HEADER SUGAR BINDING PROTEIN 24-MAR-06 2GGX
TITLE CRYSTAL STRUCTURE OF THE TRIMER NECK AND CARBOHYDRATE RECOGNITION
TITLE 2 DOMAIN OF HUMAN SURFACTANT PROTEIN D IN COMPLEX WITH P-NITROPHENYL
TITLE 3 MALTOSIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PULMONARY SURFACTANT-ASSOCIATED PROTEIN D;
COMPND 3 CHAIN: A, B, C;
COMPND 4 FRAGMENT: TRIMERIC NECK AND CARBOHYDRATE RECOGNITION DOMAIN;
COMPND 5 SYNONYM: SP-D, PSP-D;
COMPND 6 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: SFTPD;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA BLUE;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET-30A(+)
KEYWDS PROTEIN-CARBOHYDRATE LIGAND COMPLEX, SUGAR BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR J.HEAD
REVDAT 5 30-AUG-23 2GGX 1 REMARK SEQADV LINK
REVDAT 4 18-OCT-17 2GGX 1 REMARK
REVDAT 3 24-FEB-09 2GGX 1 VERSN
REVDAT 2 11-JUL-06 2GGX 1 JRNL
REVDAT 1 02-MAY-06 2GGX 0
JRNL AUTH E.CROUCH,B.MCDONALD,K.SMITH,T.CAFARELLA,B.SEATON,J.HEAD
JRNL TITL CONTRIBUTIONS OF PHENYLALANINE 335 TO LIGAND RECOGNITION BY
JRNL TITL 2 HUMAN SURFACTANT PROTEIN D: RING INTERACTIONS WITH SP-D
JRNL TITL 3 LIGANDS
JRNL REF J.BIOL.CHEM. V. 281 18008 2006
JRNL REFN ISSN 0021-9258
JRNL PMID 16636058
JRNL DOI 10.1074/JBC.M601749200
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.9
REMARK 3 NUMBER OF REFLECTIONS : 48078
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.214
REMARK 3 FREE R VALUE : 0.238
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.900
REMARK 3 FREE R VALUE TEST SET COUNT : 3953
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.91
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2620
REMARK 3 BIN FREE R VALUE : 0.3180
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 55
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3462
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 105
REMARK 3 SOLVENT ATOMS : 256
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.23
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.14400
REMARK 3 B22 (A**2) : -5.64600
REMARK 3 B33 (A**2) : 1.50100
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.71300
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.282 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.857 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.965 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.859 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 43.10
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : CNS_TOPPAR:PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : NPN.PAR
REMARK 3 PARAMETER FILE 3 : CNS_TOPPAR:ION.PARAM
REMARK 3 PARAMETER FILE 4 : CNS_TOPPAR:WATER.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2GGX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-APR-06.
