HEADER PROTEIN TRANSPORT 08-DEC-11 4ABM
TITLE CRYSTAL STRUCTURE OF CHMP4B HAIRPIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHARGED MULTIVESICULAR BODY PROTEIN 4B;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: CHMP4B HAIRPIN, RESIDUES 23-97;
COMPND 5 SYNONYM: CHROMATIN-MODIFYING PROTEIN 4B, CHMP4B, SNF7 HOMOLOG
COMPND 6 ASSOCIATED WITH ALIX 1, SNF7-2, HSNF7-2, VACUOLAR PROTEIN SORTING-
COMPND 7 ASSOCIATED PROTEIN 32-2, VPS32-2, HVPS32-2;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS CELL CYCLE, PROTEIN TRANSPORT, HIV-1
EXPDTA X-RAY DIFFRACTION
AUTHOR N.MARTINELLI,B.HARTLIEB,Y.USAMI,C.SABIN,A.DORDOR,E.A.RIBEIRO,
AUTHOR 2 H.GOTTLINGER,W.WEISSENHORN
REVDAT 2 24-JAN-18 4ABM 1 SOURCE
REVDAT 1 09-MAY-12 4ABM 0
JRNL AUTH N.MARTINELLI,B.HARTLIEB,Y.USAMI,C.SABIN,A.DORDOR,N.MIGUET,
JRNL AUTH 2 S.V.AVILOV,E.A.RIBEIRO,H.GOTTLINGER,W.WEISSENHORN
JRNL TITL CC2D1A IS A REGULATOR OF ESCRT-III CHMP4B.
JRNL REF J.MOL.BIOL. V. 419 75 2012
JRNL REFN ISSN 0022-2836
JRNL PMID 22406677
JRNL DOI 10.1016/J.JMB.2012.02.044
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 61.86
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 30007
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) : 0.230
REMARK 3 R VALUE (WORKING SET) : 0.228
REMARK 3 FREE R VALUE : 0.285
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1588
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) : 1954
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2680
REMARK 3 BIN FREE R VALUE SET COUNT : 123
REMARK 3 BIN FREE R VALUE : 0.3130
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2568
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 137
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.03000
REMARK 3 B22 (A**2) : 0.06000
REMARK 3 B33 (A**2) : -0.04000
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): 0.162
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.161
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.104
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.462
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.929
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.883
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2720 ; 0.018 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3621 ; 0.884 ; 1.988
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 : 4
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 : A 1 A 79
REMARK 3 ORIGIN FOR THE GROUP (A): 6.4780 41.4425 12.7617
REMARK 3 T TENSOR
REMARK 3 T11: 0.0214 T22: 0.0471
REMARK 3 T33: 0.1080 T12: 0.0049
REMARK 3 T13: 0.0044 T23: -0.0250
REMARK 3 L TENSOR
REMARK 3 L11: 1.2866 L22: 3.1517
REMARK 3 L33: 2.8441 L12: -1.8317
REMARK 3 L13: -1.3794 L23: 2.0355
REMARK 3 S TENSOR
REMARK 3 S11: 0.1087 S12: 0.0912 S13: 0.1151
REMARK 3 S21: -0.1247 S22: -0.1057 S23: -0.0313
REMARK 3 S31: -0.1468 S32: -0.1732 S33: -0.0030
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 : B 1 B 79
REMARK 3 ORIGIN FOR THE GROUP (A): 18.6576 17.3875 9.5986
REMARK 3 T TENSOR
REMARK 3 T11: 0.0703 T22: 0.0537
REMARK 3 T33: 0.0336 T12: 0.0031
REMARK 3 T13: 0.0068 T23: 0.0103
REMARK 3 L TENSOR
REMARK 3 L11: 5.7206 L22: 2.8513
REMARK 3 L33: 0.5842 L12: -3.2914
REMARK 3 L13: -1.4322 L23: 1.0446
REMARK 3 S TENSOR
REMARK 3 S11: -0.1989 S12: -0.1926 S13: -0.2349
REMARK 3 S21: 0.1913 S22: 0.0841 S23: 0.1601
REMARK 3 S31: 0.0944 S32: 0.0944 S33: 0.1148
