLU
SEQRES 6 A 174 ASN LYS GLY GLU ASN GLU TRP LEU HIS ASP HIS CYS MET
SEQRES 7 A 174 GLN VAL GLY ASP ALA TYR LEU ILE VAL TYR SER ILE THR
SEQRES 8 A 174 ASP ARG ALA SER PHE GLU LYS ALA SER GLU LEU ARG ILE
SEQRES 9 A 174 GLN LEU ARG ARG ALA ARG GLN THR GLU ASP ILE PRO ILE
SEQRES 10 A 174 ILE LEU VAL GLY ASN LYS SER ASP LEU VAL ARG CYS ARG
SEQRES 11 A 174 GLU VAL SER VAL SER GLU GLY ARG ALA CYS ALA VAL VAL
SEQRES 12 A 174 PHE ASP CYS LYS PHE ILE GLU THR SER ALA ALA VAL GLN
SEQRES 13 A 174 HIS ASN VAL LYS GLU LEU PHE GLU GLY ILE VAL ARG GLN
SEQRES 14 A 174 VAL ARG LEU ARG ARG
SEQRES 1 B 174 GLY SER GLY ASN THR TYR TYR ARG VAL VAL LEU ILE GLY
SEQRES 2 B 174 GLU GLN GLY VAL GLY LYS SER THR LEU ALA ASN ILE PHE
SEQRES 3 B 174 ALA GLY VAL HIS ASP SER MET ASP SER ASP CYS GLU VAL
SEQRES 4 B 174 LEU GLY GLU ASP THR TYR GLU ARG THR LEU MET VAL ASP
SEQRES 5 B 174 GLY GLU SER ALA THR ILE ILE LEU LEU ASP MET TRP GLU
SEQRES 6 B 174 ASN LYS GLY GLU ASN GLU TRP LEU HIS ASP HIS CYS MET
SEQRES 7 B 174 GLN VAL GLY ASP ALA TYR LEU ILE VAL TYR SER ILE THR
SEQRES 8 B 174 ASP ARG ALA SER PHE GLU LYS ALA SER GLU LEU ARG ILE
SEQRES 9 B 174 GLN LEU ARG ARG ALA ARG GLN THR GLU ASP ILE PRO ILE
SEQRES 10 B 174 ILE LEU VAL GLY ASN LYS SER ASP LEU VAL ARG CYS ARG
SEQRES 11 B 174 GLU VAL SER VAL SER GLU GLY ARG ALA CYS ALA VAL VAL
SEQRES 12 B 174 PHE ASP CYS LYS PHE ILE GLU THR SER ALA ALA VAL GLN
SEQRES 13 B 174 HIS ASN VAL LYS GLU LEU PHE GLU GLY ILE VAL ARG GLN
SEQRES 14 B 174 VAL ARG LEU ARG ARG
HET MG A 344 1
HET MG B 444 1
HET GDP A 545 28
HET GDP B 645 28
HETNAM MG MAGNESIUM ION
HETNAM GDP GUANOSINE-5'-DIPHOSPHATE
FORMUL 3 MG 2(MG 2+)
FORMUL 5 GDP 2(C10 H15 N5 O11 P2)
FORMUL 7 HOH *85(H2 O)
HELIX 1 1 GLY A 87 ALA A 96 1 10
HELIX 2 2 GLU A 140 GLY A 150 1 11
HELIX 3 3 ASP A 161 ARG A 179 1 19
HELIX 4 4 LEU A 195 ARG A 199 5 5
HELIX 5 5 SER A 202 ASP A 214 1 13
HELIX 6 6 ASN A 227 ARG A 242 1 16
HELIX 7 7 GLY B 87 ALA B 96 1 10
HELIX 8 8 GLU B 140 GLY B 150 1 11
HELIX 9 9 ASP B 161 ARG B 179 1 19
HELIX 10 10 LEU B 195 ARG B 199 5 5
HELIX 11 11 SER B 202 ASP B 214 1 13
HELIX 12 12 ASN B 227 LEU B 241 1 15
SHEET 1 A 6 THR A 113 VAL A 120 0
SHEET 2 A 6 GLU A 123 LEU A 130 -1 O ALA A 125 N LEU A 118
SHEET 3 A 6 TYR A 75 ILE A 81 1 N VAL A 78 O LEU A 130
SHEET 4 A 6 ALA A 152 SER A 158 1 O VAL A 156 N ILE A 81
SHEET 5 A 6 ILE A 186 ASN A 191 1 O ASN A 191 N TYR A 157
SHEET 6 A 6 LYS A 216 GLU A 219 1 O LYS A 216 N LEU A 188
SHEET 1 B 6 THR B 113 VAL B 120 0
SHEET 2 B 6 GLU B 123 LEU B 130 -1 O ALA B 125 N LEU B 118
SHEET 3 B 6 TYR B 75 ILE B 81 1 N TYR B 76 O THR B 126
SHEET 4 B 6 ALA B 152 SER B 158 1 O VAL B 156 N ILE B 81
SHEET 5 B 6 ILE B 186 ASN B 191 1 O ASN B 191 N TYR B 157
SHEET 6 B 6 LYS B 216 GLU B 219 1 O LYS B 216 N LEU B 188
LINK MG MG A 344 O3B GDP A 545 1555 1555 2.07
LINK MG MG A 344 OG SER A 89 1555 1555 2.06
LINK MG MG A 344 O HOH A 808 1555 1555 2.28
LINK MG MG A 344 O HOH A 834 1555 1555 2.23
LINK MG MG A 344 O HOH A 874 1555 1555 2.08
LINK MG MG A 344 O HOH A 884 1555 1555 2.05
LINK MG MG B 444 OG SER B 89 1555 1555 2.08
LINK MG MG B 444 O HOH B 821 1555 1555 2.32
LINK MG MG B 444 O HOH B 822 1555 1555 2.11
LINK MG MG B 444 O3B GDP B 645 1555 1555 2.16
SITE 1 AC1 6 SER A 89 GDP A 545 HOH A 808 HOH A 834
SITE 2 AC1 6 HOH A 874 HOH A 884
SITE 1 AC2 4 SER B 89 GDP B 645 HOH B 821 HOH B 822
SITE 1 AC3 17 GLY A 85 VAL A 86 GLY A 87 LYS A 88
SITE 2 AC3 17 SER A 89 THR A 90 ASN A 191 LYS A 192
SITE 3 AC3 17 ASP A 194 LEU A 195 SER A 221 ALA A 222
SITE 4 AC3 17 ALA A 223 MG A 344 HOH A 808 HOH A 866
SITE 5 AC3 17 HOH A 884
SITE 1 AC4 16 GLY B 85 VAL B 86 GLY B 87 LYS B 88
SITE 2 AC4 16 SER B 89 THR B 90 ASN B 191 LYS B 192
SITE 3 AC4 16 ASP B 194 LEU B 195 SER B 221 ALA B 222
SITE 4 AC4 16 ALA B 223 MG B 444 HOH B 821 HOH B 822
CRYST1 39.843 81.433 124.095 90.00 90.00 90.00 P 21 21 21 8
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 0.025099 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012280 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008058 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