REMARK 100 THE DEPOSITION ID IS D_1000037103.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-NOV-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X8C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 50803
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : 0.06900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.30
REMARK 200 R MERGE FOR SHELL (I) : 0.28700
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: CNS
REMARK 200 STARTING MODEL: 1PWB
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.71
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.13
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 12% PEG 8000, 150MM NACL, 10MM CACL2,
REMARK 280 100MM HEPES, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 290K
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 53.20000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8370 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20770 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -161.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 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 ALA A 196
REMARK 465 MET A 197
REMARK 465 ALA A 198
REMARK 465 ASP A 199
REMARK 465 ILE A 200
REMARK 465 GLY A 201
REMARK 465 SER A 202
REMARK 465 ASP A 203
REMARK 465 VAL A 204
REMARK 465 ALA B 196
REMARK 465 MET B 197
REMARK 465 ALA B 198
REMARK 465 ASP B 199
REMARK 465 ILE B 200
REMARK 465 GLY B 201
REMARK 465 SER B 202
REMARK 465 ASP B 203
REMARK 465 VAL B 204
REMARK 465 ALA C 196
REMARK 465 MET C 197
REMARK 465 ALA C 198
REMARK 465 ASP C 199
REMARK 465 ILE C 200
REMARK 465 GLY C 201
REMARK 465 SER C 202
REMARK 465 ASP C 203
REMARK 465 VAL C 204
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 316 48.29 -141.45
REMARK 500 SER A 328 65.81 -156.07
REMARK 500 ASP B 324 56.04 37.07
REMARK 500 SER B 328 52.68 -146.34
REMARK 500 ARG C 208 11.28 46.48
REMARK 500 ASN C 316 50.46 -141.60
REMARK 500 ASP C 324 51.70 35.87
REMARK 500 SER C 328 49.62 -150.88
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 CA A 402 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 297 OD1
REMARK 620 2 ASP A 297 OD2 50.2
REMARK 620 3 GLU A 301 OE1 99.4 78.2
REMARK 620 4 GLU A 301 OE2 121.5 72.8 51.1
REMARK 620 5 ASP A 324 OD1 158.6 150.1 84.5 77.3
REMARK 620 6 GLU A 329 O 89.2 126.5 151.2 142.8 78.1
REMARK 620 7 ASP A 330 OD1 73.4 113.3 79.5 129.0 86.8 76.7
REMARK 620 8 HOH A 777 O 101.1 79.5 128.0 77.5 92.6 76.1 152.3
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 403 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 301 OE1
REMARK 620 2 ASP A 330 OD1 78.5
REMARK 620 3 ASP A 330 OD2 117.0 51.1
REMARK 620 4 HOH A 703 O 81.2 102.8 77.0
REMARK 620 5 HOH A 784 O 158.3 122.8 79.3 89.4
REMARK 620 6 HOH A 788 O 71.9 97.5 139.0 142.2 105.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 401 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 321 OE1
REMARK 620 2 ASN A 323 OD1 73.7