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 1 C 78
REMARK 3 ORIGIN FOR THE GROUP (A): 24.4152 37.0454 20.6740
REMARK 3 T TENSOR
REMARK 3 T11: 0.0602 T22: 0.0604
REMARK 3 T33: 0.1047 T12: -0.0005
REMARK 3 T13: 0.0012 T23: -0.0471
REMARK 3 L TENSOR
REMARK 3 L11: 1.8288 L22: 2.2130
REMARK 3 L33: 4.7011 L12: -0.7388
REMARK 3 L13: 0.7460 L23: -2.3953
REMARK 3 S TENSOR
REMARK 3 S11: -0.0098 S12: 0.1687 S13: -0.0100
REMARK 3 S21: 0.0482 S22: 0.0335 S23: 0.0456
REMARK 3 S31: 0.1628 S32: 0.0899 S33: -0.0238
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 3 D 79
REMARK 3 ORIGIN FOR THE GROUP (A): 11.2251 21.0748 25.4593
REMARK 3 T TENSOR
REMARK 3 T11: 0.1443 T22: 0.0745
REMARK 3 T33: 0.0502 T12: -0.0488
REMARK 3 T13: 0.0663 T23: -0.0116
REMARK 3 L TENSOR
REMARK 3 L11: 1.3112 L22: 5.5701
REMARK 3 L33: 3.0753 L12: -0.3847
REMARK 3 L13: 1.0594 L23: 2.7152
REMARK 3 S TENSOR
REMARK 3 S11: -0.0013 S12: -0.0579 S13: 0.0393
REMARK 3 S21: -0.0922 S22: -0.1548 S23: 0.1016
REMARK 3 S31: -0.0329 S32: -0.1717 S33: 0.1561
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 RIDING
REMARK 3 POSITIONS. HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT
REMARK 4
REMARK 4 4ABM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-DEC-11.
REMARK 100 THE DEPOSITION ID IS D_1290050652.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
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) : 0.9795
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : IMOSFLM
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30007
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 41.230
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 4.400
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 7.800
REMARK 200 R MERGE (I) : 0.27000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.3000
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) : 1.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.10
REMARK 200 R MERGE FOR SHELL (I) : 0.41000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELX
REMARK 200 STARTING MODEL: NONE
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.19
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 18.79500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 61.84000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.71500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 61.84000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 18.79500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 35.71500
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, 3
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: 1740 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10510 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.7 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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
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 C 97
REMARK 465 GLY D 19
REMARK 465 ALA D 20
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 2055 O HOH B 2023 2.00
REMARK 500 OE1 GLU B 90 NH1 ARG B 93 2.03
REMARK 500 O HOH A 2027 O HOH D 2004 2.18
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 B 61 74.05 -150.25
REMARK 500 THR C 59 -46.82 -146.23
REMARK 500 LYS C 60 36.47 70.12
REMARK 500 ARG C 63 -7.67 -56.79
REMARK 500 LYS D 56 37.71 -90.22
REMARK 500 LYS D 60 -72.14 -140.66
REMARK 500
REMARK 500 REMARK: NULL