REMARK 620 3 GLU A 329 OE1 147.2 77.5
REMARK 620 4 ASN A 341 OD1 71.8 141.9 139.8
REMARK 620 5 ASP A 342 O 129.4 141.7 69.3 75.0
REMARK 620 6 ASP A 342 OD1 76.8 88.3 87.1 99.0 71.9
REMARK 620 7 NPJ A 700 O3A 75.7 76.5 112.4 79.8 133.5 151.4
REMARK 620 8 NPJ A 700 O4A 135.3 115.6 72.2 79.9 71.9 142.8 65.6
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 402 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 297 OD2
REMARK 620 2 ASP B 297 OD1 51.5
REMARK 620 3 GLU B 301 OE2 73.4 123.6
REMARK 620 4 GLU B 301 OE1 76.3 99.7 50.7
REMARK 620 5 ASP B 324 OD1 148.7 157.6 75.4 83.2
REMARK 620 6 GLU B 329 O 132.0 91.0 141.5 147.4 75.9
REMARK 620 7 ASP B 330 OD1 111.4 73.4 125.3 76.6 85.9 77.1
REMARK 620 8 HOH B 783 O 82.5 101.7 79.5 129.5 93.1 77.0 153.6
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 403 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 301 OE1
REMARK 620 2 ASP B 330 OD2 118.9
REMARK 620 3 ASP B 330 OD1 74.5 51.8
REMARK 620 4 HOH B 781 O 85.3 155.6 148.6
REMARK 620 5 HOH B 784 O 85.6 100.4 71.5 83.5
REMARK 620 6 HOH B 787 O 85.4 87.7 110.2 91.4 170.0
REMARK 620 7 HOH B 788 O 163.0 76.6 115.0 79.9 84.5 103.1
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 401 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 321 OE1
REMARK 620 2 ASN B 323 OD1 75.1
REMARK 620 3 GLU B 329 OE1 148.8 78.9
REMARK 620 4 ASN B 341 OD1 66.5 136.5 143.4
REMARK 620 5 ASP B 342 O 122.5 142.5 71.5 78.4
REMARK 620 6 ASP B 342 OD1 72.1 86.4 89.4 100.1 71.1
REMARK 620 7 NPJ B 700 O3A 76.6 76.2 113.6 75.7 136.9 147.2
REMARK 620 8 NPJ B 700 O4A 137.9 116.0 69.9 82.7 74.9 144.4 68.1
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 402 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 297 OD2
REMARK 620 2 ASP C 297 OD1 50.4
REMARK 620 3 GLU C 301 OE1 81.5 101.9
REMARK 620 4 GLU C 301 OE2 74.8 123.4 50.9
REMARK 620 5 ASP C 324 OD1 152.0 155.9 81.1 77.2
REMARK 620 6 GLU C 329 O 132.2 92.7 142.5 140.9 72.4
REMARK 620 7 ASP C 330 OD1 109.8 71.4 75.1 125.1 86.6 77.3
REMARK 620 8 HOH C 702 O 83.8 103.9 131.0 80.2 91.3 76.5 153.1
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 403 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 301 OE1
REMARK 620 2 ASP C 330 OD2 120.8
REMARK 620 3 ASP C 330 OD1 73.1 49.6
REMARK 620 4 HOH C 774 O 88.5 150.5 154.4
REMARK 620 5 HOH C 776 O 79.3 95.5 73.6 85.9
REMARK 620 6 HOH C 777 O 164.5 74.1 119.9 76.5 95.7
REMARK 620 7 HOH C 779 O 90.7 91.7 106.0 91.5 169.7 93.3
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 401 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 321 OE1
REMARK 620 2 ASN C 323 ND2 73.0
REMARK 620 3 GLU C 329 OE1 149.1 80.9
REMARK 620 4 ASN C 341 OD1 69.4 139.5 139.3
REMARK 620 5 ASP C 342 O 127.4 142.7 68.0 75.2
REMARK 620 6 ASP C 342 OD1 74.7 85.8 87.4 98.2 73.2
REMARK 620 7 NPJ C 700 O4A 137.3 114.0 68.8 85.2 74.0 144.9