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 FOUR ADDITIONAL RESIDUES AT THE N-TERMINUS
DBREF 4ABM A 23 97 UNP Q9H444 CHM4B_HUMAN 23 97
DBREF 4ABM B 23 97 UNP Q9H444 CHM4B_HUMAN 23 97
DBREF 4ABM C 23 97 UNP Q9H444 CHM4B_HUMAN 23 97
DBREF 4ABM D 23 97 UNP Q9H444 CHM4B_HUMAN 23 97
SEQADV 4ABM GLY A 19 UNP Q9H444 EXPRESSION TAG
SEQADV 4ABM ALA A 20 UNP Q9H444 EXPRESSION TAG
SEQADV 4ABM MET A 21 UNP Q9H444 EXPRESSION TAG
SEQADV 4ABM GLU A 22 UNP Q9H444 EXPRESSION TAG
SEQADV 4ABM GLY B 19 UNP Q9H444 EXPRESSION TAG
SEQADV 4ABM ALA B 20 UNP Q9H444 EXPRESSION TAG
SEQADV 4ABM MET B 21 UNP Q9H444 EXPRESSION TAG
SEQADV 4ABM GLU B 22 UNP Q9H444 EXPRESSION TAG
SEQADV 4ABM GLY C 19 UNP Q9H444 EXPRESSION TAG
SEQADV 4ABM ALA C 20 UNP Q9H444 EXPRESSION TAG
SEQADV 4ABM MET C 21 UNP Q9H444 EXPRESSION TAG
SEQADV 4ABM GLU C 22 UNP Q9H444 EXPRESSION TAG
SEQADV 4ABM GLY D 19 UNP Q9H444 EXPRESSION TAG
SEQADV 4ABM ALA D 20 UNP Q9H444 EXPRESSION TAG
SEQADV 4ABM MET D 21 UNP Q9H444 EXPRESSION TAG
SEQADV 4ABM GLU D 22 UNP Q9H444 EXPRESSION TAG
SEQRES 1 A 79 GLY ALA MET GLU GLN GLU ALA ILE GLN ARG LEU ARG ASP
SEQRES 2 A 79 THR GLU GLU MET LEU SER LYS LYS GLN GLU PHE LEU GLU
SEQRES 3 A 79 LYS LYS ILE GLU GLN GLU LEU THR ALA ALA LYS LYS HIS
SEQRES 4 A 79 GLY THR LYS ASN LYS ARG ALA ALA LEU GLN ALA LEU LYS
SEQRES 5 A 79 ARG LYS LYS ARG TYR GLU LYS GLN LEU ALA GLN ILE ASP
SEQRES 6 A 79 GLY THR LEU SER THR ILE GLU PHE GLN ARG GLU ALA LEU
SEQRES 7 A 79 GLU
SEQRES 1 B 79 GLY ALA MET GLU GLN GLU ALA ILE GLN ARG LEU ARG ASP
SEQRES 2 B 79 THR GLU GLU MET LEU SER LYS LYS GLN GLU PHE LEU GLU
SEQRES 3 B 79 LYS LYS ILE GLU GLN GLU LEU THR ALA ALA LYS LYS HIS
SEQRES 4 B 79 GLY THR LYS ASN LYS ARG ALA ALA LEU GLN ALA LEU LYS
SEQRES 5 B 79 ARG LYS LYS ARG TYR GLU LYS GLN LEU ALA GLN ILE ASP
SEQRES 6 B 79 GLY THR LEU SER THR ILE GLU PHE GLN ARG GLU ALA LEU
SEQRES 7 B 79 GLU
SEQRES 1 C 79 GLY ALA MET GLU GLN GLU ALA ILE GLN ARG LEU ARG ASP
SEQRES 2 C 79 THR GLU GLU MET LEU SER LYS LYS GLN GLU PHE LEU GLU
SEQRES 3 C 79 LYS LYS ILE GLU GLN GLU LEU THR ALA ALA LYS LYS HIS
SEQRES 4 C 79 GLY THR LYS ASN LYS ARG ALA ALA LEU GLN ALA LEU LYS
SEQRES 5 C 79 ARG LYS LYS ARG TYR GLU LYS GLN LEU ALA GLN ILE ASP
SEQRES 6 C 79 GLY THR LEU SER THR ILE GLU PHE GLN ARG GLU ALA LEU
SEQRES 7 C 79 GLU
SEQRES 1 D 79 GLY ALA MET GLU GLN GLU ALA ILE GLN ARG LEU ARG ASP
SEQRES 2 D 79 THR GLU GLU MET LEU SER LYS LYS GLN GLU PHE LEU GLU
SEQRES 3 D 79 LYS LYS ILE GLU GLN GLU LEU THR ALA ALA LYS LYS HIS
SEQRES 4 D 79 GLY THR LYS ASN LYS ARG ALA ALA LEU GLN ALA LEU LYS
SEQRES 5 D 79 ARG LYS LYS ARG TYR GLU LYS GLN LEU ALA GLN ILE ASP
SEQRES 6 D 79 GLY THR LEU SER THR ILE GLU PHE GLN ARG GLU ALA LEU
SEQRES 7 D 79 GLU
FORMUL 5 HOH *137(H2 O)
HELIX 1 1 GLY A 19 GLY A 58 1 40
HELIX 2 2 ASN A 61 GLU A 97 1 37
HELIX 3 3 GLY B 19 GLY B 58 1 40
HELIX 4 4 ASN B 61 GLU B 97 1 37
HELIX 5 5 GLY C 19 HIS C 57 1 39
HELIX 6 6 ARG C 63 LEU C 96 1 34
HELIX 7 7 MET D 21 LYS D 56 1 36
HELIX 8 8 ASN D 61 ALA D 95 1 35
CISPEP 1 HIS C 57 GLY C 58 0 -13.39
CISPEP 2 THR C 59 LYS C 60 0 -10.96
CRYST1 37.590 71.430 123.680 90.00 90.00 90.00 P 21 21 21 16
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 0.026603 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014000 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008085 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