REMARK 620 8 NPJ C 700 O3A 73.4 75.8 116.0 79.7 136.0 146.7 68.4
REMARK 620 N 1 2 3 4 5 6 7
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NPJ A 700
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NPJ B 700
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NPJ C 700
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2GGU RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH MALTOTRIOSE
DBREF 2GGX A 203 355 UNP P35247 SFTPD_HUMAN 223 375
DBREF 2GGX B 203 355 UNP P35247 SFTPD_HUMAN 223 375
DBREF 2GGX C 203 355 UNP P35247 SFTPD_HUMAN 223 375
SEQADV 2GGX ALA A 196 UNP P35247 CLONING ARTIFACT
SEQADV 2GGX MET A 197 UNP P35247 CLONING ARTIFACT
SEQADV 2GGX ALA A 198 UNP P35247 CLONING ARTIFACT
SEQADV 2GGX ASP A 199 UNP P35247 CLONING ARTIFACT
SEQADV 2GGX ILE A 200 UNP P35247 CLONING ARTIFACT
SEQADV 2GGX GLY A 201 UNP P35247 CLONING ARTIFACT
SEQADV 2GGX SER A 202 UNP P35247 CLONING ARTIFACT
SEQADV 2GGX ALA B 196 UNP P35247 CLONING ARTIFACT
SEQADV 2GGX MET B 197 UNP P35247 CLONING ARTIFACT
SEQADV 2GGX ALA B 198 UNP P35247 CLONING ARTIFACT
SEQADV 2GGX ASP B 199 UNP P35247 CLONING ARTIFACT
SEQADV 2GGX ILE B 200 UNP P35247 CLONING ARTIFACT
SEQADV 2GGX GLY B 201 UNP P35247 CLONING ARTIFACT
SEQADV 2GGX SER B 202 UNP P35247 CLONING ARTIFACT
SEQADV 2GGX ALA C 196 UNP P35247 CLONING ARTIFACT
SEQADV 2GGX MET C 197 UNP P35247 CLONING ARTIFACT
SEQADV 2GGX ALA C 198 UNP P35247 CLONING ARTIFACT
SEQADV 2GGX ASP C 199 UNP P35247 CLONING ARTIFACT
SEQADV 2GGX ILE C 200 UNP P35247 CLONING ARTIFACT
SEQADV 2GGX GLY C 201 UNP P35247 CLONING ARTIFACT
SEQADV 2GGX SER C 202 UNP P35247 CLONING ARTIFACT
SEQRES 1 A 160 ALA MET ALA ASP ILE GLY SER ASP VAL ALA SER LEU ARG
SEQRES 2 A 160 GLN GLN VAL GLU ALA LEU GLN GLY GLN VAL GLN HIS LEU
SEQRES 3 A 160 GLN ALA ALA PHE SER GLN TYR LYS LYS VAL GLU LEU PHE
SEQRES 4 A 160 PRO ASN GLY GLN SER VAL GLY GLU LYS ILE PHE LYS THR
SEQRES 5 A 160 ALA GLY PHE VAL LYS PRO PHE THR GLU ALA GLN LEU LEU
SEQRES 6 A 160 CYS THR GLN ALA GLY GLY GLN LEU ALA SER PRO ARG SER
SEQRES 7 A 160 ALA ALA GLU ASN ALA ALA LEU GLN GLN LEU VAL VAL ALA
SEQRES 8 A 160 LYS ASN GLU ALA ALA PHE LEU SER MET THR ASP SER LYS
SEQRES 9 A 160 THR GLU GLY LYS PHE THR TYR PRO THR GLY GLU SER LEU
SEQRES 10 A 160 VAL TYR SER ASN TRP ALA PRO GLY GLU PRO ASN ASP ASP
SEQRES 11 A 160 GLY GLY SER GLU ASP CYS VAL GLU ILE PHE THR ASN GLY
SEQRES 12 A 160 LYS TRP ASN ASP ARG ALA CYS GLY GLU LYS ARG LEU VAL
SEQRES 13 A 160 VAL CYS GLU PHE
SEQRES 1 B 160 ALA MET ALA ASP ILE GLY SER ASP VAL ALA SER LEU ARG
SEQRES 2 B 160 GLN GLN VAL GLU ALA LEU GLN GLY GLN VAL GLN HIS LEU
SEQRES 3 B 160 GLN ALA ALA PHE SER GLN TYR LYS LYS VAL GLU LEU PHE
SEQRES 4 B 160 PRO ASN GLY GLN SER VAL GLY GLU LYS ILE PHE LYS THR
SEQRES 5 B 160 ALA GLY PHE VAL LYS PRO PHE THR GLU ALA GLN LEU LEU
SEQRES 6 B 160 CYS THR GLN ALA GLY GLY GLN LEU ALA SER PRO ARG SER
SEQRES 7 B 160 ALA ALA GLU ASN ALA ALA LEU GLN GLN LEU VAL VAL ALA
SEQRES 8 B 160 LYS ASN GLU ALA ALA PHE LEU SER MET THR ASP SER LYS
SEQRES 9 B 160 THR GLU GLY LYS PHE THR TYR PRO THR GLY GLU SER LEU
SEQRES 10 B 160 VAL TYR SER ASN TRP ALA PRO GLY GLU PRO ASN ASP ASP
SEQRES 11 B 160 GLY GLY SER GLU ASP CYS VAL GLU ILE PHE THR ASN GLY
SEQRES 12 B 160 LYS TRP ASN ASP ARG ALA CYS GLY GLU LYS ARG LEU VAL
SEQRES 13 B 160 VAL CYS GLU PHE
SEQRES 1 C 160 ALA MET ALA ASP ILE GLY SER ASP VAL ALA SER LEU ARG
SEQRES 2 C 160 GLN GLN VAL GLU ALA LEU GLN GLY GLN VAL GLN HIS LEU
SEQRES 3 C 160 GLN ALA ALA PHE SER GLN TYR LYS LYS VAL GLU LEU PHE
SEQRES 4 C 160 PRO ASN GLY GLN SER VAL GLY GLU LYS ILE PHE LYS THR
SEQRES 5 C 160 ALA GLY PHE VAL LYS PRO PHE THR GLU ALA GLN LEU LEU
SEQRES 6 C 160 CYS THR GLN ALA GLY GLY GLN LEU ALA SER PRO ARG SER
SEQRES 7 C 160 ALA ALA GLU ASN ALA ALA LEU GLN GLN LEU VAL VAL ALA
SEQRES 8 C 160 LYS ASN GLU ALA ALA PHE LEU SER MET THR ASP SER LYS
SEQRES 9 C 160 THR GLU GLY LYS PHE THR TYR PRO THR GLY GLU SER LEU
SEQRES 10 C 160 VAL TYR SER ASN TRP ALA PRO GLY GLU PRO ASN ASP ASP
SEQRES 11 C 160 GLY GLY SER GLU ASP CYS VAL GLU ILE PHE THR ASN GLY
SEQRES 12 C 160 LYS TRP ASN ASP ARG ALA CYS GLY GLU LYS ARG LEU VAL
SEQRES 13 C 160 VAL CYS GLU PHE
HET CA A 401 1
HET CA A 402 1
HET CA A 403 1
HET NPJ A 700 32
HET CA B 401 1
HET CA B 402 1
HET CA B 403 1
HET NPJ B 700 32
HET CA C 401 1
HET CA C 402 1
HET CA C 403 1
HET NPJ C 700 32
HETNAM CA CALCIUM ION
HETNAM NPJ 4-NITROPHENYL 4-O-ALPHA-D-GLUCOPYRANOSYL-ALPHA-D-
HETNAM 2 NPJ GALACTOPYRANOSIDE
HETSYN NPJ P-NITROPHENYL MALTOSIDE
FORMUL 4 CA 9(CA 2+)
FORMUL 7 NPJ 3(C18 H25 N O13)
FORMUL 16 HOH *256(H2 O)
HELIX 1 1 LEU A 207 PHE A 234 1 28
HELIX 2 2 PHE A 254 ALA A 264 1 11
HELIX 3 3 SER A 273 ASN A 288 1 16
HELIX 4 4 ASP A 324 SER A 328 5 5
HELIX 5 5 ALA B 205 PHE B 234 1 30
HELIX 6 6 PHE B 254 ALA B 264 1 11
HELIX 7 7 SER B 273 ASN B 288 1 16
HELIX 8 8 ASP B 324 SER B 328 5 5
HELIX 9 9 ARG C 208 PHE C 234 1 27
HELIX 10 10 PHE C 254 ALA C 264 1 11
HELIX 11 11 SER C 273 ASN C 288 1 16
HELIX 12 12 ASP C 324 SER C 328 5 5
SHEET 1 A 4 GLY A 237 VAL A 240 0
SHEET 2 A 4 LYS A 243 PRO A 253 -1 O PHE A 245 N GLN A 238
SHEET 3 A 4 LYS A 348 PHE A 355 -1 O VAL A 351 N ALA A 248
SHEET 4 A 4 GLN A 267 LEU A 268 -1 N GLN A 267 O GLU A 354
SHEET 1 B 3 ALA A 291 PHE A 292 0
SHEET 2 B 3 CYS A 331 ILE A 334 -1 O ILE A 334 N ALA A 291
SHEET 3 B 3 TRP A 340 ARG A 343 -1 O ASN A 341 N GLU A 333
SHEET 1 C 2 THR A 296 THR A 300 0
SHEET 2 C 2 LYS A 303 THR A 305 -1 O THR A 305 N THR A 296
SHEET 1 D 4 GLY B 237 VAL B 240 0
SHEET 2 D 4 LYS B 243 PRO B 253 -1 O LYS B 243 N VAL B 240
SHEET 3 D 4 LYS B 348 PHE B 355 -1 O PHE B 355 N ILE B 244
SHEET 4 D 4 GLN B 267 LEU B 268 -1 N GLN B 267 O GLU B 354
SHEET 1 E 3 ALA B 291 PHE B 292 0
SHEET 2 E 3 CYS B 331 ILE B 334 -1 O ILE B 334 N ALA B 291
SHEET 3 E 3 TRP B 340 ARG B 343 -1 O ASN B 341 N GLU B 333
SHEET 1 F 4 GLY C 237 VAL C 240 0
SHEET 2 F 4 LYS C 243 PRO C 253 -1 O PHE C 245 N GLN C 238
SHEET 3 F 4 LYS C 348 PHE C 355 -1 O CYS C 353 N LYS C 246
SHEET 4 F 4 GLN C 267 LEU C 268 -1 N GLN C 267 O GLU C 354
SHEET 1 G 3 ALA C 291 PHE C 292 0
SHEET 2 G 3 CYS C 331 ILE C 334 -1 O ILE C 334 N ALA C 291
SHEET 3 G 3 TRP C 340 ARG C 343 -1 O ASN C 341 N GLU C 333
SSBOND 1 CYS A 261 CYS A 353 1555 1555 2.03
SSBOND 2 CYS A 331 CYS A 345 1555 1555 2.03
SSBOND 3 CYS B 261 CYS B 353 1555 1555 2.03
SSBOND 4 CYS B 331 CYS B 345 1555 1555 2.03
SSBOND 5 CYS C 261 CYS C 353 1555 1555 2.03
SSBOND 6 CYS C 331 CYS C 345 1555 1555 2.03
LINK OD1 ASP A 297 CA CA A 402 1555 1555 2.71
LINK OD2 ASP A 297 CA CA A 402 1555 1555 2.42
LINK OE1 GLU A 301 CA CA A 402 1555 1555 2.56
LINK OE2 GLU A 301 CA CA A 402 1555 1555 2.54
LINK OE1 GLU A 301 CA CA A 403 1555 1555 2.41
LINK OE1 GLU A 321 CA CA A 401 1555 1555 2.45
LINK OD1 ASN A 323 CA CA A 401 1555 1555 2.41
LINK OD1 ASP A 324 CA CA A 402 1555 1555 2.51
LINK OE1 GLU A 329 CA CA A 401 1555 1555 2.41
LINK O GLU A 329 CA CA A 402 1555 1555 2.45
LINK OD1 ASP A 330 CA CA A 402 1555 1555 2.41
LINK OD1 ASP A 330 CA CA A 403 1555 1555 2.61
LINK OD2 ASP A 330 CA CA A 403 1555 1555 2.49
LINK OD1 ASN A 341 CA CA A 401 1555 1555 2.50
LINK O ASP A 342 CA CA A 401 1555 1555 2.62
LINK OD1 ASP A 342 CA CA A 401 1555 1555 2.18
LINK CA CA A 401 O3A NPJ A 700 1555 1555 2.60
LINK CA CA A 401 O4A NPJ A 700 1555 1555 2.62
LINK CA CA A 402 O HOH A 777 1555 1555 2.32
LINK CA CA A 403 O HOH A 703 1555 1555 2.35
LINK CA CA A 403 O HOH A 784 1555 1555 2.42
LINK CA CA A 403 O HOH A 788 1555 1555 2.27
LINK OD2 ASP B 297 CA CA B 402 1555 1555 2.37
LINK OD1 ASP B 297 CA CA B 402 1555 1555 2.64
LINK OE2 GLU B 301 CA CA B 402 1555 1555 2.61
LINK OE1 GLU B 301 CA CA B 402 1555 1555 2.53
LINK OE1 GLU B 301 CA CA B 403 1555 1555 2.40
LINK OE1 GLU B 321 CA CA B 401 1555 1555 2.47
LINK OD1 ASN B 323 CA CA B 401 1555 1555 2.42
LINK OD1 ASP B 324 CA CA B 402 1555 1555 2.56
LINK OE1 GLU B 329 CA CA B 401 1555 1555 2.36
LINK O GLU B 329 CA CA B 402 1555 1555 2.45
LINK OD1 ASP B 330 CA CA B 402 1555 1555 2.37
LINK OD2 ASP B 330 CA CA B 403 1555 1555 2.41
LINK OD1 ASP B 330 CA CA B 403 1555 1555 2.61
LINK OD1 ASN B 341 CA CA B 401 1555 1555 2.42
LINK O ASP B 342 CA CA B 401 1555 1555 2.61
LINK OD1 ASP B 342 CA CA B 401 1555 1555 2.28
LINK CA CA B 401 O3A NPJ B 700 1555 1555 2.49
LINK CA CA B 401 O4A NPJ B 700 1555 1555 2.51
LINK CA CA B 402 O HOH B 783 1555 1555 2.39
LINK CA CA B 403 O HOH B 781 1555 1555 2.47
LINK CA CA B 403 O HOH B 784 1555 1555 2.41
LINK CA CA B 403 O HOH B 787 1555 1555 2.31
LINK CA CA B 403 O HOH B 788 1555 1555 2.42
LINK OD2 ASP C 297 CA CA C 402 1555 1555 2.47
LINK OD1 ASP C 297 CA CA C 402 1555 1555 2.66
LINK OE1 GLU C 301 CA CA C 402 1555 1555 2.57
LINK OE2 GLU C 301 CA CA C 402 1555 1555 2.55
LINK OE1 GLU C 301 CA CA C 403 1555 1555 2.30
LINK OE1 GLU C 321 CA CA C 401 1555 1555 2.61
LINK ND2 ASN C 323 CA CA C 401 1555 1555 2.47
LINK OD1 ASP C 324 CA CA C 402 1555 1555 2.50
LINK OE1 GLU C 329 CA CA C 401 1555 1555 2.32
LINK O GLU C 329 CA CA C 402 1555 1555 2.42
LINK OD1 ASP C 330 CA CA C 402 1555 1555 2.29
LINK OD2 ASP C 330 CA CA C 403 1555 1555 2.55
LINK OD1 ASP C 330 CA CA C 403 1555 1555 2.67
LINK OD1 ASN C 341 CA CA C 401 1555 1555 2.37
LINK O ASP C 342 CA CA C 401 1555 1555 2.63
LINK OD1 ASP C 342 CA CA C 401 1555 1555 2.29
LINK CA CA C 401 O4A NPJ C 700 1555 1555 2.52
LINK CA CA C 401 O3A NPJ C 700 1555 1555 2.52
LINK CA CA C 402 O HOH C 702 1555 1555 2.35
LINK CA CA C 403 O HOH C 774 1555 1555 2.48
LINK CA CA C 403 O HOH C 776 1555 1555 2.33
LINK CA CA C 403 O HOH C 777 1555 1555 2.59
LINK CA CA C 403 O HOH C 779 1555 1555 2.39
CISPEP 1 PHE A 234 PRO A 235 0 0.20
CISPEP 2 GLU A 321 PRO A 322 0 -0.34
CISPEP 3 PHE B 234 PRO B 235 0 0.18
CISPEP 4 GLU B 321 PRO B 322 0 -0.24
CISPEP 5 PHE C 234 PRO C 235 0 0.16
CISPEP 6 GLU C 321 PRO C 322 0 -0.23
SITE 1 AC1 6 GLU A 321 ASN A 323 GLU A 329 ASN A 341
SITE 2 AC1 6 ASP A 342 NPJ A 700
SITE 1 AC2 6 ASP A 297 GLU A 301 ASP A 324 GLU A 329
SITE 2 AC2 6 ASP A 330 HOH A 777
SITE 1 AC3 5 GLU A 301 ASP A 330 HOH A 703 HOH A 784
SITE 2 AC3 5 HOH A 788
SITE 1 AC4 6 GLU B 321 ASN B 323 GLU B 329 ASN B 341
SITE 2 AC4 6 ASP B 342 NPJ B 700
SITE 1 AC5 6 ASP B 297 GLU B 301 ASP B 324 GLU B 329
SITE 2 AC5 6 ASP B 330 HOH B 783
SITE 1 AC6 6 GLU B 301 ASP B 330 HOH B 781 HOH B 784
SITE 2 AC6 6 HOH B 787 HOH B 788
SITE 1 AC7 6 GLU C 321 ASN C 323 GLU C 329 ASN C 341
SITE 2 AC7 6 ASP C 342 NPJ C 700
SITE 1 AC8 6 ASP C 297 GLU C 301 ASP C 324 GLU C 329
SITE 2 AC8 6 ASP C 330 HOH C 702
SITE 1 AC9 6 GLU C 301 ASP C 330 HOH C 774 HOH C 776
SITE 2 AC9 6 HOH C 777 HOH C 779
SITE 1 BC1 11 GLU A 321 ASN A 323 GLU A 329 PHE A 335
SITE 2 BC1 11 THR A 336 ASN A 337 ASN A 341 ASP A 342
SITE 3 BC1 11 ARG A 343 CA A 401 HOH A 752
SITE 1 BC2 13 GLU B 321 ASN B 323 ASP B 325 GLU B 329
SITE 2 BC2 13 PHE B 335 THR B 336 ASN B 337 ASN B 341
SITE 3 BC2 13 ASP B 342 ARG B 343 CA B 401 HOH B 708
SITE 4 BC2 13 HOH B 715
SITE 1 BC3 13 GLU C 321 ASN C 323 GLU C 329 PHE C 335
SITE 2 BC3 13 THR C 336 ASN C 337 ASN C 341 ASP C 342
SITE 3 BC3 13 ARG C 343 CA C 401 HOH C 721 HOH C 735
SITE 4 BC3 13 HOH C 756
CRYST1 55.431 106.400 55.080 90.00 92.65 90.00 P 1 21 1 6
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 0.018040 0.000000 0.000835 0.00000
SCALE2 0.000000 0.009398 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018175 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
